RGS18_HUMAN
ID RGS18_HUMAN Reviewed; 235 AA.
AC Q9NS28; B2RD23;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Regulator of G-protein signaling 18;
DE Short=RGS18;
GN Name=RGS18; Synonyms=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].
RA Zhang W., Wan T., Yuan Z., He L., Cao X.;
RT "A novel regulator of G-protein signaling.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11042171; DOI=10.1074/jbc.m005947200;
RA Park I.K., Klug C.A., Li K., Jerabek L., Li L., Nanamori M., Neubig R.R.,
RA Hood L., Weissman I.L., Clarke M.F.;
RT "Molecular cloning and characterization of a novel regulator of G-protein
RT signaling from mouse hematopoietic stem cells.";
RL J. Biol. Chem. 276:915-923(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Platelet;
RX PubMed=11955952; DOI=10.1016/s0898-6568(02)00012-8;
RA Gagnon A.W., Murray D.L., Leadley R.J. Jr.;
RT "Cloning and characterization of a novel regulator of G protein signalling
RT in human platelets.";
RL Cell. Signal. 14:595-606(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
RN [8]
RP PHOSPHORYLATION AT SER-49.
RX PubMed=14645010; DOI=10.1182/blood-2003-07-2392;
RA Garcia A., Prabhakar S., Hughan S., Anderson T.W., Brock C.J., Pearce A.C.,
RA Dwek R.A., Watson S.P., Hebestreit H.F., Zitzmann N.;
RT "Differential proteome analysis of TRAP-activated platelets: involvement of
RT DOK-2 and phosphorylation of RGS proteins.";
RL Blood 103:2088-2095(2004).
RN [9]
RP STRUCTURE BY NMR OF 76-204.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RGS domain of human regulator of G-protein
RT signaling 18.";
RL Submitted (APR-2007) to the PDB data bank.
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 G(i) alpha-1, G(i) alpha-2, G(i)
CC alpha-3 and G(q) alpha. {ECO:0000269|PubMed:11042171,
CC ECO:0000269|PubMed:11955952}.
CC -!- INTERACTION:
CC Q9NS28; P59215: Gnao1; Xeno; NbExp=2; IntAct=EBI-15933052, EBI-8071125;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in peripheral leukocytes, bone marrow,
CC platelet, spleen and fetal liver. {ECO:0000269|PubMed:11042171,
CC ECO:0000269|PubMed:11955952}.
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DR EMBL; AF076642; AAF80227.1; -; mRNA.
DR EMBL; AF268036; AAK58589.1; -; mRNA.
DR EMBL; AL596342; CAH71160.1; -; Genomic_DNA.
DR EMBL; AL513175; CAH71160.1; JOINED; Genomic_DNA.
DR EMBL; AK315377; BAG37770.1; -; mRNA.
DR EMBL; AL513175; CAH70529.1; -; Genomic_DNA.
DR EMBL; AL596342; CAH70529.1; JOINED; Genomic_DNA.
DR EMBL; CH471067; EAW91223.1; -; Genomic_DNA.
DR EMBL; BC020632; AAH20632.1; -; mRNA.
DR CCDS; CCDS1374.1; -.
DR RefSeq; NP_570138.1; NM_130782.2.
DR PDB; 2DLV; NMR; -; A=76-202.
DR PDB; 2JM5; NMR; -; A=75-223.
DR PDB; 2OWI; NMR; -; A=75-223.
DR PDBsum; 2DLV; -.
DR PDBsum; 2JM5; -.
DR PDBsum; 2OWI; -.
DR AlphaFoldDB; Q9NS28; -.
DR BMRB; Q9NS28; -.
DR SMR; Q9NS28; -.
DR BioGRID; 122160; 6.
DR DIP; DIP-59096N; -.
DR IntAct; Q9NS28; 1.
DR STRING; 9606.ENSP00000356430; -.
DR iPTMnet; Q9NS28; -.
DR PhosphoSitePlus; Q9NS28; -.
DR BioMuta; RGS18; -.
DR DMDM; 15214228; -.
DR OGP; Q9NS28; -.
DR EPD; Q9NS28; -.
DR MassIVE; Q9NS28; -.
DR PaxDb; Q9NS28; -.
DR PeptideAtlas; Q9NS28; -.
DR PRIDE; Q9NS28; -.
DR ProteomicsDB; 82475; -.
DR Antibodypedia; 20616; 193 antibodies from 30 providers.
DR DNASU; 64407; -.
DR Ensembl; ENST00000367460.4; ENSP00000356430.3; ENSG00000150681.10.
DR GeneID; 64407; -.
DR KEGG; hsa:64407; -.
DR MANE-Select; ENST00000367460.4; ENSP00000356430.3; NM_130782.3; NP_570138.1.
DR UCSC; uc001gsg.4; human.
DR CTD; 64407; -.
DR DisGeNET; 64407; -.
DR GeneCards; RGS18; -.
DR HGNC; HGNC:14261; RGS18.
DR HPA; ENSG00000150681; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 607192; gene.
DR neXtProt; NX_Q9NS28; -.
DR OpenTargets; ENSG00000150681; -.
DR PharmGKB; PA34369; -.
DR VEuPathDB; HostDB:ENSG00000150681; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000161034; -.
DR HOGENOM; CLU_059863_3_2_1; -.
DR InParanoid; Q9NS28; -.
DR OMA; YNEFQDV; -.
DR OrthoDB; 1193829at2759; -.
DR PhylomeDB; Q9NS28; -.
DR TreeFam; TF315837; -.
DR PathwayCommons; Q9NS28; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; Q9NS28; -.
DR BioGRID-ORCS; 64407; 9 hits in 1058 CRISPR screens.
DR ChiTaRS; RGS18; human.
DR EvolutionaryTrace; Q9NS28; -.
DR GeneWiki; RGS18; -.
DR GenomeRNAi; 64407; -.
DR Pharos; Q9NS28; Tbio.
DR PRO; PR:Q9NS28; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NS28; protein.
DR Bgee; ENSG00000150681; Expressed in monocyte and 116 other tissues.
DR Genevisible; Q9NS28; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
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:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034950; RGS18.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF155; PTHR10845:SF155; 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; Cytoplasm; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..235
FT /note="Regulator of G-protein signaling 18"
FT /id="PRO_0000204227"
FT DOMAIN 86..202
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14645010"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PG4"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PG4"
FT CONFLICT 226..227
FT /note="DV -> ML (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:2DLV"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2DLV"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:2DLV"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:2DLV"
SQ SEQUENCE 235 AA; 27582 MW; 973ABDE8EC7DE3D5 CRC64;
METTLLFFSQ INMCESKEKT FFKLIHGSGK EETSKEAKIR AKEKRNRLSL LVQKPEFHED
TRSSRSGHLA KETRVSPEEA VKWGESFDKL LSHRDGLEAF TRFLKTEFSE ENIEFWIACE
DFKKSKGPQQ IHLKAKAIYE KFIQTDAPKE VNLDFHTKEV ITNSITQPTL HSFDAAQSRV
YQLMEQDSYT RFLKSDIYLD LMEGRPQRPT NLRRRSRSFT CNEFQDVQSD VAIWL
