ID RGS1_HUMAN Reviewed; 196 AA. AC Q08116; Q07918; Q9H1W2; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 12-JUN-2007, entry version 70. DE Regulator of G-protein signaling 1 (RGS1) (Early response protein DE 1R20) (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 [MRNA]. 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 [2] RP NUCLEOTIDE SEQUENCE. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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). 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 -!- 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's 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 --------------------------------------------------------------------------- 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; X73427; CAA51826.1; -; mRNA. DR EMBL; S59049; AAB26289.1; -; mRNA. DR EMBL; AF493925; AAM12639.1; -; mRNA. DR EMBL; BT006668; AAP35314.1; -; mRNA. DR EMBL; AL136987; CAC19805.1; ALT_INIT; Genomic_DNA. DR EMBL; BC015510; AAH15510.1; -; mRNA. DR PIR; S43436; S43436. DR UniGene; Hs.75256; -. DR PDB; 2BV1; X-ray; A/B=50-192. DR Ensembl; ENSG00000090104; Homo sapiens. DR KEGG; hsa:5996; -. DR H-InvDB; HIX0001431; -. DR HGNC; HGNC:9991; RGS1. DR MIM; 600323; gene. DR ArrayExpress; Q08116; -. DR GermOnline; ENSG00000090104; Homo sapiens. DR RZPD-ProtExp; G0183; -. DR RZPD-ProtExp; IOH10963; -. 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:0007193; P:G-protein signaling, adenylate cyclase inhi...; TAS:ProtInc. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR InterPro; IPR000342; RGS. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR01301; RGSPROTEIN. DR ProDom; PD001580; Regl_Gprotein; 1. DR SMART; SM00315; RGS; 1. DR PROSITE; PS50132; RGS; 1. KW 3D-structure; Phosphorylation; Signal transduction inhibitor. FT CHAIN 1 196 Regulator of G-protein signaling 1. FT /FTId=PRO_0000204175. FT DOMAIN 72 187 RGS. FT MOD_RES 19 19 Phosphoserine; by CK2 (Potential). FT MOD_RES 54 54 Phosphoserine; by PKC (Potential). FT MOD_RES 62 62 Phosphoserine; by CK2 (Potential). FT MOD_RES 146 146 Phosphothreonine; by PKC (Potential). FT MOD_RES 156 156 Phosphothreonine; by CK2 (Potential). FT MOD_RES 167 167 Phosphothreonine; by CK2 (Potential). FT MOD_RES 194 194 Phosphoserine; by PKC (Potential). FT CONFLICT 181 181 D -> H (in Ref. 1). FT HELIX 63 68 FT TURN 69 71 FT HELIX 73 78 FT HELIX 80 92 FT HELIX 97 109 FT HELIX 113 115 FT HELIX 116 127 FT HELIX 140 150 FT TURN 155 158 FT HELIX 159 171 FT HELIX 173 178 FT HELIX 181 189 SQ SEQUENCE 196 AA; 22475 MW; 6C00CEFCC458A6C4 CRC64; MPGMFFSANP KELKGTTHSL LDDKMQKRRP KTFGMDMKAY LRSMIPHLES GMKSSKSKDV LSAAEVMQWS QSLEKLLANQ TGQNVFGSFL KSEFSEENIE FWLACEDYKK TESDLLPCKA EEIYKAFVHS DAAKQINIDF RTRESTAKKI KAPTPTCFDE AQKVIYTLME KDSYPRFLKS DIYLNLLNDL QANSLK //