Full text data of RGS19
RGS19
(GAIP, GNAI3IP)
[Confidence: low (only semi-automatic identification from reviews)]
Regulator of G-protein signaling 19; RGS19 (G-alpha-interacting protein; GAIP)
Regulator of G-protein signaling 19; RGS19 (G-alpha-interacting protein; GAIP)
UniProt
P49795
ID RGS19_HUMAN Reviewed; 217 AA.
AC P49795; A8K216; E1P5G9; Q53XN0; Q8TD60;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Regulator of G-protein signaling 19;
DE Short=RGS19;
DE AltName: Full=G-alpha-interacting protein;
DE Short=GAIP;
GN Name=RGS19; Synonyms=GAIP, GNAI3IP;
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].
RX PubMed=8524874; DOI=10.1073/pnas.92.25.11916;
RA de Vries L., Mousli M., Wurmser A., Farquhar M.G.;
RT "GAIP, a protein that specifically interacts with the trimeric G
RT protein G alpha i3, is a member of a protein family with a highly
RT conserved core domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11916-11920(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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-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
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, Placenta, and Testis;
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 [8]
RP PALMITOYLATION.
RX PubMed=8986788; DOI=10.1073/pnas.93.26.15203;
RA de Vries L., Elenko E., Hubler L., Jones T.L.Z., Farquhar M.G.;
RT "GAIP is membrane-anchored by palmitoylation and interacts with the
RT activated (GTP-bound) form of G alpha i subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15203-15208(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP STRUCTURE BY NMR OF 79-206.
RX PubMed=10452897; DOI=10.1006/jmbi.1999.2989;
RA de Alba E., De Vries L., Farquhar M.G., Tjandra N.;
RT "Solution structure of human GAIP (Galpha interacting protein): a
RT regulator of G protein signaling.";
RL J. Mol. Biol. 291:927-939(1999).
RN [11]
RP INHIBITION.
RX PubMed=9748280; DOI=10.1074/jbc.273.40.26014;
RA Wang J., Ducret A., Tu Y., Kozasa T., Aebersold R., Ross E.M.;
RT "RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane
RT association, regulation by Galphaz phosphorylation, and relationship
RT to a Gz GTPase-activating protein subfamily.";
RL J. Biol. Chem. 273:26014-26025(1998).
RN [12]
RP PHOSPHORYLATION AT SER-151, AND MUTAGENESIS OF SER-151.
RX PubMed=10993892; DOI=10.1074/jbc.M006198200;
RA Ogier-Denis E., Pattingre S., El Benna J., Codogno P.;
RT "Erk1/2-dependent phosphorylation of Galpha-interacting protein
RT stimulates its GTPase accelerating activity and autophagy in human
RT colon cancer cells.";
RL J. Biol. Chem. 275:39090-39095(2000).
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. Binds to G-alpha subfamily 1
CC members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2.
CC Activity on G(z)-alpha is inhibited by phosphorylation and
CC palmitoylation of the G-protein.
CC -!- SUBUNIT: Interacts with GIPC PDZ domain.
CC -!- INTERACTION:
CC P08753:Gnai3 (xeno); NbExp=4; IntAct=EBI-874907, EBI-874897;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC -!- TISSUE SPECIFICITY: Highest expression in lung. Placenta, liver
CC and heart also express high levels of GAIP.
CC -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC motif.
CC -!- PTM: Phosphorylated, mainly on serine residues.
CC -!- SIMILARITY: Contains 1 RGS domain.
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DR EMBL; X91809; CAA62919.1; -; mRNA.
DR EMBL; AF493939; AAM12653.1; -; mRNA.
DR EMBL; AY585188; AAS94232.1; -; mRNA.
DR EMBL; BT009804; AAP88806.1; -; mRNA.
DR EMBL; AK290081; BAF82770.1; -; mRNA.
DR EMBL; AL590548; CAD11902.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75166.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75167.1; -; Genomic_DNA.
DR EMBL; BC001318; AAH01318.1; -; mRNA.
DR EMBL; BC054337; AAH54337.1; -; mRNA.
DR EMBL; BC063010; AAH63010.1; -; mRNA.
DR RefSeq; NP_001034556.1; NM_001039467.1.
DR RefSeq; NP_005864.1; NM_005873.2.
DR UniGene; Hs.422336; -.
DR PDB; 1CMZ; NMR; -; A=79-206.
DR PDBsum; 1CMZ; -.
DR ProteinModelPortal; P49795; -.
DR SMR; P49795; 79-206.
DR IntAct; P49795; 4.
DR MINT; MINT-3017930; -.
DR STRING; 9606.ENSP00000333194; -.
DR BindingDB; P49795; -.
DR PhosphoSite; P49795; -.
DR DMDM; 1730186; -.
DR PaxDb; P49795; -.
DR PRIDE; P49795; -.
DR DNASU; 10287; -.
DR Ensembl; ENST00000332298; ENSP00000333194; ENSG00000171700.
DR Ensembl; ENST00000395042; ENSP00000378483; ENSG00000171700.
DR GeneID; 10287; -.
DR KEGG; hsa:10287; -.
DR UCSC; uc002yhy.3; human.
DR CTD; 10287; -.
DR GeneCards; GC20M062704; -.
DR HGNC; HGNC:13735; RGS19.
DR HPA; CAB031925; -.
DR MIM; 605071; gene.
DR neXtProt; NX_P49795; -.
DR PharmGKB; PA34370; -.
DR eggNOG; NOG258376; -.
DR HOGENOM; HOG000233513; -.
DR HOVERGEN; HBG013233; -.
DR InParanoid; P49795; -.
DR KO; K16449; -.
DR OMA; FDKLMHS; -.
DR OrthoDB; EOG7SN8DQ; -.
DR PhylomeDB; P49795; -.
DR SignaLink; P49795; -.
DR ChiTaRS; RGS19; human.
DR EvolutionaryTrace; P49795; -.
DR GeneWiki; RGS19; -.
DR GenomeRNAi; 10287; -.
DR NextBio; 38976; -.
DR PRO; PR:P49795; -.
DR ArrayExpress; P49795; -.
DR Bgee; P49795; -.
DR CleanEx; HS_RGS19; -.
DR Genevestigator; P49795; -.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR GO; GO:0005096; F:GTPase activator activity; IBA:RefGenome.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
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; Autophagy; Complete proteome; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1 217 Regulator of G-protein signaling 19.
FT /FTId=PRO_0000204229.
FT DOMAIN 90 206 RGS.
FT REGION 207 217 Interaction with GIPC.
FT COMPBIAS 39 49 Poly-Cys.
FT MOD_RES 24 24 Phosphoserine (By similarity).
FT MOD_RES 97 97 Phosphoserine.
FT MOD_RES 151 151 Phosphoserine; by MAPK1 and MAPK3.
FT MUTAGEN 151 151 S->A: Diminishes gap activity towards
FT G(i)-alpha3 and autophagy in colon cancer
FT cells.
FT CONFLICT 204 204 A -> V (in Ref. 2; AAM12653).
FT HELIX 81 87
FT HELIX 92 95
FT HELIX 98 111
FT HELIX 115 125
FT HELIX 126 128
FT HELIX 133 145
FT TURN 146 148
FT STRAND 150 152
FT HELIX 160 168
FT STRAND 169 171
FT HELIX 178 191
FT HELIX 193 196
FT HELIX 200 203
SQ SEQUENCE 217 AA; 24636 MW; 925A5687DC222CBD CRC64;
MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS WNQERRRAWQ
ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG RSVFRAFLRT EYSEENMLFW
LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINKKMQ EPSAHTFDDA
QLQIYTLMHR DSYPRFLSSP TYRALLLQGP SQSSSEA
//
ID RGS19_HUMAN Reviewed; 217 AA.
AC P49795; A8K216; E1P5G9; Q53XN0; Q8TD60;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Regulator of G-protein signaling 19;
DE Short=RGS19;
DE AltName: Full=G-alpha-interacting protein;
DE Short=GAIP;
GN Name=RGS19; Synonyms=GAIP, GNAI3IP;
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].
RX PubMed=8524874; DOI=10.1073/pnas.92.25.11916;
RA de Vries L., Mousli M., Wurmser A., Farquhar M.G.;
RT "GAIP, a protein that specifically interacts with the trimeric G
RT protein G alpha i3, is a member of a protein family with a highly
RT conserved core domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11916-11920(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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-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
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, Placenta, and Testis;
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 [8]
RP PALMITOYLATION.
RX PubMed=8986788; DOI=10.1073/pnas.93.26.15203;
RA de Vries L., Elenko E., Hubler L., Jones T.L.Z., Farquhar M.G.;
RT "GAIP is membrane-anchored by palmitoylation and interacts with the
RT activated (GTP-bound) form of G alpha i subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15203-15208(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP STRUCTURE BY NMR OF 79-206.
RX PubMed=10452897; DOI=10.1006/jmbi.1999.2989;
RA de Alba E., De Vries L., Farquhar M.G., Tjandra N.;
RT "Solution structure of human GAIP (Galpha interacting protein): a
RT regulator of G protein signaling.";
RL J. Mol. Biol. 291:927-939(1999).
RN [11]
RP INHIBITION.
RX PubMed=9748280; DOI=10.1074/jbc.273.40.26014;
RA Wang J., Ducret A., Tu Y., Kozasa T., Aebersold R., Ross E.M.;
RT "RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane
RT association, regulation by Galphaz phosphorylation, and relationship
RT to a Gz GTPase-activating protein subfamily.";
RL J. Biol. Chem. 273:26014-26025(1998).
RN [12]
RP PHOSPHORYLATION AT SER-151, AND MUTAGENESIS OF SER-151.
RX PubMed=10993892; DOI=10.1074/jbc.M006198200;
RA Ogier-Denis E., Pattingre S., El Benna J., Codogno P.;
RT "Erk1/2-dependent phosphorylation of Galpha-interacting protein
RT stimulates its GTPase accelerating activity and autophagy in human
RT colon cancer cells.";
RL J. Biol. Chem. 275:39090-39095(2000).
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. Binds to G-alpha subfamily 1
CC members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2.
CC Activity on G(z)-alpha is inhibited by phosphorylation and
CC palmitoylation of the G-protein.
CC -!- SUBUNIT: Interacts with GIPC PDZ domain.
CC -!- INTERACTION:
CC P08753:Gnai3 (xeno); NbExp=4; IntAct=EBI-874907, EBI-874897;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC -!- TISSUE SPECIFICITY: Highest expression in lung. Placenta, liver
CC and heart also express high levels of GAIP.
CC -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC motif.
CC -!- PTM: Phosphorylated, mainly on serine residues.
CC -!- SIMILARITY: Contains 1 RGS domain.
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DR EMBL; X91809; CAA62919.1; -; mRNA.
DR EMBL; AF493939; AAM12653.1; -; mRNA.
DR EMBL; AY585188; AAS94232.1; -; mRNA.
DR EMBL; BT009804; AAP88806.1; -; mRNA.
DR EMBL; AK290081; BAF82770.1; -; mRNA.
DR EMBL; AL590548; CAD11902.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75166.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75167.1; -; Genomic_DNA.
DR EMBL; BC001318; AAH01318.1; -; mRNA.
DR EMBL; BC054337; AAH54337.1; -; mRNA.
DR EMBL; BC063010; AAH63010.1; -; mRNA.
DR RefSeq; NP_001034556.1; NM_001039467.1.
DR RefSeq; NP_005864.1; NM_005873.2.
DR UniGene; Hs.422336; -.
DR PDB; 1CMZ; NMR; -; A=79-206.
DR PDBsum; 1CMZ; -.
DR ProteinModelPortal; P49795; -.
DR SMR; P49795; 79-206.
DR IntAct; P49795; 4.
DR MINT; MINT-3017930; -.
DR STRING; 9606.ENSP00000333194; -.
DR BindingDB; P49795; -.
DR PhosphoSite; P49795; -.
DR DMDM; 1730186; -.
DR PaxDb; P49795; -.
DR PRIDE; P49795; -.
DR DNASU; 10287; -.
DR Ensembl; ENST00000332298; ENSP00000333194; ENSG00000171700.
DR Ensembl; ENST00000395042; ENSP00000378483; ENSG00000171700.
DR GeneID; 10287; -.
DR KEGG; hsa:10287; -.
DR UCSC; uc002yhy.3; human.
DR CTD; 10287; -.
DR GeneCards; GC20M062704; -.
DR HGNC; HGNC:13735; RGS19.
DR HPA; CAB031925; -.
DR MIM; 605071; gene.
DR neXtProt; NX_P49795; -.
DR PharmGKB; PA34370; -.
DR eggNOG; NOG258376; -.
DR HOGENOM; HOG000233513; -.
DR HOVERGEN; HBG013233; -.
DR InParanoid; P49795; -.
DR KO; K16449; -.
DR OMA; FDKLMHS; -.
DR OrthoDB; EOG7SN8DQ; -.
DR PhylomeDB; P49795; -.
DR SignaLink; P49795; -.
DR ChiTaRS; RGS19; human.
DR EvolutionaryTrace; P49795; -.
DR GeneWiki; RGS19; -.
DR GenomeRNAi; 10287; -.
DR NextBio; 38976; -.
DR PRO; PR:P49795; -.
DR ArrayExpress; P49795; -.
DR Bgee; P49795; -.
DR CleanEx; HS_RGS19; -.
DR Genevestigator; P49795; -.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR GO; GO:0005096; F:GTPase activator activity; IBA:RefGenome.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
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; Autophagy; Complete proteome; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1 217 Regulator of G-protein signaling 19.
FT /FTId=PRO_0000204229.
FT DOMAIN 90 206 RGS.
FT REGION 207 217 Interaction with GIPC.
FT COMPBIAS 39 49 Poly-Cys.
FT MOD_RES 24 24 Phosphoserine (By similarity).
FT MOD_RES 97 97 Phosphoserine.
FT MOD_RES 151 151 Phosphoserine; by MAPK1 and MAPK3.
FT MUTAGEN 151 151 S->A: Diminishes gap activity towards
FT G(i)-alpha3 and autophagy in colon cancer
FT cells.
FT CONFLICT 204 204 A -> V (in Ref. 2; AAM12653).
FT HELIX 81 87
FT HELIX 92 95
FT HELIX 98 111
FT HELIX 115 125
FT HELIX 126 128
FT HELIX 133 145
FT TURN 146 148
FT STRAND 150 152
FT HELIX 160 168
FT STRAND 169 171
FT HELIX 178 191
FT HELIX 193 196
FT HELIX 200 203
SQ SEQUENCE 217 AA; 24636 MW; 925A5687DC222CBD CRC64;
MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS WNQERRRAWQ
ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG RSVFRAFLRT EYSEENMLFW
LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINKKMQ EPSAHTFDDA
QLQIYTLMHR DSYPRFLSSP TYRALLLQGP SQSSSEA
//
MIM
605071
*RECORD*
*FIELD* NO
605071
*FIELD* TI
*605071 REGULATOR OF G PROTEIN SIGNALING 19; RGS19
;;G PROTEIN, ALPHA-INTERACTING PROTEIN; GAIP
read more*FIELD* TX
DESCRIPTION
The RGS19 (GAIP) protein interacts with the heterotrimeric G protein
GNAI3 (139370). Heterotrimeric G proteins are responsible for
transmitting signals from plasma membrane receptors to intracellular
effectors, such as ion channels and adenylate cyclase (e.g., ADCY1;
103072). G proteins are also involved in intracellular trafficking
through the Golgi secretory pathways (summary by De Vries et al., 1995).
CLONING
By screening a HeLa cell cDNA library using a yeast 2-hybrid system with
rat GNAI3 as bait, followed by searching an EST database, De Vries et
al. (1995) identified a cDNA encoding a 217-amino acid protein that they
designated GAIP (G protein, alpha-interacting protein). Sequence
analysis predicted that GAIP is a 24.6-kD, hydrophilic protein that
lacks a transmembrane domain and contains multiple potential
phosphorylation sites. GAIP shares approximately 31% amino acid identity
with regulator of G protein signaling-1 (RGS1; 600323) and -2 (RGS2;
600861); the 125-amino acid core domains of GAIP, RGS1, and RGS2 share
approximately 64% homology. Northern blot analysis detected a 1.6-kb
GAIP transcript in lung, placenta, liver, heart, and pancreas, with
almost no expression detected in brain, skeletal muscle, and kidney.
Yeast 2-hybrid binding analyses showed that through its core domain,
GAIP interacts strongly with GNAI3 and weakly with GNAI2 (139360), but
does not interact with GNA11 (139313).
GENE STRUCTURE
Sierra et al. (2002) determined that the RGS19 gene contains 5 exons.
MAPPING
By genomic sequence analysis, Sierra et al. (2002) mapped the RGS19 gene
to chromosome 20q13.3. They mapped the mouse Rgs19 gene to chromosome 2
by interspecific backcross mapping.
*FIELD* RF
1. De Vries, L.; Mousli, M.; Wurmser, A.; Farquhar, M. G.: GAIP,
a protein that specifically interacts with the trimeric G protein
G-alpha(i3), is a member of a protein family with a highly conserved
core domain. Proc. Nat. Acad. Sci. 92: 11916-11920, 1995.
2. 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.
*FIELD* CN
Patricia A. Hartz - updated: 9/12/2002
*FIELD* CD
Paul J. Converse: 6/23/2000
*FIELD* ED
alopez: 03/27/2012
mgross: 9/12/2002
mgross: 3/16/2001
mgross: 6/23/2000
*RECORD*
*FIELD* NO
605071
*FIELD* TI
*605071 REGULATOR OF G PROTEIN SIGNALING 19; RGS19
;;G PROTEIN, ALPHA-INTERACTING PROTEIN; GAIP
read more*FIELD* TX
DESCRIPTION
The RGS19 (GAIP) protein interacts with the heterotrimeric G protein
GNAI3 (139370). Heterotrimeric G proteins are responsible for
transmitting signals from plasma membrane receptors to intracellular
effectors, such as ion channels and adenylate cyclase (e.g., ADCY1;
103072). G proteins are also involved in intracellular trafficking
through the Golgi secretory pathways (summary by De Vries et al., 1995).
CLONING
By screening a HeLa cell cDNA library using a yeast 2-hybrid system with
rat GNAI3 as bait, followed by searching an EST database, De Vries et
al. (1995) identified a cDNA encoding a 217-amino acid protein that they
designated GAIP (G protein, alpha-interacting protein). Sequence
analysis predicted that GAIP is a 24.6-kD, hydrophilic protein that
lacks a transmembrane domain and contains multiple potential
phosphorylation sites. GAIP shares approximately 31% amino acid identity
with regulator of G protein signaling-1 (RGS1; 600323) and -2 (RGS2;
600861); the 125-amino acid core domains of GAIP, RGS1, and RGS2 share
approximately 64% homology. Northern blot analysis detected a 1.6-kb
GAIP transcript in lung, placenta, liver, heart, and pancreas, with
almost no expression detected in brain, skeletal muscle, and kidney.
Yeast 2-hybrid binding analyses showed that through its core domain,
GAIP interacts strongly with GNAI3 and weakly with GNAI2 (139360), but
does not interact with GNA11 (139313).
GENE STRUCTURE
Sierra et al. (2002) determined that the RGS19 gene contains 5 exons.
MAPPING
By genomic sequence analysis, Sierra et al. (2002) mapped the RGS19 gene
to chromosome 20q13.3. They mapped the mouse Rgs19 gene to chromosome 2
by interspecific backcross mapping.
*FIELD* RF
1. De Vries, L.; Mousli, M.; Wurmser, A.; Farquhar, M. G.: GAIP,
a protein that specifically interacts with the trimeric G protein
G-alpha(i3), is a member of a protein family with a highly conserved
core domain. Proc. Nat. Acad. Sci. 92: 11916-11920, 1995.
2. 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.
*FIELD* CN
Patricia A. Hartz - updated: 9/12/2002
*FIELD* CD
Paul J. Converse: 6/23/2000
*FIELD* ED
alopez: 03/27/2012
mgross: 9/12/2002
mgross: 3/16/2001
mgross: 6/23/2000