RGS6_HUMAN
ID RGS6_HUMAN Reviewed; 472 AA.
AC P49758; C9JE95; F8W7W5; O75576; O75577; Q7Z4K3; Q7Z4K4; Q7Z4K5; Q7Z4K6;
AC Q8TE13; Q8TE14; Q8TE15; Q8TE16; Q8TE17; Q8TE18; Q8TE19; Q8TE20; Q8TE21;
AC Q8TE22; Q9UDS8; Q9UDT0; Q9Y245; Q9Y647;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 5.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Regulator of G-protein signaling 6;
DE Short=RGS6;
DE AltName: Full=S914;
GN Name=RGS6;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 5; 6; 7; 8; 9; 10;
RP 11; 12; 13; 14; 15 AND 16), INTERACTION WITH GNB5, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12761221; DOI=10.1074/jbc.m212687200;
RA Chatterjee T.K., Liu Z., Fisher R.A.;
RT "Human RGS6 gene structure, complex alternative splicing, and role of N
RT terminus and G protein gamma-subunit-like (GGL) domain in subcellular
RT localization of RGS6 splice variants.";
RL J. Biol. Chem. 278:30261-30271(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH GNB5, AND
RP MUTAGENESIS OF ASP-297 AND TRP-309.
RC TISSUE=Brain;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GNB5,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10521509; DOI=10.1074/jbc.274.43.31087;
RA Posner B.A., Gilman A.G., Harris B.A.;
RT "Regulators of G protein signaling 6 and 7. Purification of complexes with
RT gbeta5 and assessment of their effects on g protein-mediated signaling
RT pathways.";
RL J. Biol. Chem. 274:31087-31093(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 362-472 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7596406; DOI=10.1038/375754a0;
RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M.,
RA Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F.,
RA Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L., Nee L.,
RA Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W.,
RA da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D.,
RA Fraser P.E., Rommens J.M., St George-Hyslop P.H.;
RT "Cloning of a gene bearing missense mutations in early-onset familial
RT Alzheimer's disease.";
RL Nature 375:754-760(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 325-470, AND INTERACTION WITH
RP GNAI1.
RX PubMed=18434541; DOI=10.1073/pnas.0801508105;
RA Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
RA Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
RA Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
RT "Structural diversity in the RGS domain and its interaction with
RT heterotrimeric G protein alpha-subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
CC Inhibits signal transduction by increasing the GTPase activity of G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity
CC (PubMed:10521509). {ECO:0000269|PubMed:10521509}.
CC -!- SUBUNIT: Interacts with GNB5 (PubMed:12761221, PubMed:10339615,
CC PubMed:10521509). Interacts with RGS7BP, leading to regulate the
CC subcellular location of the heterodimer formed with GNB5 (By
CC similarity). Interacts with GNAI1 (PubMed:18434541).
CC {ECO:0000250|UniProtKB:Q9Z2H2, ECO:0000269|PubMed:10339615,
CC ECO:0000269|PubMed:10521509, ECO:0000269|PubMed:12761221,
CC ECO:0000269|PubMed:18434541}.
CC -!- INTERACTION:
CC P49758; P08238: HSP90AB1; NbExp=2; IntAct=EBI-6426927, EBI-352572;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12761221}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:10521509}. Membrane
CC {ECO:0000269|PubMed:10521509}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10521509}. Nucleus {ECO:0000269|PubMed:12761221}.
CC Cell membrane {ECO:0000250|UniProtKB:Q9Z2H2}. Note=Interaction with
CC GNB5 mediates translocation to the nucleus.
CC {ECO:0000269|PubMed:12761221}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=15;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000269|PubMed:12761221};
CC Name=1; Synonyms=RGS6Lalpha2;
CC IsoId=P49758-4; Sequence=Displayed;
CC Name=2; Synonyms=RGS6Lgamma1, RGS6Lbeta1 {ECO:0000303|PubMed:12761221};
CC IsoId=P49758-2; Sequence=VSP_035848;
CC Name=3; Synonyms=RGS6Lalpha1;
CC IsoId=P49758-3; Sequence=VSP_035847;
CC Name=5; Synonyms=RGS6Lbeta;
CC IsoId=P49758-5; Sequence=VSP_035849;
CC Name=6; Synonyms=RGS6Lbeta-GGL;
CC IsoId=P49758-6; Sequence=VSP_035846, VSP_035849;
CC Name=7; Synonyms=RGS6Lalpha2-GGL;
CC IsoId=P49758-7; Sequence=VSP_035846;
CC Name=8; Synonyms=RGS6Lgamma2, RGS6Lbeta2 {ECO:0000303|PubMed:12761221};
CC IsoId=P49758-8; Sequence=VSP_035850;
CC Name=9; Synonyms=RGS6Lalpha1-GGL;
CC IsoId=P49758-9; Sequence=VSP_035846, VSP_035847;
CC Name=10; Synonyms=RGS6Lgamma1-GGL;
CC IsoId=P49758-10; Sequence=VSP_035846, VSP_035848;
CC Name=11; Synonyms=RGS6Lgamma2-GGL;
CC IsoId=P49758-11; Sequence=VSP_035846, VSP_035850;
CC Name=12; Synonyms=RGS6Sbeta1 {ECO:0000303|PubMed:12761221};
CC IsoId=P49758-12; Sequence=VSP_035845, VSP_035848;
CC Name=13; Synonyms=RGS6Lepsilon;
CC IsoId=P49758-13; Sequence=VSP_047806;
CC Name=14; Synonyms=RGS6Ldelta;
CC IsoId=P49758-14; Sequence=VSP_047807;
CC Name=15; Synonyms=RGS6Lgamma;
CC IsoId=P49758-15; Sequence=VSP_047808;
CC Name=16; Synonyms=RGS6Leta;
CC IsoId=P49758-16; Sequence=VSP_047809;
CC -!- DOMAIN: The RGS domain interacts avidly with Galpha and mediates the
CC acceleration of Galpha-mediated GTP hydrolysis.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42001.1; Type=Frameshift; Evidence={ECO:0000305};
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; AF073920; AAC26049.2; -; mRNA.
DR EMBL; AF073921; AAC26050.1; -; mRNA.
DR EMBL; AY309097; AAP74386.1; -; mRNA.
DR EMBL; AY309098; AAP74387.1; -; mRNA.
DR EMBL; AY309099; AAP74388.1; -; mRNA.
DR EMBL; AY309100; AAP74389.1; -; mRNA.
DR EMBL; AF465727; AAM03004.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465722; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465726; AAM03004.1; JOINED; Genomic_DNA.
DR EMBL; AF465727; AAM03005.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465722; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465726; AAM03005.1; JOINED; Genomic_DNA.
DR EMBL; AF465726; AAM03006.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465722; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03006.1; JOINED; Genomic_DNA.
DR EMBL; AF465727; AAM03007.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465726; AAM03007.1; JOINED; Genomic_DNA.
DR EMBL; AF465727; AAM03008.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465726; AAM03008.1; JOINED; Genomic_DNA.
DR EMBL; AF465727; AAM03009.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465722; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03009.1; JOINED; Genomic_DNA.
DR EMBL; AF465727; AAM03010.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465722; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03010.1; JOINED; Genomic_DNA.
DR EMBL; AF465727; AAM03011.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03011.1; JOINED; Genomic_DNA.
DR EMBL; AF465727; AAM03012.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03012.1; JOINED; Genomic_DNA.
DR EMBL; AF465726; AAM03013.1; -; Genomic_DNA.
DR EMBL; AF465711; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465712; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465713; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465714; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465715; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465716; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465717; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465718; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465719; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465720; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465721; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465723; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465724; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF465725; AAM03013.1; JOINED; Genomic_DNA.
DR EMBL; AF107619; AAD34717.1; -; mRNA.
DR EMBL; AF107620; AAD34718.1; -; mRNA.
DR EMBL; AF156932; AAD40183.1; -; mRNA.
DR EMBL; AC004828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005157; AAC83180.1; -; Genomic_DNA.
DR EMBL; AC005226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005477; AAD05031.1; -; Genomic_DNA.
DR EMBL; AC005533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L40394; AAC42001.1; ALT_FRAME; mRNA.
DR CCDS; CCDS55924.1; -. [P49758-3]
DR CCDS; CCDS9808.1; -. [P49758-4]
DR RefSeq; NP_001191345.1; NM_001204416.2. [P49758-3]
DR RefSeq; NP_001191346.1; NM_001204417.2. [P49758-2]
DR RefSeq; NP_001191347.1; NM_001204418.2. [P49758-8]
DR RefSeq; NP_001191348.1; NM_001204419.2. [P49758-9]
DR RefSeq; NP_001191349.1; NM_001204420.2. [P49758-7]
DR RefSeq; NP_001191350.1; NM_001204421.2. [P49758-10]
DR RefSeq; NP_001191351.1; NM_001204422.2. [P49758-11]
DR RefSeq; NP_001191352.1; NM_001204423.1.
DR RefSeq; NP_001191353.1; NM_001204424.1. [P49758-3]
DR RefSeq; NP_004287.3; NM_004296.6. [P49758-4]
DR RefSeq; XP_016877315.1; XM_017021826.1. [P49758-13]
DR RefSeq; XP_016877318.1; XM_017021829.1.
DR RefSeq; XP_016877319.1; XM_017021830.1. [P49758-5]
DR RefSeq; XP_016877321.1; XM_017021832.1. [P49758-16]
DR RefSeq; XP_016877323.1; XM_017021834.1. [P49758-12]
DR PDB; 2ES0; X-ray; 2.10 A; A=325-470.
DR PDBsum; 2ES0; -.
DR AlphaFoldDB; P49758; -.
DR SMR; P49758; -.
DR BioGRID; 114987; 15.
DR CORUM; P49758; -.
DR IntAct; P49758; 9.
DR STRING; 9606.ENSP00000451030; -.
DR iPTMnet; P49758; -.
DR PhosphoSitePlus; P49758; -.
DR BioMuta; RGS6; -.
DR DMDM; 215274268; -.
DR MassIVE; P49758; -.
DR MaxQB; P49758; -.
DR PaxDb; P49758; -.
DR PeptideAtlas; P49758; -.
DR PRIDE; P49758; -.
DR ProteomicsDB; 56079; -. [P49758-4]
DR ProteomicsDB; 56080; -. [P49758-10]
DR ProteomicsDB; 56081; -. [P49758-11]
DR ProteomicsDB; 56082; -. [P49758-12]
DR ProteomicsDB; 56083; -. [P49758-2]
DR ProteomicsDB; 56084; -. [P49758-3]
DR ProteomicsDB; 56085; -. [P49758-5]
DR ProteomicsDB; 56086; -. [P49758-6]
DR ProteomicsDB; 56087; -. [P49758-7]
DR ProteomicsDB; 56088; -. [P49758-8]
DR ProteomicsDB; 56089; -. [P49758-9]
DR ProteomicsDB; 69197; -.
DR ProteomicsDB; 69198; -.
DR ProteomicsDB; 69199; -.
DR ProteomicsDB; 69200; -.
DR Antibodypedia; 145; 135 antibodies from 25 providers.
DR DNASU; 9628; -.
DR Ensembl; ENST00000355512.10; ENSP00000347699.6; ENSG00000182732.18. [P49758-16]
DR Ensembl; ENST00000404301.6; ENSP00000385243.2; ENSG00000182732.18. [P49758-15]
DR Ensembl; ENST00000406236.8; ENSP00000384218.4; ENSG00000182732.18. [P49758-13]
DR Ensembl; ENST00000407322.8; ENSP00000384612.4; ENSG00000182732.18. [P49758-14]
DR Ensembl; ENST00000553525.6; ENSP00000451030.1; ENSG00000182732.18. [P49758-3]
DR Ensembl; ENST00000553530.5; ENSP00000452331.1; ENSG00000182732.18. [P49758-4]
DR Ensembl; ENST00000554474.5; ENSP00000450858.1; ENSG00000182732.18. [P49758-5]
DR Ensembl; ENST00000554782.1; ENSP00000451912.1; ENSG00000182732.18. [P49758-12]
DR Ensembl; ENST00000555571.5; ENSP00000450936.1; ENSG00000182732.18. [P49758-4]
DR Ensembl; ENST00000556437.5; ENSP00000451855.1; ENSG00000182732.18. [P49758-3]
DR GeneID; 9628; -.
DR KEGG; hsa:9628; -.
DR MANE-Select; ENST00000553525.6; ENSP00000451030.1; NM_001204424.2; NP_001191353.1. [P49758-3]
DR UCSC; uc001xmy.5; human. [P49758-4]
DR CTD; 9628; -.
DR DisGeNET; 9628; -.
DR GeneCards; RGS6; -.
DR HGNC; HGNC:10002; RGS6.
DR HPA; ENSG00000182732; Tissue enhanced (brain).
DR MIM; 603894; gene.
DR neXtProt; NX_P49758; -.
DR OpenTargets; ENSG00000182732; -.
DR PharmGKB; PA34377; -.
DR VEuPathDB; HostDB:ENSG00000182732; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157159; -.
DR InParanoid; P49758; -.
DR OMA; ASHHQRG; -.
DR OrthoDB; 415625at2759; -.
DR PhylomeDB; P49758; -.
DR TreeFam; TF351956; -.
DR PathwayCommons; P49758; -.
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; P49758; -.
DR SIGNOR; P49758; -.
DR BioGRID-ORCS; 9628; 5 hits in 1064 CRISPR screens.
DR ChiTaRS; RGS6; human.
DR EvolutionaryTrace; P49758; -.
DR GeneWiki; RGS6; -.
DR GenomeRNAi; 9628; -.
DR Pharos; P49758; Tbio.
DR PRO; PR:P49758; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P49758; protein.
DR Bgee; ENSG00000182732; Expressed in cortical plate and 127 other tissues.
DR ExpressionAtlas; P49758; baseline and differential.
DR Genevisible; P49758; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR CDD; cd00068; GGL; 1.
DR CDD; cd08737; RGS_RGS6; 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; IPR037956; RGS6_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 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW GTPase activation; Membrane; Nucleus; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..472
FT /note="Regulator of G-protein signaling 6"
FT /id="PRO_0000204192"
FT DOMAIN 40..115
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 261..330
FT /note="G protein gamma"
FT DOMAIN 336..441
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_035845"
FT VAR_SEQ 285..321
FT /note="Missing (in isoform 6, isoform 7, isoform 9, isoform
FT 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_035846"
FT VAR_SEQ 456
FT /note="K -> KPESEQGRRTSLEKFTRSV (in isoform 3 and isoform
FT 9)"
FT /evidence="ECO:0000303|PubMed:10339615,
FT ECO:0000303|PubMed:12761221"
FT /id="VSP_035847"
FT VAR_SEQ 457..472
FT /note="GKSLAGKRLTGLMQSS -> PESEQGRRTSLEKFTRSVG (in isoform
FT 13)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_047806"
FT VAR_SEQ 457..472
FT /note="GKSLAGKRLTGLMQSS -> PESEQGRRTSLEKFTRSVLLF (in
FT isoform 14)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_047807"
FT VAR_SEQ 457..472
FT /note="GKSLAGKRLTGLMQSS -> PESEQGRRTSLEKFTRSVCLQLLF (in
FT isoform 15)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_047808"
FT VAR_SEQ 457..472
FT /note="GKSLAGKRLTGLMQSS -> VWLL (in isoform 16)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_047809"
FT VAR_SEQ 457..472
FT /note="GKSLAGKRLTGLMQSS -> PESEQGRRTSLEKFTRSVLYSNTPLAKRP
FT (in isoform 2, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_035848"
FT VAR_SEQ 457..472
FT /note="GKSLAGKRLTGLMQSS -> KVSKVVELP (in isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_035849"
FT VAR_SEQ 457..472
FT /note="GKSLAGKRLTGLMQSS -> LYSNTPLAKRP (in isoform 8 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:12761221"
FT /id="VSP_035850"
FT MUTAGEN 297
FT /note="D->A: Loss of interaction with GNB5."
FT /evidence="ECO:0000269|PubMed:10339615"
FT MUTAGEN 309
FT /note="W->F: Diminishes interaction with GNB5."
FT /evidence="ECO:0000269|PubMed:10339615"
FT CONFLICT 165
FT /note="R -> K (in Ref. 1; AAC26049/AAM03004/AAM03005/
FT AAM03006/AAM03007/AAM03008/AAM03009/AAM03010/AAM03011/
FT AAM03012/AAM03013)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="V -> L (in Ref. 1; AAC26049/AAM03004/AAM03005/
FT AAM03006/AAM03007/AAM03008/AAM03009/AAM03010/AAM03011/
FT AAM03012/AAM03013)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..313
FT /note="DD -> EE (in Ref. 1; AAC26049/AAM03004/AAM03005/
FT AAM03006/AAM03009/AAM03010)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="E -> D (in Ref. 1; AAC26049/AAM03004/AAM03005/
FT AAM03006/AAM03007/AAM03008/AAM03009/AAM03010/AAM03011/
FT AAM03012/AAM03013)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="L -> C (in Ref. 5; AAC42001)"
FT /evidence="ECO:0000305"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 344..356
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 404..416
FT /evidence="ECO:0007829|PDB:2ES0"
FT TURN 417..422
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 423..436
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 438..443
FT /evidence="ECO:0007829|PDB:2ES0"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:2ES0"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:2ES0"
SQ SEQUENCE 472 AA; 54423 MW; 1424518EA697CD76 CRC64;
MAQGSGDQRA VGVADPEESS PNMIVYCKIE DIITKMQDDK TGGVPIRTVK SFLSKIPSVV
TGTDIVQWLM KNLSIEDPVE AIHLGSLIAA QGYIFPISDH VLTMKDDGTF YRFQAPYFWP
SNCWEPENTD YAIYLCKRTM QNKARLELAD YEAENLARLQ RAFARKWEFI FMQAEAQVKI
DRKKDKTERK ILDSQERAFW DVHRPVPGCV NTTEMDIRKC RRLKNPQKVK KSVYGVTEES
QAQSPVHVLS QPIRKTTKED IRKQITFLNA QIDRHCLKMS KVAESLIAYT EQYVEYDPLI
TPAEPSNPWI SDDVALWDIE MSKEPSQQRV KRWGFSFDEI LKDQVGRDQF LRFLESEFSS
ENLRFWLAVQ DLKKQPLQDV AKRVEEIWQE FLAPGAPSAI NLDSHSYEIT SQNVKDGGRY
TFEDAQEHIY KLMKSDSYAR FLRSNAYQDL LLAKKKGKSL AGKRLTGLMQ SS
