ID   RGS13_HUMAN             Reviewed;         159 AA.
AC   O14921; Q6PGR2; Q8TD63; Q9BX45;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Regulator of G-protein signaling 13;
DE            Short=RGS13;
GN   Name=RGS13;
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].
RC   TISSUE=Lung;
RA   Chatterjee T.K., Fisher R.A.;
RT   "Molecular cloning of human RGS13 cDNA.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-150.
RC   TISSUE=Brain;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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 vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) 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., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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=Lymph;
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).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into their
CC       inactive GDP-bound form. Binds to both G(i)-alpha and G(q)-alpha (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       O14921; Q9BWW8: APOL6; NbExp=3; IntAct=EBI-17843660, EBI-11574440;
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DR   EMBL; AF030107; AAB84000.1; -; mRNA.
DR   EMBL; AF493935; AAM12649.1; -; mRNA.
DR   EMBL; AY562947; AAS66360.1; -; mRNA.
DR   EMBL; BT006929; AAP35575.1; -; mRNA.
DR   EMBL; CR536532; CAG38769.1; -; mRNA.
DR   EMBL; AL136454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL596119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016667; AAH16667.1; -; mRNA.
DR   EMBL; BC056866; AAH56866.2; -; mRNA.
DR   CCDS; CCDS1376.1; -.
DR   RefSeq; NP_002918.1; NM_002927.4.
DR   RefSeq; NP_658912.1; NM_144766.2.
DR   AlphaFoldDB; O14921; -.
DR   SMR; O14921; -.
DR   BioGRID; 111935; 28.
DR   IntAct; O14921; 8.
DR   MINT; O14921; -.
DR   STRING; 9606.ENSP00000442837; -.
DR   iPTMnet; O14921; -.
DR   PhosphoSitePlus; O14921; -.
DR   BioMuta; RGS13; -.
DR   MassIVE; O14921; -.
DR   MaxQB; O14921; -.
DR   PaxDb; 9606-ENSP00000442837; -.
DR   PeptideAtlas; O14921; -.
DR   ProteomicsDB; 48301; -.
DR   Antibodypedia; 20618; 274 antibodies from 32 providers.
DR   DNASU; 6003; -.
DR   Ensembl; ENST00000391995.7; ENSP00000375853.2; ENSG00000127074.15.
DR   Ensembl; ENST00000543215.5; ENSP00000442837.1; ENSG00000127074.15.
DR   GeneID; 6003; -.
DR   KEGG; hsa:6003; -.
DR   MANE-Select; ENST00000391995.7; ENSP00000375853.2; NM_002927.5; NP_002918.1.
DR   UCSC; uc001gsj.4; human.
DR   AGR; HGNC:9995; -.
DR   CTD; 6003; -.
DR   DisGeNET; 6003; -.
DR   GeneCards; RGS13; -.
DR   HGNC; HGNC:9995; RGS13.
DR   HPA; ENSG00000127074; Tissue enriched (lymphoid).
DR   MIM; 607190; gene.
DR   neXtProt; NX_O14921; -.
DR   OpenTargets; ENSG00000127074; -.
DR   PharmGKB; PA34365; -.
DR   VEuPathDB; HostDB:ENSG00000127074; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000158520; -.
DR   HOGENOM; CLU_059863_1_5_1; -.
DR   InParanoid; O14921; -.
DR   OMA; QWSDSLE; -.
DR   OrthoDB; 22856at2759; -.
DR   PhylomeDB; O14921; -.
DR   TreeFam; TF315837; -.
DR   PathwayCommons; O14921; -.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; O14921; -.
DR   SIGNOR; O14921; -.
DR   BioGRID-ORCS; 6003; 103 hits in 1111 CRISPR screens.
DR   ChiTaRS; RGS13; human.
DR   GeneWiki; RGS13; -.
DR   GenomeRNAi; 6003; -.
DR   Pharos; O14921; Tbio.
DR   PRO; PR:O14921; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O14921; Protein.
DR   Bgee; ENSG00000127074; Expressed in vermiform appendix and 94 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd08716; RGS_RGS13; 1.
DR   Gene3D; 1.10.196.10; -; 2.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR024066; RGS_subdom1/3.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR10845; REGULATOR OF G PROTEIN SIGNALING; 1.
DR   PANTHER; PTHR10845:SF32; REGULATOR OF G-PROTEIN SIGNALING 13; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   Genevisible; O14921; HS.
PE   1: Evidence at protein level;
KW   Reference proteome; Signal transduction inhibitor.
FT   CHAIN           1..159
FT                   /note="Regulator of G-protein signaling 13"
FT                   /id="PRO_0000204215"
FT   DOMAIN          34..150
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   VARIANT         150
FT                   /note="L -> F (in dbSNP:rs16834603)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_034453"
SQ   SEQUENCE   159 AA;  19135 MW;  A7AEFD70DB8450C3 CRC64;
     MSRRNCWICK MCRDESKRPP SNLTLEEVLQ WAQSFENLMA TKYGPVVYAA YLKMEHSDEN
     IQFWMACETY KKIASRWSRI SRAKKLYKIY IQPQSPREIN IDSSTRETII RNIQEPTETC
     FEEAQKIVYM HMERDSYPRF LKSEMYQKLL KTMQSNNSF
//