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 15-JUN-2010, entry version 101. DE RecName: Full=Regulator of G-protein signaling 1; DE Short=RGS1; DE AltName: Full=Early response protein 1R20; DE AltName: Full=B-cell activation protein BL34; 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). RC TISSUE=B-cell; RX MEDLINE=93232596; 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 MEDLINE=94060109; 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. CC -!- FUNCTION: Inhibits signal transduction by increasing the GTPase CC activity of G protein alpha subunits thereby driving them into CC their inactive GDP-bound form. This protein may be involved in the CC regulation of B-cell activation and proliferation. 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: B-cell specific. Expression is relatively low CC in B-cells and chronic lymphocytic leukemia B-cells; however, in CC other types of malignant B-cell such as non-Hodgkin lymphoma and CC hairy cell leukemia, expression is constitutively high. CC -!- INDUCTION: In response to several B-cell activation signals. CC -!- PTM: Could be phosphorylated. Might be functionally regulated by CC protein kinase(s). CC -!- SIMILARITY: Contains 1 RGS domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAB26289.1; Type=Erroneous initiation; CC Sequence=AAH15510.1; Type=Erroneous initiation; CC Sequence=BAG37976.1; Type=Erroneous initiation; CC Sequence=BAG64242.1; Type=Erroneous initiation; CC Sequence=CAA51826.1; Type=Erroneous initiation; 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; CAC19805.1; -; 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 IPI; IPI00873849; -. DR IPI; IPI00908845; -. DR PIR; S43436; S43436. DR RefSeq; NP_002913.3; -. 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 IntAct; Q08116; 4. DR MINT; MINT-1367963; -. DR STRING; Q08116; -. DR Ensembl; ENST00000367459; ENSP00000356429; ENSG00000090104; Homo sapiens. DR GeneID; 5996; -. DR KEGG; hsa:5996; -. DR UCSC; uc001gsi.1; human. DR CTD; 5996; -. DR GeneCards; GC01P190811; -. DR H-InvDB; HIX0001431; -. DR HGNC; HGNC:9991; RGS1. DR MIM; 600323; gene. DR PharmGKB; PA34361; -. DR eggNOG; prNOG15027; -. DR HOGENOM; HBG713967; -. DR HOVERGEN; HBG013233; -. DR InParanoid; Q08116; -. DR OMA; CKAEKIY; -. DR OrthoDB; EOG9GQSQH; -. DR NextBio; 23367; -. DR ArrayExpress; Q08116; -. DR Bgee; Q08116; -. DR CleanEx; HS_RGS1; -. DR Genevestigator; Q08116; -. DR GermOnline; ENSG00000090104; Homo sapiens. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0005516; F:calmodulin binding; TAS:ProtInc. DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0007193; P:inhibition of adenylate cyclase activity by...; TAS:ProtInc. DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR InterPro; IPR000342; Regulat_G_prot_signal. DR InterPro; IPR016137; Regulat_G_prot_signal_superfam. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR01301; RGSPROTEIN. DR SMART; SM00315; RGS; 1. DR SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1. DR PROSITE; PS50132; RGS; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein; KW Signal transduction inhibitor. FT CHAIN 1 209 Regulator of G-protein signaling 1. FT /FTId=PRO_0000204175. FT DOMAIN 85 200 RGS. FT MOD_RES 32 32 Phosphoserine; by CK2 (Potential). FT MOD_RES 67 67 Phosphoserine; by PKC (Potential). FT MOD_RES 75 75 Phosphoserine; by CK2 (Potential). FT MOD_RES 159 159 Phosphothreonine; by PKC (Potential). FT MOD_RES 169 169 Phosphothreonine; by CK2 (Potential). FT MOD_RES 180 180 Phosphothreonine; by CK2 (Potential). FT MOD_RES 207 207 Phosphoserine; by PKC (Potential). FT VAR_SEQ 149 209 INIDFRTRESTAKKIKAPTPTCFDEAQKVIYTLMEKDSYPR FT FLKSDIYLNLLNDLQANSLK -> VSIKLIIISFSIKDPIC FT RNNI (in isoform 2). FT /FTId=VSP_036422. FT CONFLICT 177 177 V -> A (in Ref. 1; BAG37976). FT CONFLICT 194 194 D -> H (in Ref. 5; CAA51826). FT STRAND 72 75 FT HELIX 76 81 FT TURN 82 84 FT HELIX 86 91 FT HELIX 93 105 FT HELIX 110 122 FT HELIX 126 128 FT HELIX 129 140 FT HELIX 153 163 FT TURN 168 171 FT HELIX 172 184 FT HELIX 186 191 FT HELIX 194 202 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 //