Full text data of RGS10
RGS10
[Confidence: low (only semi-automatic identification from reviews)]
Regulator of G-protein signaling 10; RGS10
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Regulator of G-protein signaling 10; RGS10
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43665
ID RGS10_HUMAN Reviewed; 173 AA.
AC O43665; A8K408; B1AMR8; Q6IAZ6; Q96GN0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 14-AUG-2001, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Regulator of G-protein signaling 10;
DE Short=RGS10;
GN Name=RGS10;
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] (ISOFORM 1).
RX PubMed=8774883; DOI=10.1038/383175a0;
RA Hunt T.W., Fields T.A., Casey P.J., Peralta E.G.;
RT "RGS10 is a selective activator of G alpha i GTPase activity.";
RL Nature 383:175-177(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10791963; DOI=10.1074/jbc.M002082200;
RA Chatterjee T.K., Fisher R.A.;
RT "Cytoplasmic, nuclear, and Golgi localization of RGS proteins.
RT Evidence for N-terminal and RGS domain sequences as intracellular
RT targeting motifs.";
RL J. Biol. Chem. 275:24013-24021(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11443111; DOI=10.1074/jbc.M100960200;
RA Burgon P.G., Lee W.L., Nixon A.B., Peralta E.G., Casey P.J.;
RT "Phosphorylation and nuclear translocation of a regulator of G protein
RT signaling (RGS10).";
RL J. Biol. Chem. 276:32828-32834(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
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 [10]
RP PALMITOYLATION AT CYS-66.
RX PubMed=10608901; DOI=10.1074/jbc.274.53.38260;
RA Tu Y., Popov S., Slaughter C., Ross E.M.;
RT "Palmitoylation of a conserved cysteine in the regulator of G protein
RT signaling (RGS) domain modulates the GTPase-activating activity of
RT RGS4 and RGS10.";
RL J. Biol. Chem. 274:38260-38267(1999).
RN [11]
RP INHIBITION.
RX PubMed=9353196; DOI=10.1126/science.278.5340.1132;
RA Tu Y., Wang J., Ross E.M.;
RT "Inhibition of brain Gz GAP and other RGS proteins by palmitoylation
RT of G protein alpha subunits.";
RL Science 278:1132-1135(1997).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP STRUCTURE BY NMR OF 23-158.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RGS domain of human regulator of G-protein
RT signaling 10.";
RL Submitted (OCT-2006) 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
CC their inactive GDP-bound form. Associates specifically with the
CC activated forms of the G protein subunits G(i)-alpha and G(z)-
CC alpha but fails to interact with the structurally and functionally
CC distinct G(s)-alpha subunit. Activity on G(z)-alpha is inhibited
CC by palmitoylation of the G-protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O43665-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43665-2; Sequence=VSP_005681;
CC Name=3;
CC IsoId=O43665-3; Sequence=VSP_027366;
CC -!- PTM: Isoform 3 is phosphorylated on Ser-16.
CC -!- SIMILARITY: Contains 1 RGS domain.
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DR EMBL; AF368902; AAK52979.1; -; mRNA.
DR EMBL; AF045229; AAC03783.1; -; mRNA.
DR EMBL; AF493934; AAM12648.1; -; mRNA.
DR EMBL; AK290773; BAF83462.1; -; mRNA.
DR EMBL; CR457008; CAG33289.1; -; mRNA.
DR EMBL; AL355273; CAI16486.1; -; Genomic_DNA.
DR EMBL; AC012468; CAI16486.1; JOINED; Genomic_DNA.
DR EMBL; AL355273; CAI16488.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49389.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49390.1; -; Genomic_DNA.
DR EMBL; BC009361; AAH09361.1; -; mRNA.
DR PIR; S71812; S71812.
DR RefSeq; NP_001005339.1; NM_001005339.1.
DR RefSeq; NP_002916.1; NM_002925.3.
DR UniGene; Hs.501200; -.
DR PDB; 2DLR; NMR; -; A=23-158.
DR PDB; 2I59; NMR; -; A=22-157.
DR PDB; 2IHB; X-ray; 2.71 A; B=9-152.
DR PDBsum; 2DLR; -.
DR PDBsum; 2I59; -.
DR PDBsum; 2IHB; -.
DR ProteinModelPortal; O43665; -.
DR SMR; O43665; 20-157.
DR DIP; DIP-50368N; -.
DR STRING; 9606.ENSP00000358099; -.
DR OGP; O43665; -.
DR PaxDb; O43665; -.
DR PRIDE; O43665; -.
DR DNASU; 6001; -.
DR Ensembl; ENST00000369101; ENSP00000358097; ENSG00000148908.
DR Ensembl; ENST00000369103; ENSP00000358099; ENSG00000148908.
DR Ensembl; ENST00000392865; ENSP00000376605; ENSG00000148908.
DR GeneID; 6001; -.
DR KEGG; hsa:6001; -.
DR UCSC; uc001lee.3; human.
DR CTD; 6001; -.
DR GeneCards; GC10M121249; -.
DR HGNC; HGNC:9992; RGS10.
DR HPA; CAB004559; -.
DR HPA; HPA021305; -.
DR MIM; 602856; gene.
DR neXtProt; NX_O43665; -.
DR PharmGKB; PA34362; -.
DR eggNOG; NOG271158; -.
DR HOGENOM; HOG000233512; -.
DR HOVERGEN; HBG013233; -.
DR KO; K16449; -.
DR OMA; PKSTAKW; -.
DR OrthoDB; EOG7XDBF0; -.
DR SignaLink; O43665; -.
DR EvolutionaryTrace; O43665; -.
DR GeneWiki; RGS10; -.
DR GenomeRNAi; 6001; -.
DR NextBio; 23399; -.
DR PMAP-CutDB; O43665; -.
DR PRO; PR:O43665; -.
DR Bgee; O43665; -.
DR CleanEx; HS_RGS10; -.
DR Genevestigator; O43665; -.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR GO; GO:0005096; F:GTPase activator activity; IBA:RefGenome.
DR GO; GO:0038032; P:termination of G-protein coupled receptor signaling pathway; IEA:InterPro.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR024066; Regulat_G_prot_signal_dom1.
DR InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR InterPro; IPR000342; RGS_dom.
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; Alternative splicing; Complete proteome; Lipoprotein;
KW Palmitate; Phosphoprotein; Polymorphism; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1 173 Regulator of G-protein signaling 10.
FT /FTId=PRO_0000204207.
FT DOMAIN 33 148 RGS.
FT LIPID 66 66 S-palmitoyl cysteine.
FT VAR_SEQ 1 9 MQSELCFAD -> MEH (in isoform 2).
FT /FTId=VSP_005681.
FT VAR_SEQ 1 8 MQSELCFA -> MFNRAVSRLSRKRPPS (in isoform
FT 3).
FT /FTId=VSP_027366.
FT VARIANT 94 94 A -> V (in dbSNP:rs1802228).
FT /FTId=VAR_011896.
FT HELIX 25 32
FT HELIX 34 39
FT HELIX 41 53
FT HELIX 58 71
FT HELIX 75 89
FT HELIX 94 96
FT HELIX 103 105
FT HELIX 108 112
FT TURN 116 119
FT HELIX 120 132
FT HELIX 134 138
FT TURN 142 144
FT TURN 146 150
SQ SEQUENCE 173 AA; 20236 MW; CA73D1E38F551EF1 CRC64;
MQSELCFADI HDSDGSSSSS HQSLKSTAKW AASLENLLED PEGVKRFREF LKKEFSEENV
LFWLACEDFK KMQDKTQMQE KAKEIYMTFL SSKASSQVNV EGQSRLNEKI LEEPHPLMFQ
KLQDQIFNLM KYDSYSRFLK SDLFLKHKRT EEEEEDLPDA QTAAKRASRI YNT
//
ID RGS10_HUMAN Reviewed; 173 AA.
AC O43665; A8K408; B1AMR8; Q6IAZ6; Q96GN0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 14-AUG-2001, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Regulator of G-protein signaling 10;
DE Short=RGS10;
GN Name=RGS10;
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] (ISOFORM 1).
RX PubMed=8774883; DOI=10.1038/383175a0;
RA Hunt T.W., Fields T.A., Casey P.J., Peralta E.G.;
RT "RGS10 is a selective activator of G alpha i GTPase activity.";
RL Nature 383:175-177(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10791963; DOI=10.1074/jbc.M002082200;
RA Chatterjee T.K., Fisher R.A.;
RT "Cytoplasmic, nuclear, and Golgi localization of RGS proteins.
RT Evidence for N-terminal and RGS domain sequences as intracellular
RT targeting motifs.";
RL J. Biol. Chem. 275:24013-24021(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11443111; DOI=10.1074/jbc.M100960200;
RA Burgon P.G., Lee W.L., Nixon A.B., Peralta E.G., Casey P.J.;
RT "Phosphorylation and nuclear translocation of a regulator of G protein
RT signaling (RGS10).";
RL J. Biol. Chem. 276:32828-32834(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
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 [10]
RP PALMITOYLATION AT CYS-66.
RX PubMed=10608901; DOI=10.1074/jbc.274.53.38260;
RA Tu Y., Popov S., Slaughter C., Ross E.M.;
RT "Palmitoylation of a conserved cysteine in the regulator of G protein
RT signaling (RGS) domain modulates the GTPase-activating activity of
RT RGS4 and RGS10.";
RL J. Biol. Chem. 274:38260-38267(1999).
RN [11]
RP INHIBITION.
RX PubMed=9353196; DOI=10.1126/science.278.5340.1132;
RA Tu Y., Wang J., Ross E.M.;
RT "Inhibition of brain Gz GAP and other RGS proteins by palmitoylation
RT of G protein alpha subunits.";
RL Science 278:1132-1135(1997).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP STRUCTURE BY NMR OF 23-158.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RGS domain of human regulator of G-protein
RT signaling 10.";
RL Submitted (OCT-2006) 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
CC their inactive GDP-bound form. Associates specifically with the
CC activated forms of the G protein subunits G(i)-alpha and G(z)-
CC alpha but fails to interact with the structurally and functionally
CC distinct G(s)-alpha subunit. Activity on G(z)-alpha is inhibited
CC by palmitoylation of the G-protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O43665-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43665-2; Sequence=VSP_005681;
CC Name=3;
CC IsoId=O43665-3; Sequence=VSP_027366;
CC -!- PTM: Isoform 3 is phosphorylated on Ser-16.
CC -!- SIMILARITY: Contains 1 RGS domain.
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DR EMBL; AF368902; AAK52979.1; -; mRNA.
DR EMBL; AF045229; AAC03783.1; -; mRNA.
DR EMBL; AF493934; AAM12648.1; -; mRNA.
DR EMBL; AK290773; BAF83462.1; -; mRNA.
DR EMBL; CR457008; CAG33289.1; -; mRNA.
DR EMBL; AL355273; CAI16486.1; -; Genomic_DNA.
DR EMBL; AC012468; CAI16486.1; JOINED; Genomic_DNA.
DR EMBL; AL355273; CAI16488.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49389.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49390.1; -; Genomic_DNA.
DR EMBL; BC009361; AAH09361.1; -; mRNA.
DR PIR; S71812; S71812.
DR RefSeq; NP_001005339.1; NM_001005339.1.
DR RefSeq; NP_002916.1; NM_002925.3.
DR UniGene; Hs.501200; -.
DR PDB; 2DLR; NMR; -; A=23-158.
DR PDB; 2I59; NMR; -; A=22-157.
DR PDB; 2IHB; X-ray; 2.71 A; B=9-152.
DR PDBsum; 2DLR; -.
DR PDBsum; 2I59; -.
DR PDBsum; 2IHB; -.
DR ProteinModelPortal; O43665; -.
DR SMR; O43665; 20-157.
DR DIP; DIP-50368N; -.
DR STRING; 9606.ENSP00000358099; -.
DR OGP; O43665; -.
DR PaxDb; O43665; -.
DR PRIDE; O43665; -.
DR DNASU; 6001; -.
DR Ensembl; ENST00000369101; ENSP00000358097; ENSG00000148908.
DR Ensembl; ENST00000369103; ENSP00000358099; ENSG00000148908.
DR Ensembl; ENST00000392865; ENSP00000376605; ENSG00000148908.
DR GeneID; 6001; -.
DR KEGG; hsa:6001; -.
DR UCSC; uc001lee.3; human.
DR CTD; 6001; -.
DR GeneCards; GC10M121249; -.
DR HGNC; HGNC:9992; RGS10.
DR HPA; CAB004559; -.
DR HPA; HPA021305; -.
DR MIM; 602856; gene.
DR neXtProt; NX_O43665; -.
DR PharmGKB; PA34362; -.
DR eggNOG; NOG271158; -.
DR HOGENOM; HOG000233512; -.
DR HOVERGEN; HBG013233; -.
DR KO; K16449; -.
DR OMA; PKSTAKW; -.
DR OrthoDB; EOG7XDBF0; -.
DR SignaLink; O43665; -.
DR EvolutionaryTrace; O43665; -.
DR GeneWiki; RGS10; -.
DR GenomeRNAi; 6001; -.
DR NextBio; 23399; -.
DR PMAP-CutDB; O43665; -.
DR PRO; PR:O43665; -.
DR Bgee; O43665; -.
DR CleanEx; HS_RGS10; -.
DR Genevestigator; O43665; -.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR GO; GO:0005096; F:GTPase activator activity; IBA:RefGenome.
DR GO; GO:0038032; P:termination of G-protein coupled receptor signaling pathway; IEA:InterPro.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR024066; Regulat_G_prot_signal_dom1.
DR InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR InterPro; IPR000342; RGS_dom.
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; Alternative splicing; Complete proteome; Lipoprotein;
KW Palmitate; Phosphoprotein; Polymorphism; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1 173 Regulator of G-protein signaling 10.
FT /FTId=PRO_0000204207.
FT DOMAIN 33 148 RGS.
FT LIPID 66 66 S-palmitoyl cysteine.
FT VAR_SEQ 1 9 MQSELCFAD -> MEH (in isoform 2).
FT /FTId=VSP_005681.
FT VAR_SEQ 1 8 MQSELCFA -> MFNRAVSRLSRKRPPS (in isoform
FT 3).
FT /FTId=VSP_027366.
FT VARIANT 94 94 A -> V (in dbSNP:rs1802228).
FT /FTId=VAR_011896.
FT HELIX 25 32
FT HELIX 34 39
FT HELIX 41 53
FT HELIX 58 71
FT HELIX 75 89
FT HELIX 94 96
FT HELIX 103 105
FT HELIX 108 112
FT TURN 116 119
FT HELIX 120 132
FT HELIX 134 138
FT TURN 142 144
FT TURN 146 150
SQ SEQUENCE 173 AA; 20236 MW; CA73D1E38F551EF1 CRC64;
MQSELCFADI HDSDGSSSSS HQSLKSTAKW AASLENLLED PEGVKRFREF LKKEFSEENV
LFWLACEDFK KMQDKTQMQE KAKEIYMTFL SSKASSQVNV EGQSRLNEKI LEEPHPLMFQ
KLQDQIFNLM KYDSYSRFLK SDLFLKHKRT EEEEEDLPDA QTAAKRASRI YNT
//
MIM
602856
*RECORD*
*FIELD* NO
602856
*FIELD* TI
*602856 REGULATOR OF G PROTEIN SIGNALING 10; RGS10
*FIELD* TX
DESCRIPTION
RGS proteins negatively regulate signaling pathways involving
read more7-transmembrane receptors and heterotrimeric G proteins. See 602189 for
background.
CLONING
Using a yeast 2-hybrid system with a mutationally activated form of rat
G-alpha(i3) as the bait, Hunt et al. (1996) isolated HeLa cell cDNAs
encoding RGS10. Like all members of the RGS family, the predicted
173-amino acid RGS10 contains a 120-amino acid core domain that is
strongly conserved with the yeast Sst2 protein. Northern blot analysis
detected an approximately 900-bp RGS10 transcript in HeLa cells, human
embryonic kidney 293 cells, and mouse brain.
By microarray analysis, Yang and Li (2007) found that RGS10 was highly
expressed in human osteoclastoma. Northern blot analysis confirmed high
RGS10 expression in osteoclastoma and detected weaker expression in
brain, liver, kidney, and the Hep2 cell line; no expression was detected
in other tissues and cell lines examined. Mouse Rgs10 was highly
expressed in preosteoclasts and osteoclasts derived from RANKL (TNFSF11;
602642)-stimulated bone marrow-derived monocytes, but it was not
expressed in osteoblasts or preosteoblasts.
GENE FUNCTION
Using coimmunoprecipitation studies, Hunt et al. (1996) demonstrated
that RGS10 associates specifically with the activated forms of the 2
related G protein subunits G-alpha(i3) and G-alpha(z) but fails to
interact with the structurally and functionally distinct G-alpha(s)
subunit. In vitro assays indicated that RGS10 potently and selectively
increases the GTP hydrolytic activity of several G-alpha(i) family
members.
Using human T cells silenced for or overexpressing RGS10, Garcia-Bernal
et al. (2011) showed that RGS10 inhibited G-alpha-dependent,
chemokine-upregulated T-cell adhesion mediated by alpha-4 (ITGA4;
192975)/beta-1 (ITGB1; 135630) and alpha-L (ITGAL; 153370)/beta-2
(ITGB2; 600065) integrins. The data suggested that RGS10 opposes
activation by chemokines of the VAV1 (164875)-RAC1 (602048) pathway in T
cells, leading to repression of adhesion strengthening mediated by
alpha-4/beta-1. RGS10 also limited adhesion-independent cell chemotaxis
and activation of CDC42 (116952).
GENE STRUCTURE
Sierra et al. (2002) determined that the RGS10 gene contains 5 exons and
spans 35 kb.
MAPPING
By genomic sequence analysis, Sierra et al. (2002) mapped the RGS10 gene
to chromosome 10q26.11. They mapped the mouse Rgs10 gene to chromosome 7
by interspecific backcross mapping.
ANIMAL MODEL
Yang and Li (2007) obtained Rgs10 -/- mice at the expected mendelian
ratio, but they were smaller and had shorter limbs than their wildtype
littermates. Growth retardation became apparent during the first or
second postnatal week. Histologically, Rgs10 -/- mice exhibited severe
osteopetrosis. Disruption of Rgs10 impaired osteoclast differentiation
due to the absence of calcium current oscillations and loss of Nfatc1
(600489) expression. Ectopic expression of Rgs10 markedly enhanced
Rankl-induced osteoclast differentiation. Rgs10 competitively bound
Ca(2+)/calmodulin (see CALM1; 114180) and phosphatidylinositol
3-phosphate in a Ca(2+)-dependent manner. Yang and Li (2007) concluded
that RGS10 is a key regulator of Ca(2+) current oscillations during
osteoclast differentiation.
*FIELD* RF
1. Garcia-Bernal, D.; Dios-Esponera, A.; Sotillo-Mallo, E.; Garcia-Verdugo,
R.; Arellano-Sanchez, N.; Teixido, J.: RGS10 restricts upregulation
by chemokines of T cell adhesion mediated by alpha-4-beta-1 and alpha-L-beta-2
integrins. J. Immun. 187: 1264-1272, 2011.
2. Hunt, T. W.; Fields, T. A.; Casey, P. J.; Peralta, E. G.: RGS10
is a selective activator of G-alpha(i) GTPase activity. Nature 383:
175-177, 1996.
3. Sierra, D. A.; Gilbert, D. J.; Householder, D.; Grishin, N. V.;
Yu, K.; Ukidwe, P.; Barker, S. A.; He, W.; Wensel, T. G.; Otero, G.;
Brown, G.; Copeland, N. G.; Jenkins, N. A.; Wilkie, T. M.: Evolution
of the regulators of G-protein signaling multigene family in mouse
and human. Genomics 79: 177-185, 2002.
4. Yang, S.; Li, Y.-P.: RGS10-null mutation impairs osteoclast differentiation
resulting from the loss of [Ca2+]i oscillation regulation. Genes
Dev. 21: 1803-1816, 2007.
*FIELD* CN
Paul J. Converse - updated: 1/6/2012
Patricia A. Hartz - updated: 8/23/2007
Patricia A. Hartz - updated: 9/12/2002
*FIELD* CD
Patti M. Sherman: 7/16/1998
*FIELD* ED
mgross: 01/19/2012
terry: 1/6/2012
mgross: 8/31/2007
terry: 8/23/2007
mgross: 9/12/2002
carol: 7/24/1998
dkim: 7/23/1998
carol: 7/16/1998
*RECORD*
*FIELD* NO
602856
*FIELD* TI
*602856 REGULATOR OF G PROTEIN SIGNALING 10; RGS10
*FIELD* TX
DESCRIPTION
RGS proteins negatively regulate signaling pathways involving
read more7-transmembrane receptors and heterotrimeric G proteins. See 602189 for
background.
CLONING
Using a yeast 2-hybrid system with a mutationally activated form of rat
G-alpha(i3) as the bait, Hunt et al. (1996) isolated HeLa cell cDNAs
encoding RGS10. Like all members of the RGS family, the predicted
173-amino acid RGS10 contains a 120-amino acid core domain that is
strongly conserved with the yeast Sst2 protein. Northern blot analysis
detected an approximately 900-bp RGS10 transcript in HeLa cells, human
embryonic kidney 293 cells, and mouse brain.
By microarray analysis, Yang and Li (2007) found that RGS10 was highly
expressed in human osteoclastoma. Northern blot analysis confirmed high
RGS10 expression in osteoclastoma and detected weaker expression in
brain, liver, kidney, and the Hep2 cell line; no expression was detected
in other tissues and cell lines examined. Mouse Rgs10 was highly
expressed in preosteoclasts and osteoclasts derived from RANKL (TNFSF11;
602642)-stimulated bone marrow-derived monocytes, but it was not
expressed in osteoblasts or preosteoblasts.
GENE FUNCTION
Using coimmunoprecipitation studies, Hunt et al. (1996) demonstrated
that RGS10 associates specifically with the activated forms of the 2
related G protein subunits G-alpha(i3) and G-alpha(z) but fails to
interact with the structurally and functionally distinct G-alpha(s)
subunit. In vitro assays indicated that RGS10 potently and selectively
increases the GTP hydrolytic activity of several G-alpha(i) family
members.
Using human T cells silenced for or overexpressing RGS10, Garcia-Bernal
et al. (2011) showed that RGS10 inhibited G-alpha-dependent,
chemokine-upregulated T-cell adhesion mediated by alpha-4 (ITGA4;
192975)/beta-1 (ITGB1; 135630) and alpha-L (ITGAL; 153370)/beta-2
(ITGB2; 600065) integrins. The data suggested that RGS10 opposes
activation by chemokines of the VAV1 (164875)-RAC1 (602048) pathway in T
cells, leading to repression of adhesion strengthening mediated by
alpha-4/beta-1. RGS10 also limited adhesion-independent cell chemotaxis
and activation of CDC42 (116952).
GENE STRUCTURE
Sierra et al. (2002) determined that the RGS10 gene contains 5 exons and
spans 35 kb.
MAPPING
By genomic sequence analysis, Sierra et al. (2002) mapped the RGS10 gene
to chromosome 10q26.11. They mapped the mouse Rgs10 gene to chromosome 7
by interspecific backcross mapping.
ANIMAL MODEL
Yang and Li (2007) obtained Rgs10 -/- mice at the expected mendelian
ratio, but they were smaller and had shorter limbs than their wildtype
littermates. Growth retardation became apparent during the first or
second postnatal week. Histologically, Rgs10 -/- mice exhibited severe
osteopetrosis. Disruption of Rgs10 impaired osteoclast differentiation
due to the absence of calcium current oscillations and loss of Nfatc1
(600489) expression. Ectopic expression of Rgs10 markedly enhanced
Rankl-induced osteoclast differentiation. Rgs10 competitively bound
Ca(2+)/calmodulin (see CALM1; 114180) and phosphatidylinositol
3-phosphate in a Ca(2+)-dependent manner. Yang and Li (2007) concluded
that RGS10 is a key regulator of Ca(2+) current oscillations during
osteoclast differentiation.
*FIELD* RF
1. Garcia-Bernal, D.; Dios-Esponera, A.; Sotillo-Mallo, E.; Garcia-Verdugo,
R.; Arellano-Sanchez, N.; Teixido, J.: RGS10 restricts upregulation
by chemokines of T cell adhesion mediated by alpha-4-beta-1 and alpha-L-beta-2
integrins. J. Immun. 187: 1264-1272, 2011.
2. Hunt, T. W.; Fields, T. A.; Casey, P. J.; Peralta, E. G.: RGS10
is a selective activator of G-alpha(i) GTPase activity. Nature 383:
175-177, 1996.
3. Sierra, D. A.; Gilbert, D. J.; Householder, D.; Grishin, N. V.;
Yu, K.; Ukidwe, P.; Barker, S. A.; He, W.; Wensel, T. G.; Otero, G.;
Brown, G.; Copeland, N. G.; Jenkins, N. A.; Wilkie, T. M.: Evolution
of the regulators of G-protein signaling multigene family in mouse
and human. Genomics 79: 177-185, 2002.
4. Yang, S.; Li, Y.-P.: RGS10-null mutation impairs osteoclast differentiation
resulting from the loss of [Ca2+]i oscillation regulation. Genes
Dev. 21: 1803-1816, 2007.
*FIELD* CN
Paul J. Converse - updated: 1/6/2012
Patricia A. Hartz - updated: 8/23/2007
Patricia A. Hartz - updated: 9/12/2002
*FIELD* CD
Patti M. Sherman: 7/16/1998
*FIELD* ED
mgross: 01/19/2012
terry: 1/6/2012
mgross: 8/31/2007
terry: 8/23/2007
mgross: 9/12/2002
carol: 7/24/1998
dkim: 7/23/1998
carol: 7/16/1998