RGS3_HUMAN
ID RGS3_HUMAN Reviewed; 1198 AA.
AC P49796; A6NHA0; A8K0V1; B3KUB2; Q5VXB8; Q5VXC1; Q5VZ05; Q5VZ06; Q6ZRM5;
AC Q8IUQ1; Q8NC47; Q8NFN4; Q8NFN5; Q8NFN6; Q8TD59; Q8TD68; Q8WV02; Q8WXA0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Regulator of G-protein signaling 3;
DE Short=RGP3;
DE Short=RGS3;
GN Name=RGS3;
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 1), AND FUNCTION.
RX PubMed=8602223; DOI=10.1038/379742a0;
RA Druey K.M., Blumer K.J., Kang V.H., Kehrl J.H.;
RT "Inhibition of G-protein-mediated MAP kinase activation by a new mammalian
RT gene family.";
RL Nature 379:742-746(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 8), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 105-1198 (ISOFORM 1).
RX PubMed=12036301; DOI=10.1006/geno.2002.6773;
RA Kehrl J.H., Srikumar D., Harrison K., Wilson G.L., Shi C.S.;
RT "Additional 5' exons in the RGS3 locus generate multiple mRNA transcripts,
RT one of which accounts for the origin of human PDZ-RGS3.";
RL Genomics 79:860-868(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 5 AND 9).
RC TISSUE=Amygdala, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 4).
RA Chatterjee T.K., Fisher R.A.;
RT "Human PDZ-RGS3.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, INTERACTION WITH GNA11 AND GNA13, AND SUBCELLULAR LOCATION.
RX PubMed=9858594; DOI=10.1128/mcb.19.1.714;
RA Dulin N.O., Sorokin A., Reed E., Elliott S., Kehrl J.H., Dunn M.J.;
RT "RGS3 inhibits G protein-mediated signaling via translocation to the
RT membrane and binding to Galpha11.";
RL Mol. Cell. Biol. 19:714-723(1999).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10749886; DOI=10.1074/jbc.m910079199;
RA Dulin N.O., Pratt P., Tiruppathi C., Niu J., Voyno-Yasenetskaya T.,
RA Dunn M.J.;
RT "Regulator of G protein signaling RGS3T is localized to the nucleus and
RT induces apoptosis.";
RL J. Biol. Chem. 275:21317-21323(2000).
RN [11]
RP FUNCTION, INTERACTION WITH HETERODIMERIC GNB1-GNG2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11294858; DOI=10.1074/jbc.m100089200;
RA Shi C.-S., Lee S.B., Sinnarajah S., Dessauer C.W., Rhee S.G., Kehrl J.H.;
RT "Regulator of G-protein signaling 3 (RGS3) inhibits G-beta1/gamma2-induced
RT inositol phosphate production, mitogen-activated protein kinase activation,
RT and Akt activation.";
RL J. Biol. Chem. 276:24293-24300(2001).
RN [12]
RP ISGYLATION.
RX PubMed=16884686; DOI=10.1016/j.bbrc.2006.07.076;
RA Takeuchi T., Inoue S., Yokosawa H.;
RT "Identification and Herc5-mediated ISGylation of novel target proteins.";
RL Biochem. Biophys. Res. Commun. 348:473-477(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-943, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-448, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Down-regulates signaling from heterotrimeric G-proteins by
CC increasing the GTPase activity of the alpha subunits, thereby driving
CC them into their inactive GDP-bound form. Down-regulates G-protein-
CC mediated release of inositol phosphates and activation of MAP kinases.
CC {ECO:0000269|PubMed:10749886, ECO:0000269|PubMed:11294858,
CC ECO:0000269|PubMed:8602223, ECO:0000269|PubMed:9858594}.
CC -!- SUBUNIT: Binds EFNB1 and EFNB2 (By similarity). Binds the GNB1-GNG2
CC heterodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P49796; Q96AP0: ACD; NbExp=2; IntAct=EBI-2107809, EBI-717666;
CC P49796; O15162: PLSCR1; NbExp=3; IntAct=EBI-2107809, EBI-740019;
CC P49796-4; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12006708, EBI-3867333;
CC P49796-8; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-10211517, EBI-739467;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9858594}. Nucleus
CC {ECO:0000269|PubMed:10749886}. Cell membrane
CC {ECO:0000269|PubMed:9858594}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9858594}. Note=Long isoforms are cytoplasmic and
CC associated with the plasma membrane (PubMed:9858594). Short isoforms
CC are nuclear (PubMed:10749886).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=3;
CC IsoId=P49796-3; Sequence=Displayed;
CC Name=1;
CC IsoId=P49796-1; Sequence=VSP_013958;
CC Name=2; Synonyms=RGS3T;
CC IsoId=P49796-2; Sequence=VSP_005662;
CC Name=4; Synonyms=1;
CC IsoId=P49796-4; Sequence=VSP_013959, VSP_013963;
CC Name=5;
CC IsoId=P49796-5; Sequence=VSP_013961, VSP_013962, VSP_013964,
CC VSP_013965;
CC Name=6; Synonyms=C2PA-RGS3;
CC IsoId=P49796-6; Sequence=VSP_013960;
CC Name=7;
CC IsoId=P49796-7; Sequence=VSP_047029;
CC Name=8; Synonyms=RGS3S;
CC IsoId=P49796-8; Sequence=VSP_047029, VSP_053533;
CC Name=9;
CC IsoId=P49796-9; Sequence=VSP_013959, VSP_013963, VSP_054690;
CC -!- PTM: Phosphorylated by cyclic GMP-dependent protein kinase.
CC {ECO:0000250}.
CC -!- PTM: ISGylated. {ECO:0000305|PubMed:16884686}.
CC -!- MISCELLANEOUS: [Isoform 2]: Nuclear. {ECO:0000269|PubMed:10749886}.
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; U27655; AAC50394.1; -; mRNA.
DR EMBL; AF490838; AAM33253.1; -; mRNA.
DR EMBL; AF490839; AAM33254.1; -; mRNA.
DR EMBL; AF490840; AAM33255.1; -; mRNA.
DR EMBL; AK074977; BAC11328.1; -; mRNA.
DR EMBL; AK096840; BAG53374.1; -; mRNA.
DR EMBL; AK128127; BAC87285.1; -; mRNA.
DR EMBL; AK289666; BAF82355.1; -; mRNA.
DR EMBL; AF493927; AAM12641.1; -; mRNA.
DR EMBL; AF493941; AAM12655.1; -; mRNA.
DR EMBL; AY585192; AAT79495.1; -; mRNA.
DR EMBL; AF463495; AAL68829.1; -; Genomic_DNA.
DR EMBL; AL137066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87388.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87391.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87393.1; -; Genomic_DNA.
DR EMBL; BC019039; AAH19039.3; -; mRNA.
DR EMBL; BC042555; AAH42555.1; -; mRNA.
DR CCDS; CCDS35113.1; -. [P49796-5]
DR CCDS; CCDS43869.1; -. [P49796-6]
DR CCDS; CCDS65111.1; -. [P49796-9]
DR CCDS; CCDS6797.1; -. [P49796-4]
DR CCDS; CCDS6798.1; -. [P49796-1]
DR PIR; S78089; S78089.
DR RefSeq; NP_001263189.1; NM_001276260.1. [P49796-1]
DR RefSeq; NP_001263190.1; NM_001276261.1. [P49796-9]
DR RefSeq; NP_001263191.1; NM_001276262.1.
DR RefSeq; NP_001269851.1; NM_001282922.1. [P49796-1]
DR RefSeq; NP_001269852.1; NM_001282923.1.
DR RefSeq; NP_060260.3; NM_017790.4. [P49796-5]
DR RefSeq; NP_570613.2; NM_130795.3. [P49796-4]
DR RefSeq; NP_602299.1; NM_134427.2.
DR RefSeq; NP_652759.3; NM_144488.5. [P49796-3]
DR RefSeq; NP_652760.2; NM_144489.3. [P49796-7]
DR RefSeq; XP_006717282.1; XM_006717219.2.
DR RefSeq; XP_006717289.1; XM_006717226.2.
DR RefSeq; XP_006717293.1; XM_006717230.3.
DR RefSeq; XP_011517198.1; XM_011518896.1.
DR RefSeq; XP_011517199.1; XM_011518897.2.
DR RefSeq; XP_011517200.1; XM_011518898.1.
DR RefSeq; XP_011517202.1; XM_011518900.1.
DR RefSeq; XP_011517203.1; XM_011518901.1.
DR RefSeq; XP_016870494.1; XM_017015005.1.
DR RefSeq; XP_016870495.1; XM_017015006.1.
DR PDB; 2F5Y; X-ray; 2.39 A; A/B=300-384.
DR PDB; 2OJ4; X-ray; 2.30 A; A=1064-1190.
DR PDB; 3FBK; X-ray; 2.00 A; A/B=134-276.
DR PDBsum; 2F5Y; -.
DR PDBsum; 2OJ4; -.
DR PDBsum; 3FBK; -.
DR AlphaFoldDB; P49796; -.
DR BMRB; P49796; -.
DR SMR; P49796; -.
DR BioGRID; 111930; 61.
DR IntAct; P49796; 56.
DR MINT; P49796; -.
DR STRING; 9606.ENSP00000363255; -.
DR iPTMnet; P49796; -.
DR PhosphoSitePlus; P49796; -.
DR SwissPalm; P49796; -.
DR BioMuta; RGS3; -.
DR DMDM; 67477383; -.
DR EPD; P49796; -.
DR jPOST; P49796; -.
DR MassIVE; P49796; -.
DR MaxQB; P49796; -.
DR PaxDb; P49796; -.
DR PeptideAtlas; P49796; -.
DR PRIDE; P49796; -.
DR ProteomicsDB; 3705; -.
DR ProteomicsDB; 56123; -. [P49796-3]
DR ProteomicsDB; 56124; -. [P49796-1]
DR ProteomicsDB; 56125; -. [P49796-2]
DR ProteomicsDB; 56126; -. [P49796-4]
DR ProteomicsDB; 56127; -. [P49796-5]
DR ProteomicsDB; 56128; -. [P49796-6]
DR ProteomicsDB; 65662; -.
DR Antibodypedia; 15339; 176 antibodies from 30 providers.
DR DNASU; 5998; -.
DR Ensembl; ENST00000317613.10; ENSP00000312844.6; ENSG00000138835.22. [P49796-5]
DR Ensembl; ENST00000343817.9; ENSP00000340284.5; ENSG00000138835.22. [P49796-4]
DR Ensembl; ENST00000350696.9; ENSP00000259406.7; ENSG00000138835.22. [P49796-3]
DR Ensembl; ENST00000374134.7; ENSP00000363249.3; ENSG00000138835.22. [P49796-1]
DR Ensembl; ENST00000374140.6; ENSP00000363255.2; ENSG00000138835.22. [P49796-3]
DR Ensembl; ENST00000394646.7; ENSP00000378141.3; ENSG00000138835.22. [P49796-9]
DR Ensembl; ENST00000462143.5; ENSP00000420356.1; ENSG00000138835.22. [P49796-1]
DR Ensembl; ENST00000462403.5; ENSP00000436168.1; ENSG00000138835.22. [P49796-7]
DR Ensembl; ENST00000613049.4; ENSP00000482612.1; ENSG00000138835.22. [P49796-7]
DR GeneID; 5998; -.
DR KEGG; hsa:5998; -.
DR UCSC; uc004bhq.5; human. [P49796-3]
DR CTD; 5998; -.
DR DisGeNET; 5998; -.
DR GeneCards; RGS3; -.
DR HGNC; HGNC:9999; RGS3.
DR HPA; ENSG00000138835; Low tissue specificity.
DR MIM; 602189; gene.
DR neXtProt; NX_P49796; -.
DR OpenTargets; ENSG00000138835; -.
DR PharmGKB; PA34374; -.
DR VEuPathDB; HostDB:ENSG00000138835; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000154416; -.
DR HOGENOM; CLU_005574_0_0_1; -.
DR InParanoid; P49796; -.
DR OMA; GHRKXAK; -.
DR OrthoDB; 201302at2759; -.
DR PhylomeDB; P49796; -.
DR TreeFam; TF351952; -.
DR PathwayCommons; P49796; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P49796; -.
DR BioGRID-ORCS; 5998; 14 hits in 1074 CRISPR screens.
DR ChiTaRS; RGS3; human.
DR EvolutionaryTrace; P49796; -.
DR GeneWiki; RGS3; -.
DR GenomeRNAi; 5998; -.
DR Pharos; P49796; Tbio.
DR PRO; PR:P49796; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P49796; protein.
DR Bgee; ENSG00000138835; Expressed in apex of heart and 192 other tissues.
DR ExpressionAtlas; P49796; baseline and differential.
DR Genevisible; P49796; HS.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
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:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd08713; RGS_RGS3; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034951; RGS_RGS3.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor; Ubl conjugation.
FT CHAIN 1..1198
FT /note="Regulator of G-protein signaling 3"
FT /id="PRO_0000204182"
FT DOMAIN 137..256
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 299..376
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1073..1198
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 669..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..777
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..906
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 448
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC04"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC04"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC04"
FT VAR_SEQ 1..1027
FT /note="MPVIPALWEVEMGRSQGQEIETILANRSHSDSTPLPNFLSGSHRPECCTCRL
FT LTASGAQDSLPFGRRLYSGPWRSCEEVCHVSVLSVLSTSCGLSLSLPIFPGWMEWLSPD
FT IALPRRDEWTQTSPARKRITHAKVQGAGQLRLSIDAQDRVLLLHIIEGKGLISKQPGTC
FT DPYVKISLIPEDSRLRHQKTQTVPDCRDPAFHEHFFFPVQEEDDQKRLLVTVWNRASQS
FT RQSGLIGCMSFGVKSLLTPDKEISGWYYLLGEHLGRTKHLKVARRRLRPLRDPLLRMPG
FT GGDTENGKKLKITIPRGKDGFGFTICCDSPVRVQAVDSGGPAERAGLQQLDTVLQLNER
FT PVEHWKCVELAHEIRSCPSEIILLVWRMVPQVKPGPDGGVLRRASCKSTHDLQSPPNKR
FT EKNCTHGVQARPEQRHSCHLVCDSSDGLLLGGWERYTEVAKRGGQHTLPALSRATAPTD
FT PNYIILAPLNPGSQLLRPVYQEDTIPEESGSPSKGKSYTGLGKKSRLMKTVQTMKGHGN
FT YQNCPVVRPHATHSSYGTYVTLAPKVLVFPVFVQPLDLCNPARTLLLSEELLLYEGRNK
FT AAEVTLFAYSDLLLFTKEDEPGRCDVLRNPLYLQSVKLQEGSSEDLKFCVLYLAEKAEC
FT LFTLEAHSQEQKKRVCWCLSENIAKQQQLAASPPDSKMFETEADEKREMALEEGKGPGA
FT EDSPPSKEPSPGQELPPGQDLPPNKDSPSGQEPAPSQEPLSSKDSATSEGSPPGPDAPP
FT SKDVPPCQEPPPAQDLSPCQDLPAGQEPLPHQDPLLTKDLPAIQESPTRDLPPCQDLPP
FT SQVSLPAKALTEDTMSSGDLLAATGDPPAAPRPAFVIPEVRLDSTYSQKAGAEQGCSGD
FT EEDAEEAEEVEEGEEGEEDEDEDTSDDNYGERSEAKRSSMIETGQGAEGGLSLRVQNSL
FT RRRTHSEGSLLQEPRGPCFASDTTLHCSDGEGAASTWGMPSPSTLKKELGRNGGSMHHL
FT SLFFTGHRKMSGADTVGDDDEASRKRKSKNL -> MVTRRPVTNSWDWLPAGAAPEAVP
FT CRHMPLSRLPLRVGQKEFFFPLPLLVPPISWLLLSESQPRLVPGSPVIRPGFQRACVAA
FT ACTVAARCPGRGVGDRSQSGASYRPICGPKVGGPTEMLRGMYLTRNGNLQRRHTMKE
FT (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12036301"
FT /id="VSP_047029"
FT VAR_SEQ 1..992
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_005662"
FT VAR_SEQ 1..679
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12036301,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:8602223,
FT ECO:0000303|Ref.5"
FT /id="VSP_013958"
FT VAR_SEQ 1..281
FT /note="Missing (in isoform 4 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:12036301,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8602223, ECO:0000303|Ref.5"
FT /id="VSP_013959"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013961"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12036301"
FT /id="VSP_013960"
FT VAR_SEQ 113..138
FT /note="ALPRRDEWTQTSPARKRITHAKVQGA -> MERSLHRVSLGSRRAHPDLSFY
FT LTTF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013962"
FT VAR_SEQ 282..299
FT /note="PLLRMPGGGDTENGKKLK -> MNRFNGLCKVCSERRYRQ (in isoform
FT 4 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:12036301,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8602223, ECO:0000303|Ref.5"
FT /id="VSP_013963"
FT VAR_SEQ 679..1004
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054690"
FT VAR_SEQ 680..714
FT /note="MFETEADEKREMALEEGKGPGAEDSPPSKEPSPGQ -> KLHPFGSLQQEMG
FT PVNSTNATQDRSFTSPGQTLIG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013964"
FT VAR_SEQ 715..1198
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013965"
FT VAR_SEQ 1198
FT /note="L -> LDYKDDDDK (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:12036301"
FT /id="VSP_053533"
FT VARIANT 129
FT /note="R -> K (in dbSNP:rs16933949)"
FT /id="VAR_051794"
FT VARIANT 809
FT /note="R -> Q (in dbSNP:rs41305473)"
FT /id="VAR_061769"
FT CONFLICT 170
FT /note="C -> W (in Ref. 2; AAM33254)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="F -> S (in Ref. 3; BAC11328)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="T -> A (in Ref. 2; AAM33254)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="A -> V (in Ref. 4; AAL68829)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="A -> V (in Ref. 2; AAM33255)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="C -> R (in Ref. 3; BAC11328)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="Missing (in Ref. 2; AAM33254)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="N -> S (in Ref. 8; AAH42555)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="Q -> H (in Ref. 2; AAM33254)"
FT /evidence="ECO:0000305"
FT CONFLICT 883..884
FT /note="EE -> KQ (in Ref. 2; AAM33254)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="K -> R (in Ref. 5; AAM12641)"
FT /evidence="ECO:0000305"
FT CONFLICT 1127
FT /note="A -> V (in Ref. 2; AAM33253)"
FT /evidence="ECO:0000305"
FT STRAND 140..161
FT /evidence="ECO:0007829|PDB:3FBK"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3FBK"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:3FBK"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:3FBK"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3FBK"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:3FBK"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:3FBK"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:3FBK"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:3FBK"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:3FBK"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3FBK"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:2F5Y"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:2F5Y"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2F5Y"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:2F5Y"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:2F5Y"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:2F5Y"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:2F5Y"
FT STRAND 365..374
FT /evidence="ECO:0007829|PDB:2F5Y"
FT HELIX 1066..1070
FT /evidence="ECO:0007829|PDB:2OJ4"
FT HELIX 1074..1078
FT /evidence="ECO:0007829|PDB:2OJ4"
FT HELIX 1081..1093
FT /evidence="ECO:0007829|PDB:2OJ4"
FT HELIX 1097..1109
FT /evidence="ECO:0007829|PDB:2OJ4"
FT HELIX 1115..1129
FT /evidence="ECO:0007829|PDB:2OJ4"
FT HELIX 1142..1150
FT /evidence="ECO:0007829|PDB:2OJ4"
FT TURN 1157..1160
FT /evidence="ECO:0007829|PDB:2OJ4"
FT HELIX 1161..1173
FT /evidence="ECO:0007829|PDB:2OJ4"
FT HELIX 1175..1181
FT /evidence="ECO:0007829|PDB:2OJ4"
FT HELIX 1183..1186
FT /evidence="ECO:0007829|PDB:2OJ4"
FT TURN 1187..1189
FT /evidence="ECO:0007829|PDB:2OJ4"
SQ SEQUENCE 1198 AA; 132336 MW; E615DA49022EFFE4 CRC64;
MPVIPALWEV EMGRSQGQEI ETILANRSHS DSTPLPNFLS GSHRPECCTC RLLTASGAQD
SLPFGRRLYS GPWRSCEEVC HVSVLSVLST SCGLSLSLPI FPGWMEWLSP DIALPRRDEW
TQTSPARKRI THAKVQGAGQ LRLSIDAQDR VLLLHIIEGK GLISKQPGTC DPYVKISLIP
EDSRLRHQKT QTVPDCRDPA FHEHFFFPVQ EEDDQKRLLV TVWNRASQSR QSGLIGCMSF
GVKSLLTPDK EISGWYYLLG EHLGRTKHLK VARRRLRPLR DPLLRMPGGG DTENGKKLKI
TIPRGKDGFG FTICCDSPVR VQAVDSGGPA ERAGLQQLDT VLQLNERPVE HWKCVELAHE
IRSCPSEIIL LVWRMVPQVK PGPDGGVLRR ASCKSTHDLQ SPPNKREKNC THGVQARPEQ
RHSCHLVCDS SDGLLLGGWE RYTEVAKRGG QHTLPALSRA TAPTDPNYII LAPLNPGSQL
LRPVYQEDTI PEESGSPSKG KSYTGLGKKS RLMKTVQTMK GHGNYQNCPV VRPHATHSSY
GTYVTLAPKV LVFPVFVQPL DLCNPARTLL LSEELLLYEG RNKAAEVTLF AYSDLLLFTK
EDEPGRCDVL RNPLYLQSVK LQEGSSEDLK FCVLYLAEKA ECLFTLEAHS QEQKKRVCWC
LSENIAKQQQ LAASPPDSKM FETEADEKRE MALEEGKGPG AEDSPPSKEP SPGQELPPGQ
DLPPNKDSPS GQEPAPSQEP LSSKDSATSE GSPPGPDAPP SKDVPPCQEP PPAQDLSPCQ
DLPAGQEPLP HQDPLLTKDL PAIQESPTRD LPPCQDLPPS QVSLPAKALT EDTMSSGDLL
AATGDPPAAP RPAFVIPEVR LDSTYSQKAG AEQGCSGDEE DAEEAEEVEE GEEGEEDEDE
DTSDDNYGER SEAKRSSMIE TGQGAEGGLS LRVQNSLRRR THSEGSLLQE PRGPCFASDT
TLHCSDGEGA ASTWGMPSPS TLKKELGRNG GSMHHLSLFF TGHRKMSGAD TVGDDDEASR
KRKSKNLAKD MKNKLGIFRR RNESPGAPPA GKADKMMKSF KPTSEEALKW GESLEKLLVH
KYGLAVFQAF LRTEFSEENL EFWLACEDFK KVKSQSKMAS KAKKIFAEYI AIQACKEVNL
DSYTREHTKD NLQSVTRGCF DLAQKRIFGL MEKDSYPRFL RSDLYLDLIN QKKMSPPL
