ID RGS1_HUMAN Reviewed; 209 AA. AC Q08116; B2RDM9; B4DZY0; Q07918; Q9H1W2; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 3. DT 28-FEB-2018, entry version 164. DE RecName: Full=Regulator of G-protein signaling 1; DE Short=RGS1; DE AltName: Full=B-cell activation protein BL34 {ECO:0000303|PubMed:8473738}; DE AltName: Full=Early response protein 1R20; GN Name=RGS1; Synonyms=1R20, BL34, IER1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Skeletal muscle, and Thymus; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-209 (ISOFORM 1). RC TISSUE=Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-209 (ISOFORM 1), TISSUE SPECIFICITY, RP AND INDUCTION. RC TISSUE=B-cell; RX PubMed=8473738; RA Hong J.X., Wilson G.L., Fox C.H., Kehrl J.H.; RT "Isolation and characterization of a novel B cell activation gene."; RL J. Immunol. 150:3895-3904(1993). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-209 (ISOFORM 1). RC TISSUE=B-cell; RX PubMed=8241276; DOI=10.1016/0167-4781(93)90163-8; RA Newton J.S., Deed R.W., Mitchell E.L.D., Murphy J.J., Norton J.D.; RT "A B cell specific immediate early human gene is located on chromosome RT band 1q31 and encodes an alpha helical basic phosphoprotein."; RL Biochim. Biophys. Acta 1216:314-316(1993). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-209 (ISOFORM 1). RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-209 (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=10480894; DOI=10.1074/jbc.274.38.26860; RA Denecke B., Meyerdierks A., Boettger E.C.; RT "RGS1 is expressed in monocytes and acts as a GTPase-activating RT protein for G-protein-coupled chemoattractant receptors."; RL J. Biol. Chem. 274:26860-26868(1999). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 63-205 IN COMPLEX WITH RP GNAI1, INTERACTION WITH GNAI1 AND GNAQ, AND FUNCTION. 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 including signaling downstream of the N-formylpeptide CC chemoattractant receptors and leukotriene receptors CC (PubMed:10480894). Inhibits B cell chemotaxis toward CXCL12 (By CC similarity). Inhibits signal transduction by increasing the GTPase CC activity of G protein alpha subunits thereby driving them into CC their inactive GDP-bound form (PubMed:10480894, PubMed:18434541). CC {ECO:0000250|UniProtKB:Q9JL25, ECO:0000269|PubMed:10480894, CC ECO:0000269|PubMed:18434541}. CC -!- SUBUNIT: Interacts with GNAI1 and GNAQ. CC {ECO:0000269|PubMed:18434541}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10480894}; CC Peripheral membrane protein {ECO:0000269|PubMed:10480894}; CC Cytoplasmic side {ECO:0000269|PubMed:10480894}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:10480894}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q08116-1; Sequence=Displayed; CC Name=2; CC IsoId=Q08116-2; Sequence=VSP_036422; CC -!- TISSUE SPECIFICITY: Detected in peripheral blood monocytes CC (PubMed:10480894). Expression is relatively low in B-cells and CC chronic lymphocytic leukemia B-cells; however, in other types of CC malignant B-cell such as non-Hodgkin lymphoma and hairy cell CC leukemia, expression is constitutively high (PubMed:8473738). CC {ECO:0000269|PubMed:10480894, ECO:0000269|PubMed:8473738}. CC -!- INDUCTION: In response to several B-cell activation signals. CC {ECO:0000269|PubMed:8473738}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB26289.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH15510.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAG37976.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAG64242.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA51826.1; Type=Erroneous initiation; 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; AK303138; BAG64242.1; ALT_INIT; mRNA. DR EMBL; AK315607; BAG37976.1; ALT_INIT; mRNA. DR EMBL; AL136987; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015510; AAH15510.1; ALT_INIT; mRNA. DR EMBL; S59049; AAB26289.1; ALT_INIT; mRNA. DR EMBL; X73427; CAA51826.1; ALT_INIT; mRNA. DR EMBL; AF493925; AAM12639.1; -; mRNA. DR EMBL; BT006668; AAP35314.1; -; mRNA. DR CCDS; CCDS1375.2; -. [Q08116-1] DR PIR; S43436; S43436. DR RefSeq; NP_002913.3; NM_002922.3. [Q08116-1] DR UniGene; Hs.75256; -. DR PDB; 2BV1; X-ray; 2.00 A; A/B=63-205. DR PDB; 2GTP; X-ray; 2.55 A; C/D=63-205. DR PDBsum; 2BV1; -. DR PDBsum; 2GTP; -. DR ProteinModelPortal; Q08116; -. DR SMR; Q08116; -. DR BioGrid; 111928; 7. DR DIP; DIP-59091N; -. DR IntAct; Q08116; 6. DR STRING; 9606.ENSP00000356429; -. DR iPTMnet; Q08116; -. DR PhosphoSitePlus; Q08116; -. DR BioMuta; RGS1; -. DR DMDM; 229470360; -. DR PaxDb; Q08116; -. DR PeptideAtlas; Q08116; -. DR PRIDE; Q08116; -. DR DNASU; 5996; -. DR Ensembl; ENST00000367459; ENSP00000356429; ENSG00000090104. [Q08116-1] DR Ensembl; ENST00000469578; ENSP00000464323; ENSG00000090104. [Q08116-2] DR GeneID; 5996; -. DR KEGG; hsa:5996; -. DR UCSC; uc001gsi.2; human. [Q08116-1] DR CTD; 5996; -. DR DisGeNET; 5996; -. DR EuPathDB; HostDB:ENSG00000090104.11; -. DR GeneCards; RGS1; -. DR H-InvDB; HIX0001431; -. DR HGNC; HGNC:9991; RGS1. DR MIM; 600323; gene. DR neXtProt; NX_Q08116; -. DR OpenTargets; ENSG00000090104; -. DR PharmGKB; PA34361; -. DR eggNOG; KOG3589; Eukaryota. DR eggNOG; ENOG410YMJD; LUCA. DR GeneTree; ENSGT00760000118903; -. DR HOGENOM; HOG000233512; -. DR HOVERGEN; HBG013233; -. DR InParanoid; Q08116; -. DR KO; K16449; -. DR OMA; KIYKAFV; -. DR OrthoDB; EOG091G0BDG; -. DR PhylomeDB; Q08116; -. DR TreeFam; TF315837; -. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR ChiTaRS; RGS1; human. DR EvolutionaryTrace; Q08116; -. DR GeneWiki; RGS1; -. DR GenomeRNAi; 5996; -. DR PRO; PR:Q08116; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000090104; -. DR CleanEx; HS_RGS1; -. DR ExpressionAtlas; Q08116; baseline and differential. DR Genevisible; Q08116; HS. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0005516; F:calmodulin binding; TAS:ProtInc. DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0061737; P:leukotriene signaling pathway; IDA:UniProtKB. 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 protein signaling pathway; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB. DR Gene3D; 1.10.196.10; -; 2. DR InterPro; IPR016137; RGS. DR InterPro; IPR030409; RGS1. DR InterPro; IPR036305; RGS_sf. DR InterPro; IPR024066; RGS_subdom1/3. DR PANTHER; PTHR10845:SF34; PTHR10845:SF34; 1. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR01301; RGSPROTEIN. DR SMART; SM00315; RGS; 1. DR SUPFAM; SSF48097; SSF48097; 1. DR PROSITE; PS50132; RGS; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome; KW Cytoplasm; GTPase activation; Membrane; Reference proteome; KW Signal transduction inhibitor. FT CHAIN 1 209 Regulator of G-protein signaling 1. FT /FTId=PRO_0000204175. FT DOMAIN 85 200 RGS. {ECO:0000255|PROSITE- FT ProRule:PRU00171}. FT VAR_SEQ 149 209 INIDFRTRESTAKKIKAPTPTCFDEAQKVIYTLMEKDSYPR FT FLKSDIYLNLLNDLQANSLK -> VSIKLIIISFSIKDPIC FT RNNI (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_036422. FT CONFLICT 177 177 V -> A (in Ref. 1; BAG37976). FT {ECO:0000305}. FT CONFLICT 194 194 D -> H (in Ref. 5; CAA51826). FT {ECO:0000305}. FT STRAND 72 75 {ECO:0000244|PDB:2BV1}. FT HELIX 76 81 {ECO:0000244|PDB:2BV1}. FT TURN 82 84 {ECO:0000244|PDB:2BV1}. FT HELIX 86 91 {ECO:0000244|PDB:2BV1}. FT HELIX 93 105 {ECO:0000244|PDB:2BV1}. FT HELIX 110 122 {ECO:0000244|PDB:2BV1}. FT HELIX 126 128 {ECO:0000244|PDB:2BV1}. FT HELIX 129 140 {ECO:0000244|PDB:2BV1}. FT HELIX 153 163 {ECO:0000244|PDB:2BV1}. FT TURN 168 171 {ECO:0000244|PDB:2BV1}. FT HELIX 172 184 {ECO:0000244|PDB:2BV1}. FT HELIX 186 191 {ECO:0000244|PDB:2BV1}. FT HELIX 194 202 {ECO:0000244|PDB:2BV1}. SQ SEQUENCE 209 AA; 23858 MW; D8D7D8E80819496A CRC64; MRAAAISTPK LDKMPGMFFS ANPKELKGTT HSLLDDKMQK RRPKTFGMDM KAYLRSMIPH LESGMKSSKS KDVLSAAEVM QWSQSLEKLL ANQTGQNVFG SFLKSEFSEE NIEFWLACED YKKTESDLLP CKAEEIYKAF VHSDAAKQIN IDFRTRESTA KKIKAPTPTC FDEAQKVIYT LMEKDSYPRF LKSDIYLNLL NDLQANSLK //