RGS12_HUMAN
ID RGS12_HUMAN Reviewed; 1447 AA.
AC O14924; B1AQ30; B1AQ31; B1AQ32; B7Z764; E7EMN9; O14922; O14923; O43510;
AC O75338; Q147X0; Q8WX95;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Regulator of G-protein signaling 12;
DE Short=RGS12;
GN Name=RGS12;
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] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Lung;
RX PubMed=10869340; DOI=10.1074/jbc.m000330200;
RA Chatterjee T.K., Fisher R.A.;
RT "Novel alternative splicing and nuclear localization of human RGS12 gene
RT products.";
RL J. Biol. Chem. 275:29660-29671(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=9651375; DOI=10.1074/jbc.273.28.17749;
RA Snow B.E., Hall R.A., Krumins A.M., Brothers G.M., Bouchard D.,
RA Brothers C.A., Chung S., Mangion J., Gilman A.G., Lefkowitz R.J.,
RA Siderovski D.P.;
RT "GTPase activating specificity of RGS12 and binding specificity of an
RT alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain.";
RL J. Biol. Chem. 273:17749-17755(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RA Chatterjee T.K., Fisher R.A.;
RT "Novel amino terminal variant of RGS12TS-S.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Synovium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
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 [8]
RP ALTERNATIVE SPLICING (ISOFORM 5), FUNCTION (ISOFORM 5), AND SUBCELLULAR
RP LOCATION (ISOFORM 5).
RX PubMed=12024043; DOI=10.1128/mcb.22.12.4334-4345.2002;
RA Chatterjee T.K., Fisher R.A.;
RT "RGS12TS-S localizes at nuclear matrix-associated subnuclear structures and
RT represses transcription: structural requirements for subnuclear targeting
RT and transcriptional repression.";
RL Mol. Cell. Biol. 22:4334-4345(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP INTERACTION WITH 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).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-524, 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).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-196, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
RP STRUCTURE BY NMR OF 705-852.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RGS domain from human regulator of G-protein
RT signaling 12 (RGS12).";
RL Submitted (MAR-2008) to the PDB data bank.
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. {ECO:0000250|UniProtKB:O08774}.
CC -!- FUNCTION: [Isoform 5]: Behaves as a cell cycle-dependent
CC transcriptional repressor, promoting inhibition of S-phase DNA
CC synthesis. {ECO:0000269|PubMed:12024043}.
CC -!- SUBUNIT: Interacts with GNAI1 (PubMed:18434541). Interacts with GNAI2
CC and GNAI3; the interactions are GDP-dependent (By similarity).
CC {ECO:0000250|UniProtKB:O08774, ECO:0000269|PubMed:18434541}.
CC -!- INTERACTION:
CC O14924; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-7358493, EBI-11339910;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10869340}. Cytoplasm
CC {ECO:0000250|UniProtKB:O08774}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:O08774}. Synapse {ECO:0000250|UniProtKB:O08774}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Nucleus matrix
CC {ECO:0000269|PubMed:12024043}. Note=Also localized to discrete nuclear
CC foci that are distinct from sites of RNA processing, PML nuclear
CC bodies, and PcG domains. {ECO:0000269|PubMed:12024043}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=RGS12TS-L, TS, trans-spliced;
CC IsoId=O14924-1; Sequence=Displayed;
CC Name=2; Synonyms=P, peripheral;
CC IsoId=O14924-2; Sequence=VSP_005682, VSP_005683;
CC Name=3; Synonyms=B, brain;
CC IsoId=O14924-3; Sequence=VSP_005684, VSP_005685;
CC Name=4;
CC IsoId=O14924-4; Sequence=VSP_005686, VSP_005687;
CC Name=5; Synonyms=RGS12TS-S;
CC IsoId=O14924-5; Sequence=VSP_047743, VSP_047744;
CC Name=6;
CC IsoId=O14924-6; Sequence=VSP_047741, VSP_047742, VSP_047743,
CC VSP_047744;
CC Name=7;
CC IsoId=O14924-7; Sequence=VSP_005682, VSP_005683, VSP_047743,
CC VSP_047744;
CC -!- TISSUE SPECIFICITY: Isoform 3 is brain specific.
CC -!- DOMAIN: The GoLoco domain is necessary for interaction with GNAI1,
CC GNAI2 and GNAI3. {ECO:0000250}.
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DR EMBL; AF030112; AAB84187.1; -; mRNA.
DR EMBL; AF030111; AAB84114.1; -; mRNA.
DR EMBL; AF030110; AAB84007.1; -; mRNA.
DR EMBL; AF030109; AAB84186.1; -; mRNA.
DR EMBL; AF030149; AAB96645.1; -; Genomic_DNA.
DR EMBL; AF030151; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030152; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030135; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030136; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030137; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030138; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030139; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030140; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030141; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030142; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030143; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030144; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030145; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030146; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030147; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030148; AAB96645.1; JOINED; Genomic_DNA.
DR EMBL; AF030149; AAB96646.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF030135; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030136; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030137; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030138; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030139; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030140; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030141; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030142; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030143; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030144; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030145; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030146; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030147; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030148; AAB96646.1; JOINED; Genomic_DNA.
DR EMBL; AF030149; AAB96644.1; -; Genomic_DNA.
DR EMBL; AF030134; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030135; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030136; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030137; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030138; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030139; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030140; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030141; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030142; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030143; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030144; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030145; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030146; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030147; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF030148; AAB96644.1; JOINED; Genomic_DNA.
DR EMBL; AF035152; AAC39835.1; -; mRNA.
DR EMBL; AF464737; AAL69961.1; -; mRNA.
DR EMBL; AK301510; BAH13500.1; -; mRNA.
DR EMBL; AL590235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82465.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82468.1; -; Genomic_DNA.
DR EMBL; BC118594; AAI18595.1; -; mRNA.
DR EMBL; CH471131; EAW82469.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82470.1; -; Genomic_DNA.
DR CCDS; CCDS3366.1; -. [O14924-1]
DR CCDS; CCDS3367.1; -. [O14924-4]
DR CCDS; CCDS3368.1; -. [O14924-3]
DR RefSeq; NP_002917.1; NM_002926.3. [O14924-4]
DR RefSeq; NP_937870.1; NM_198227.1. [O14924-3]
DR RefSeq; NP_937872.1; NM_198229.2. [O14924-1]
DR RefSeq; XP_006713968.1; XM_006713905.1. [O14924-1]
DR RefSeq; XP_006713969.1; XM_006713906.2. [O14924-5]
DR RefSeq; XP_006713970.1; XM_006713907.1.
DR RefSeq; XP_011511845.1; XM_011513543.2.
DR RefSeq; XP_016864018.1; XM_017008529.1. [O14924-1]
DR RefSeq; XP_016864020.1; XM_017008531.1.
DR RefSeq; XP_016864021.1; XM_017008532.1.
DR RefSeq; XP_016864022.1; XM_017008533.1.
DR PDB; 2EBZ; NMR; -; A=705-852.
DR PDB; 2KV8; NMR; -; A=18-100.
DR PDBsum; 2EBZ; -.
DR PDBsum; 2KV8; -.
DR AlphaFoldDB; O14924; -.
DR SMR; O14924; -.
DR BioGRID; 111934; 41.
DR IntAct; O14924; 9.
DR MINT; O14924; -.
DR STRING; 9606.ENSP00000339381; -.
DR ChEMBL; CHEMBL1293276; -.
DR iPTMnet; O14924; -.
DR PhosphoSitePlus; O14924; -.
DR BioMuta; RGS12; -.
DR EPD; O14924; -.
DR jPOST; O14924; -.
DR MassIVE; O14924; -.
DR MaxQB; O14924; -.
DR PaxDb; O14924; -.
DR PeptideAtlas; O14924; -.
DR PRIDE; O14924; -.
DR ProteomicsDB; 48302; -. [O14924-1]
DR ProteomicsDB; 48303; -. [O14924-2]
DR ProteomicsDB; 48304; -. [O14924-3]
DR ProteomicsDB; 48305; -. [O14924-4]
DR ProteomicsDB; 6836; -.
DR ProteomicsDB; 74991; -.
DR TopDownProteomics; O14924-2; -. [O14924-2]
DR Antibodypedia; 22482; 98 antibodies from 21 providers.
DR DNASU; 6002; -.
DR Ensembl; ENST00000336727.8; ENSP00000338509.4; ENSG00000159788.20. [O14924-1]
DR Ensembl; ENST00000338806.4; ENSP00000342133.4; ENSG00000159788.20. [O14924-3]
DR Ensembl; ENST00000344733.9; ENSP00000339381.5; ENSG00000159788.20. [O14924-1]
DR Ensembl; ENST00000382788.7; ENSP00000372238.3; ENSG00000159788.20. [O14924-4]
DR GeneID; 6002; -.
DR KEGG; hsa:6002; -.
DR MANE-Select; ENST00000336727.8; ENSP00000338509.4; NM_001394154.1; NP_001381083.1.
DR UCSC; uc003ggw.4; human. [O14924-1]
DR CTD; 6002; -.
DR DisGeNET; 6002; -.
DR GeneCards; RGS12; -.
DR HGNC; HGNC:9994; RGS12.
DR HPA; ENSG00000159788; Low tissue specificity.
DR MIM; 602512; gene.
DR neXtProt; NX_O14924; -.
DR OpenTargets; ENSG00000159788; -.
DR PharmGKB; PA34364; -.
DR VEuPathDB; HostDB:ENSG00000159788; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000159741; -.
DR HOGENOM; CLU_002190_0_0_1; -.
DR InParanoid; O14924; -.
DR OMA; HKSEWSK; -.
DR OrthoDB; 275783at2759; -.
DR PhylomeDB; O14924; -.
DR TreeFam; TF328814; -.
DR PathwayCommons; O14924; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O14924; -.
DR BioGRID-ORCS; 6002; 11 hits in 1085 CRISPR screens.
DR ChiTaRS; RGS12; human.
DR EvolutionaryTrace; O14924; -.
DR GeneWiki; RGS12; -.
DR GenomeRNAi; 6002; -.
DR Pharos; O14924; Tbio.
DR PRO; PR:O14924; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O14924; protein.
DR Bgee; ENSG00000159788; Expressed in ganglionic eminence and 162 other tissues.
DR ExpressionAtlas; O14924; baseline and differential.
DR Genevisible; O14924; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0000794; C:condensed nuclear chromosome; TAS:ProtInc.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0030695; F:GTPase regulator activity; IDA:UniProtKB.
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; IBA:GO_Central.
DR CDD; cd08742; RGS_RGS12; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR037880; RGS12_RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF02188; GoLoco; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF02196; RBD; 2.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00390; GoLoco; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00455; RBD; 2.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50877; GOLOCO; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50898; RBD; 2.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW GTPase activation; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Signal transduction inhibitor;
KW Synapse; Transcription; Ubl conjugation.
FT CHAIN 1..1447
FT /note="Regulator of G-protein signaling 12"
FT /id="PRO_0000204213"
FT DOMAIN 22..98
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 228..340
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 715..832
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 962..1032
FT /note="RBD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 1034..1104
FT /note="RBD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 1187..1209
FT /note="GoLoco"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1296
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 524
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 633
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..658
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10869340,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_005682"
FT VAR_SEQ 1..647
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10869340"
FT /id="VSP_005684"
FT VAR_SEQ 1..25
FT /note="MFRAGEASKRPLPGPSPPRVRSVEV -> MKKHDFAENLPSSLLIIILVIFT
FT LS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_047741"
FT VAR_SEQ 26..627
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_047742"
FT VAR_SEQ 648..666
FT /note="RSFGRSKRFSITRSLDDLE -> MNLGKELSNETHVSNDQQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10869340"
FT /id="VSP_005685"
FT VAR_SEQ 659..666
FT /note="TRSLDDLE -> MSLSLFFQ (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10869340,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_005683"
FT VAR_SEQ 1138..1157
FT /note="GEERTLGKSNSIKIKGENGK -> SFLSLFPKLRATEQMTNVGC (in
FT isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_047743"
FT VAR_SEQ 1158..1447
FT /note="Missing (in isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_047744"
FT VAR_SEQ 1373..1376
FT /note="SGTH -> TSRF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9651375"
FT /id="VSP_005686"
FT VAR_SEQ 1377..1447
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9651375"
FT /id="VSP_005687"
FT VARIANT 225
FT /note="I -> V (in dbSNP:rs7679941)"
FT /id="VAR_034451"
FT VARIANT 277
FT /note="M -> L (in dbSNP:rs16844152)"
FT /id="VAR_034452"
FT VARIANT 1124
FT /note="N -> S (in dbSNP:rs2269497)"
FT /id="VAR_020208"
FT CONFLICT 941
FT /note="A -> V (in Ref. 7; AAI18595)"
FT /evidence="ECO:0000305"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:2KV8"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2KV8"
FT TURN 52..56
FT /evidence="ECO:0007829|PDB:2KV8"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2KV8"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:2KV8"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2KV8"
FT HELIX 711..714
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 716..721
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 723..735
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 739..753
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 759..773
FT /evidence="ECO:0007829|PDB:2EBZ"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 790..796
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 802..816
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 818..824
FT /evidence="ECO:0007829|PDB:2EBZ"
FT HELIX 826..837
FT /evidence="ECO:0007829|PDB:2EBZ"
FT TURN 844..846
FT /evidence="ECO:0007829|PDB:2EBZ"
SQ SEQUENCE 1447 AA; 156357 MW; 033CD7403DAD2725 CRC64;
MFRAGEASKR PLPGPSPPRV RSVEVARGRA GYGFTLSGQA PCVLSCVMRG SPADFVGLRA
GDQILAVNEI NVKKASHEDV VKLIGKCSGV LHMVIAEGVG RFESCSSDEE GGLYEGKGWL
KPKLDSKALG INRAERVVEE MQSGGIFNMI FENPSLCASN SEPLKLKQRS LSESAATRFD
VGHESINNPN PNMLSKEEIS KVIHDDSVFS IGLESHDDFA LDASILNVAM IVGYLGSIEL
PSTSSNLESD SLQAIRGCMR RLRAEQKIHS LVTMKIMHDC VQLSTDKAGV VAEYPAEKLA
FSAVCPDDRR FFGLVTMQTN DDGSLAQEEE GALRTSCHVF MVDPDLFNHK IHQGIARRFG
FECTADPDTN GCLEFPASSL PVLQFISVLY RDMGELIEGM RARAFLDGDA DAHQNNSTSS
NSDSGIGNFH QEEKSNRVLV VDLGGSSSRH GPGGSAWDGV GGRGAQPWGA PWTGPFCPDP
EGSPPFEAAH QTDRFWDLNK HLGPASPVEV PPASLRSSVP PSKRGTVGAG CGFNQRWLPV
HVLREWQCGH TSDQDSYTDS TDGWSSINCG TLPPPMSKIP ADRYRVEGSF AQPPLNAPKR
EWSRKAFGMQ SIFGPHRNVR KTKEDKKGSK FGRGTGLTQP SQRTSARRSF GRSKRFSITR
SLDDLESATV SDGELTGADL KDCVSNNSLS SNASLPSVQS CRRLRERRVA SWAVSFERLL
QDPVGVRYFS DFLRKEFSEE NILFWQACEY FNHVPAHDKK ELSYRAREIF SKFLCSKATT
PVNIDSQAQL ADDVLRAPHP DMFKEQQLQI FNLMKFDSYT RFLKSPLYQE CILAEVEGRA
LPDSQQVPSS PASKHSLGSD HSSVSTPKKL SGKSKSGRSL NEELGDEDSE KKRKGAFFSW
SRTRSTGRSQ KKREHGDHAD DALHANGGLC RRESQGSVSS AGSLDLSEAC RTLAPEKDKA
TKHCCIHLPD GTSCVVAVKA GFSIKDILSG LCERHGINGA AADLFLVGGD KPLVLHQDSS
ILESRDLRLE KRTLFRLDLV PINRSVGLKA KPTKPVTEVL RPVVARYGLD LSGLLVRLSG
EKEPLDLGAP ISSLDGQRVV LEEKDPSRGK ASADKQKGVP VKQNTAVNSS SRNHSATGEE
RTLGKSNSIK IKGENGKNAR DPRLSKREES IAKIGKKKYQ KINLDEAEEF FELISKAQSN
RADDQRGLLR KEDLVLPEFL RLPPGSTELT LPTPAAVAKG FSKRSATGNG RESASQPGEQ
WEPVQESSDS PSTSPGSASS PPGPPGTTPP GQKSPSGPFC TPQSPVSLAQ EGTAQIWKRQ
SQEVEAGGIQ TVEDEHVAEL TLMGEGDISS PNSTLLPPPS TPQEVPGPSR PGSGTHGSRD
LPVNRIIDVD LVTGSAPGRD GGIAGAQAGP GRSQASGGPP TSDLPGLGPV PGEPAKPKTS
AHHATFV
