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 27-MAR-2024, entry version 214. 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 NHERF1. 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 NHERF1 CC (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; Q5T601: ADGRF1; NbExp=2; IntAct=EBI-3909604, EBI-46447105; 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="https://atlasgeneticsoncology.org/gene/43280/GNAQ"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7F6G; EM; 2.90 A; B=2-359. 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 PDB; 7W3Z; EM; 3.00 A; B=36-359. DR PDB; 7W40; EM; 3.00 A; B=36-359. DR PDB; 7XOW; EM; 3.10 A; A=36-359. DR PDB; 8G59; EM; 2.64 A; A=335-359. DR PDB; 8IA7; EM; 3.10 A; A=36-359. DR PDB; 8IYS; EM; 2.95 A; A=36-359. DR PDB; 8JPB; EM; 3.07 A; Q=37-359. DR PDB; 8JPC; EM; 3.07 A; Q=37-359. DR PDB; 8JPE; EM; 2.91 A; Q=37-359. DR PDB; 8UQN; EM; 3.40 A; A=7-359. DR PDB; 8UQO; EM; 3.37 A; A=7-359. DR PDBsum; 6VU5; -. DR PDBsum; 7EZM; -. DR PDBsum; 7F6G; -. DR PDBsum; 7F6H; -. DR PDBsum; 7F6I; -. DR PDBsum; 7F8W; -. DR PDBsum; 7W3Z; -. DR PDBsum; 7W40; -. DR PDBsum; 7XOW; -. DR PDBsum; 8G59; -. DR PDBsum; 8IA7; -. DR PDBsum; 8IYS; -. DR PDBsum; 8JPB; -. DR PDBsum; 8JPC; -. DR PDBsum; 8JPE; -. DR PDBsum; 8UQN; -. DR PDBsum; 8UQO; -. DR AlphaFoldDB; P50148; -. DR EMDB; EMD-21387; -. DR EMDB; EMD-31389; -. DR EMDB; EMD-31479; -. DR EMDB; EMD-31480; -. DR EMDB; EMD-31481; -. DR EMDB; EMD-31494; -. DR EMDB; EMD-32297; -. DR EMDB; EMD-32298; -. DR EMDB; EMD-33241; -. DR EMDB; EMD-33361; -. DR EMDB; EMD-33362; -. DR EMDB; EMD-35830; -. DR EMDB; EMD-36474; -. DR EMDB; EMD-36475; -. DR EMDB; EMD-36477; -. DR EMDB; EMD-41267; -. DR EMDB; EMD-41268; -. DR SMR; P50148; -. DR BioGRID; 109038; 115. DR CORUM; P50148; -. DR DIP; DIP-41652N; -. DR IntAct; P50148; 50. 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; 9606-ENSP00000286548; -. DR PeptideAtlas; P50148; -. DR ProteomicsDB; 56198; -. DR Pumba; P50148; -. DR Antibodypedia; 4101; 320 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 AGR; HGNC:4390; -. 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; EHQSEFY; -. DR OrthoDB; 2897309at2759; -. 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; 42 hits in 1129 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 215 other cell types or tissues. DR ExpressionAtlas; P50148; baseline and differential. 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: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:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central. 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; GI Alpha 1, domain 2-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR PANTHER; PTHR10218:SF316; GUANINE NUCLEOTIDE-BINDING PROTEIN G(Q) SUBUNIT ALPHA; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00442; GPROTEINAQ. DR SMART; SM00275; G_alpha; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1. DR PROSITE; PS51882; G_ALPHA; 1. DR Genevisible; P50148; HS. 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:7F6G" FT HELIX 52..62 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 69..96 FT /evidence="ECO:0007829|PDB:7F6G" FT HELIX 104..115 FT /evidence="ECO:0007829|PDB:7F6G" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:7F6G" FT HELIX 126..137 FT /evidence="ECO:0007829|PDB:7F6G" FT HELIX 139..146 FT /evidence="ECO:0007829|PDB:7F6G" FT TURN 147..150 FT /evidence="ECO:0007829|PDB:7F6G" FT HELIX 157..162 FT /evidence="ECO:0007829|PDB:7F6G" FT HELIX 164..168 FT /evidence="ECO:0007829|PDB:7F6G" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:7F6G" FT HELIX 176..181 FT /evidence="ECO:0007829|PDB:7F6G" 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 STRAND 299..301 FT /evidence="ECO:0007829|PDB:7XOW" 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..354 FT /evidence="ECO:0007829|PDB:8G59" FT TURN 355..357 FT /evidence="ECO:0007829|PDB:8G59" 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 //