GNAQ_HUMAN
ID GNAQ_HUMAN Reviewed; 359 AA.
AC P50148; O15108; Q13462; Q6NT27; Q92471; Q9BZB9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE AltName: Full=Guanine nucleotide-binding protein alpha-q;
GN Name=GNAQ; Synonyms=GAQ;
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].
RX PubMed=8825633; DOI=10.1006/geno.1995.1267;
RA Dong Q., Shenker A., Way J., Haddad B.R., Lin K., Hughes M.R.,
RA McBride W.O., Spiegel A.M., Battey J.;
RT "Molecular cloning of human G alpha q cDNA and chromosomal localization of
RT the G alpha q gene (GNAQ) and a processed pseudogene.";
RL Genomics 30:470-475(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Prostate;
RX PubMed=8664309; DOI=10.1016/0005-2736(96)00039-9;
RA Chen B., Leverette R.D., Schwinn D.A., Kwatra M.M.;
RT "Human G(alpha q): cDNA and tissue distribution.";
RL Biochim. Biophys. Acta 1281:125-128(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8836152; DOI=10.1042/bj3181023;
RA Johnson G.J., Leis L.A., Dunlop P.C.;
RT "Specificity of G alpha q and G alpha 11 gene expression in platelets and
RT erythrocytes. Expressions of cellular differentiation and species
RT differences.";
RL Biochem. J. 318:1023-1031(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9700850; DOI=10.1016/s0049-3848(98)00071-1;
RA Gabbeta J., Dhanasekaran N., Rao A.K.;
RT "G alpha q cDNA sequence from human platelets.";
RL Thromb. Res. 91:29-32(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bai X.H., Acharya R., Rivera C., Murtagh J.J.;
RT "Nucleotide sequence of human Gq guanine nucleotide binding protein.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-235.
RC TISSUE=Brain cortex;
RX PubMed=1333286; DOI=10.1016/0006-3223(92)90070-g;
RA Lesch K.-P., Manji H.K.;
RT "Signal-transducing G proteins and antidepressant drugs: evidence for
RT modulation of alpha subunit gene expression in rat brain.";
RL Biol. Psychiatry 32:549-579(1992).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-337.
RC TISSUE=Hematopoietic;
RX PubMed=7492305; DOI=10.1042/bj3120151;
RA Thomas C.P., Dunn M.J., Mattera R.;
RT "Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl
RT sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated
RT pathways.";
RL Biochem. J. 312:151-158(1995).
RN [12]
RP INTERACTION WITH SLC9A3R1.
RX PubMed=12193606; DOI=10.1074/jbc.m207910200;
RA Rochdi M.D., Watier V., La Madeleine C., Nakata H., Kozasa T.,
RA Parent J.-L.;
RT "Regulation of GTP-binding protein alpha q (Galpha q) signaling by the
RT ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50).";
RL J. Biol. Chem. 277:40751-40759(2002).
RN [13]
RP INTERACTION WITH PECAM1.
RX PubMed=18672896; DOI=10.1021/bi8003846;
RA Yeh J.C., Otte L.A., Frangos J.A.;
RT "Regulation of G protein-coupled receptor activities by the platelet-
RT endothelial cell adhesion molecule, PECAM-1.";
RL Biochemistry 47:9029-9039(2008).
RN [14]
RP PALMITOYLATION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=19001095; DOI=10.1128/mcb.01144-08;
RA Tsutsumi R., Fukata Y., Noritake J., Iwanaga T., Perez F., Fukata M.;
RT "Identification of G protein alpha subunit-palmitoylating enzyme.";
RL Mol. Cell. Biol. 29:435-447(2009).
RN [15]
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., Buerckstuemmer T.,
RA 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 [16]
RP TISSUE SPECIFICITY.
RX PubMed=21923740; DOI=10.1111/j.1365-3083.2011.02635.x;
RA Wang Y., Li Y., He Y., Sun Y., Sun W., Xie Q., Yin G., Du Y., Wang L.,
RA Shi G.;
RT "Expression of G protein alphaq subunit is decreased in lymphocytes from
RT rheumatoid arthritis patients and is correlated with disease activity.";
RL Scand. J. Immunol. 75:203-209(2012).
RN [17]
RP INTERACTION WITH GAS2L2.
RX PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT of the A2A adenosine receptor.";
RL Biochim. Biophys. Acta 1833:3145-3154(2013).
RN [18]
RP INVOLVEMENT IN CMC, VARIANT SWS GLN-183, AND CHARACTERIZATION OF VARIANT
RP SWS GLN-183.
RX PubMed=23656586; DOI=10.1056/nejmoa1213507;
RA Shirley M.D., Tang H., Gallione C.J., Baugher J.D., Frelin L.P., Cohen B.,
RA North P.E., Marchuk D.A., Comi A.M., Pevsner J.;
RT "Sturge-Weber syndrome and port-wine stains caused by somatic mutation in
RT GNAQ.";
RL N. Engl. J. Med. 368:1971-1979(2013).
RN [19]
RP DEAMIDATION AT GLN-209 (MICROBIAL INFECTION).
RX PubMed=24141704; DOI=10.1038/nsmb.2688;
RA Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
RA Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
RA Aktories K.;
RT "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation
RT of Gq and Gi proteins.";
RL Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP FUNCTION.
RX PubMed=27852822; DOI=10.1074/jbc.m116.754887;
RA Alvarez-Curto E., Inoue A., Jenkins L., Raihan S.Z., Prihandoko R.,
RA Tobin A.B., Milligan G.;
RT "Targeted Elimination of G Proteins and Arrestins Defines Their Specific
RT Contributions to Both Intensity and Duration of G Protein-coupled Receptor
RT Signaling.";
RL J. Biol. Chem. 291:27147-27159(2016).
RN [23]
RP CHARACTERIZATION OF VARIANT LEU-209.
RX PubMed=19078957; DOI=10.1038/nature07586;
RA Van Raamsdonk C.D., Bezrookove V., Green G., Bauer J., Gaugler L.,
RA O'Brien J.M., Simpson E.M., Barsh G.S., Bastian B.C.;
RT "Frequent somatic mutations of GNAQ in uveal melanoma and blue naevi.";
RL Nature 457:599-602(2009).
RN [24]
RP VARIANT GLN-183.
RX PubMed=22307269; DOI=10.1007/s00401-012-0948-x;
RA Murali R., Wiesner T., Rosenblum M.K., Bastian B.C.;
RT "GNAQ and GNA11 mutations in melanocytomas of the central nervous system.";
RL Acta Neuropathol. 123:457-459(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Required for platelet activation. Regulates B-cell selection
CC and survival and is required to prevent B-cell-dependent autoimmunity.
CC Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in
CC vitro) (By similarity). Transduces FFAR4 signaling in response to long-
CC chain fatty acids (LCFAs) (PubMed:27852822). Together with GNA11,
CC required for heart development (By similarity).
CC {ECO:0000250|UniProtKB:P21279, ECO:0000269|PubMed:27852822}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. Binds
CC SLC9A3R1 (PubMed:12193606). Forms a complex with PECAM1 and BDKRB2
CC (PubMed:18672896). Interacts with PECAM1. Interacts with GAS2L2
CC (PubMed:23994616). {ECO:0000269|PubMed:12193606,
CC ECO:0000269|PubMed:18672896, ECO:0000269|PubMed:23994616}.
CC -!- INTERACTION:
CC P50148; P49407: ARRB1; NbExp=2; IntAct=EBI-3909604, EBI-743313;
CC P50148; Q6DN90: IQSEC1; NbExp=2; IntAct=EBI-3909604, EBI-3044091;
CC P50148; Q969F8: KISS1R; NbExp=2; IntAct=EBI-3909604, EBI-8481408;
CC P50148; P10276: RARA; NbExp=4; IntAct=EBI-3909604, EBI-413374;
CC P50148; Q8R455: Trpm8; Xeno; NbExp=4; IntAct=EBI-3909604, EBI-15993527;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19001095};
CC Lipid-anchor {ECO:0000269|PubMed:19001095}. Golgi apparatus
CC {ECO:0000269|PubMed:19001095}. Nucleus {ECO:0000250|UniProtKB:P21279}.
CC Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Colocalizes with
CC the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane
CC of cardiac myocytes. {ECO:0000250|UniProtKB:P21279}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in ovary, prostate, testis
CC and colon. Down-regulated in the peripheral blood lymphocytes (PBLs) of
CC rheumatoid arthritis patients (at protein level).
CC {ECO:0000269|PubMed:21923740, ECO:0000269|PubMed:8664309}.
CC -!- PTM: Palmitoylated by ZDHHC3 and ZDHHC7 (PubMed:19001095).
CC Palmitoylation occurs in the Golgi and participates in the localization
CC of GNAQ to the plasma membrane (PubMed:19001095).
CC {ECO:0000269|PubMed:19001095}.
CC -!- PTM: (Microbial infection) Deamidated at Gln-209 by Photorhabdus
CC asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric
CC GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby
CC activating RhoA. {ECO:0000269|PubMed:24141704}.
CC -!- PTM: Histaminylated at Gln-209 residues by TGM2.
CC {ECO:0000250|UniProtKB:P21279}.
CC -!- DISEASE: Capillary malformations, congenital (CMC) [MIM:163000]: A form
CC of vascular malformations that are present from birth, tend to grow
CC with the individual, do not regress spontaneously, and show normal
CC rates of endothelial cell turnover. Capillary malformations are
CC distinct from capillary hemangiomas, which are highly proliferative
CC lesions that appear shortly after birth and show rapid growth, slow
CC involution, and endothelial hypercellularity.
CC {ECO:0000269|PubMed:23656586}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Sturge-Weber syndrome (SWS) [MIM:185300]: A syndrome
CC characterized by an intracranial vascular anomaly, leptomeningeal
CC angiomatosis, most often involving the occipital and posterior parietal
CC lobes. The most common features are facial cutaneous vascular
CC malformations (port-wine stains), seizures, and glaucoma. Stasis
CC results in ischemia underlying the leptomeningeal angiomatosis, leading
CC to calcification and laminar cortical necrosis. The clinical course is
CC highly variable and some children experience intractable seizures,
CC intellectual disability, and recurrent stroke-like episodes.
CC {ECO:0000269|PubMed:23656586}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GNAQID43280ch9q21.html";
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DR EMBL; U40038; AAC50363.1; -; mRNA.
DR EMBL; U43083; AAB06875.1; -; mRNA.
DR EMBL; L76256; AAB39498.1; -; mRNA.
DR EMBL; AF329284; AAG61117.1; -; mRNA.
DR EMBL; AF011496; AAB64301.1; -; mRNA.
DR EMBL; AF493896; AAM12610.1; -; mRNA.
DR EMBL; AL160268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62607.1; -; Genomic_DNA.
DR EMBL; BC057777; AAH57777.1; -; mRNA.
DR EMBL; BC067850; AAH67850.1; -; mRNA.
DR EMBL; BC069520; AAH69520.1; -; mRNA.
DR EMBL; BC075096; AAH75096.1; -; mRNA.
DR EMBL; BC075097; AAH75097.1; -; mRNA.
DR EMBL; L40629; AAA99950.1; -; mRNA.
DR CCDS; CCDS6658.1; -.
DR PIR; S59635; S59635.
DR PIR; S71963; S71963.
DR RefSeq; NP_002063.2; NM_002072.4.
DR PDB; 6VU5; EM; 3.50 A; B=1-359.
DR PDB; 7EZM; EM; 2.90 A; A=37-359.
DR PDB; 7F6H; EM; 2.90 A; B=2-359.
DR PDB; 7F6I; EM; 2.80 A; B=2-359.
DR PDB; 7F8W; EM; 3.10 A; A=29-359.
DR PDBsum; 6VU5; -.
DR PDBsum; 7EZM; -.
DR PDBsum; 7F6H; -.
DR PDBsum; 7F6I; -.
DR PDBsum; 7F8W; -.
DR AlphaFoldDB; P50148; -.
DR SMR; P50148; -.
DR BioGRID; 109038; 113.
DR CORUM; P50148; -.
DR DIP; DIP-41652N; -.
DR IntAct; P50148; 47.
DR MINT; P50148; -.
DR STRING; 9606.ENSP00000286548; -.
DR BindingDB; P50148; -.
DR ChEMBL; CHEMBL3286079; -.
DR iPTMnet; P50148; -.
DR PhosphoSitePlus; P50148; -.
DR SwissPalm; P50148; -.
DR BioMuta; GNAQ; -.
DR DMDM; 251757492; -.
DR EPD; P50148; -.
DR jPOST; P50148; -.
DR MassIVE; P50148; -.
DR MaxQB; P50148; -.
DR PaxDb; P50148; -.
DR PeptideAtlas; P50148; -.
DR PRIDE; P50148; -.
DR ProteomicsDB; 56198; -.
DR Antibodypedia; 4101; 291 antibodies from 36 providers.
DR DNASU; 2776; -.
DR Ensembl; ENST00000286548.9; ENSP00000286548.4; ENSG00000156052.11.
DR GeneID; 2776; -.
DR KEGG; hsa:2776; -.
DR MANE-Select; ENST00000286548.9; ENSP00000286548.4; NM_002072.5; NP_002063.2.
DR UCSC; uc004akw.5; human.
DR CTD; 2776; -.
DR DisGeNET; 2776; -.
DR GeneCards; GNAQ; -.
DR HGNC; HGNC:4390; GNAQ.
DR HPA; ENSG00000156052; Low tissue specificity.
DR MalaCards; GNAQ; -.
DR MIM; 163000; phenotype.
DR MIM; 185300; phenotype.
DR MIM; 600998; gene.
DR neXtProt; NX_P50148; -.
DR OpenTargets; ENSG00000156052; -.
DR Orphanet; 624; Familial multiple nevi flammei.
DR Orphanet; 79483; Phakomatosis cesioflammea.
DR Orphanet; 3205; Sturge-Weber syndrome.
DR Orphanet; 39044; Uveal melanoma.
DR PharmGKB; PA174; -.
DR VEuPathDB; HostDB:ENSG00000156052; -.
DR eggNOG; KOG0085; Eukaryota.
DR GeneTree; ENSGT00940000161347; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P50148; -.
DR OMA; AVTYLWN; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P50148; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; P50148; -.
DR Reactome; R-HSA-112043; PLC beta mediated events.
DR Reactome; R-HSA-202040; G-protein activation.
DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; P50148; -.
DR SIGNOR; P50148; -.
DR BioGRID-ORCS; 2776; 40 hits in 1045 CRISPR screens.
DR ChiTaRS; GNAQ; human.
DR GeneWiki; GNAQ; -.
DR GenomeRNAi; 2776; -.
DR Pharos; P50148; Tbio.
DR PRO; PR:P50148; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P50148; protein.
DR Bgee; ENSG00000156052; Expressed in CA1 field of hippocampus and 213 other tissues.
DR ExpressionAtlas; P50148; baseline and differential.
DR Genevisible; P50148; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001508; P:action potential; IBA:GO_Central.
DR GO; GO:0007202; P:activation of phospholipase C activity; TAS:ProtInc.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0009649; P:entrainment of circadian clock; ISS:AgBase.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:AgBase.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:BHF-UCL.
DR GO; GO:0007603; P:phototransduction, visible light; ISS:AgBase.
DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010543; P:regulation of platelet activation; ISS:UniProtKB.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00442; GPROTEINAQ.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cell membrane; Disease variant;
KW Golgi apparatus; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Nucleus; Palmitate; Reference proteome;
KW Transducer.
FT CHAIN 1..359
FT /note="Guanine nucleotide-binding protein G(q) subunit
FT alpha"
FT /id="PRO_0000203760"
FT DOMAIN 38..359
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 41..54
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 178..186
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 201..210
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 270..277
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 329..334
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P29992"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 180..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 274..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT MOD_RES 209
FT /note="5-glutamyl histamine"
FT /evidence="ECO:0000250|UniProtKB:P21279"
FT MOD_RES 209
FT /note="Deamidated glutamine; by Photorhabdus PAU_02230"
FT /evidence="ECO:0000269|PubMed:24141704"
FT LIPID 9
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21279"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21279"
FT VARIANT 183
FT /note="R -> Q (in SWS; found as somatic mosaic mutation in
FT CMC; also found in melanocytomas sample; somatic mutation;
FT shows significant activation of EPHB2 compared to control;
FT dbSNP:rs397514698)"
FT /evidence="ECO:0000269|PubMed:22307269,
FT ECO:0000269|PubMed:23656586"
FT /id="VAR_067270"
FT VARIANT 209
FT /note="Q -> L (found in blue naevi and uveal melanoma
FT samples; somatic mutation; constitutive activation;
FT dbSNP:rs121913492)"
FT /evidence="ECO:0000269|PubMed:19078957"
FT /id="VAR_067271"
FT VARIANT 355
FT /note="E -> D (in dbSNP:rs1059531)"
FT /id="VAR_059319"
FT CONFLICT 4
FT /note="E -> D (in Ref. 5; AAB64301)"
FT /evidence="ECO:0000305"
FT CONFLICT 28..29
FT /note="QL -> HV (in Ref. 1; AAC50363)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="R -> T (in Ref. 5; AAB64301)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="Y -> C (in Ref. 5; AAB64301)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="I -> N (in Ref. 2; AAB06875)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="I -> V (in Ref. 5; AAB64301)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="L -> A (in Ref. 3; AAB39498)"
FT /evidence="ECO:0000305"
FT HELIX 15..35
FT /evidence="ECO:0007829|PDB:7F6I"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:7F6I"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:7F6I"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7F6H"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:7F6I"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:7F6I"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:7F6I"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:7F6I"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:7F6I"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:7F6I"
FT TURN 240..244
FT /evidence="ECO:0007829|PDB:7F6I"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:7F6I"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:7F6I"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:7F6I"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:7F6I"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:7F6I"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:7F6I"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:7F6I"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:7F6I"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:7F6I"
FT HELIX 336..355
FT /evidence="ECO:0007829|PDB:7F6I"
SQ SEQUENCE 359 AA; 42142 MW; 6F69C4F617DFA7C7 CRC64;
MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP YKYEHNKAHA QLVREVDVEK
VSAFENPYVD AIKSLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRVADP AYLPTQQDVL
RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
