ID RGS1_HUMAN STANDARD; PRT; 196 AA. AC Q08116; Q07918; Q9H1W2; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Regulator of G-protein signaling 1 (RGS1) (Early response protein DE 1R20) (B-cell activation protein BL34). GN RGS1 OR 1R20 OR BL34. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=B-cell; RX MEDLINE=94060109; PubMed=8241276; 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 RT chromosome band 1q31 and encodes an alpha helical basic RT phosphoprotein."; RL Biochim. Biophys. Acta 1216:314-316(1993). RN [2] RP SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RA Skuce C.; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC TISSUE=Skin; RA Strausberg R.; RL Submitted (OCT-2001) 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 -!- 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; -. DR EMBL; S59049; AAB26289.1; -. DR EMBL; AF493925; AAM12639.1; -. DR EMBL; AL136987; CAC19805.1; ALT_INIT. DR EMBL; BC015510; AAH15510.1; -. DR PIR; S34157; S34157. DR PIR; S43436; S43436. DR HSSP; P49799; 1AGR. DR Genew; HGNC:9991; RGS1. DR MIM; 600323; -. DR InterPro; IPR000342; Regl_Gprotein. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR01301; RGSPROTEIN. DR ProDom; PD001580; Reg_of_prG; 1. DR SMART; SM00315; RGS; 1. DR PROSITE; PS50132; RGS; 1. KW Signal transduction inhibitor; B-cell activation; Phosphorylation. FT DOMAIN 72 187 RGS. FT MOD_RES 19 19 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 54 54 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 62 62 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 146 146 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT MOD_RES 156 156 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 167 167 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 194 194 PHOSPHORYLATION (BY PKC) (POTENTIAL). FT CONFLICT 181 181 D -> H (IN REF. 1). 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 //