ID GNAS2_HUMAN Reviewed; 394 AA. AC P63092; A6NI00; E1P5G5; P04895; Q12927; Q14433; Q32P26; Q5JWD2; Q5JWD4; AC Q5JWD5; Q6NR75; Q6NXS0; Q8TBC0; Q96H70; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 27-MAR-2024, entry version 199. DE RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms short; DE AltName: Full=Adenylate cyclase-stimulating G alpha protein; GN Name=GNAS; Synonyms=GNAS1, GSP; 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] (ISOFORMS GNAS-1 AND GNAS-2). RC TISSUE=Liver; RX PubMed=3093273; DOI=10.1016/0014-5793(86)81336-9; RA Mattera R., Codina J., Crozat A., Kidd V., Woo S.L.C., Birnbaumer L.; RT "Identification by molecular cloning of two forms of the alpha-subunit of RT the human liver stimulatory (GS) regulatory component of adenylyl RT cyclase."; RL FEBS Lett. 206:36-42(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-1). RX PubMed=3131741; DOI=10.1093/nar/16.8.3585; RA Harris B.A.; RT "Complete cDNA sequence of a human stimulatory GTP-binding protein alpha RT subunit."; RL Nucleic Acids Res. 16:3585-3585(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS RP GNAS-1 AND GNAS-2). RX PubMed=3127824; DOI=10.1073/pnas.85.7.2081; RA Kozasa T., Itoh H., Tsukamoto T., Kaziro Y.; RT "Isolation and characterization of the human Gs alpha gene."; RL Proc. Natl. Acad. Sci. U.S.A. 85:2081-2085(1988). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GNAS-1 AND GNAS-2). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GNAS-1). 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 vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [6] 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., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., 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., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [7] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GNAS-1; 3 AND 4). RC TISSUE=Bone marrow, Brain, Muscle, and Pancreas; 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-394 (ISOFORMS GNAS-1 AND 4). RX PubMed=3024154; DOI=10.1073/pnas.83.23.8893; RA Bray P., Carter A., Simons C., Guo V., Puckett C., Kamholz J., Spiegel A., RA Nirenberg M.; RT "Human cDNA clones for four species of G alpha s signal transduction RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8893-8897(1986). RN [10] RP PROTEIN SEQUENCE OF 187-199 AND 308-317. RC TISSUE=Adipocyte; RX PubMed=15242332; DOI=10.1042/bj20040647; RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.; RT "Vectorial proteomics reveal targeting, phosphorylation and specific RT fragmentation of polymerase I and transcript release factor (PTRF) at the RT surface of caveolae in human adipocytes."; RL Biochem. J. 383:237-248(2004). RN [11] RP FUNCTION. RX PubMed=12391161; DOI=10.1128/mcb.22.22.7942-7952.2002; RA Pak Y., Pham N., Rotin D.; RT "Direct binding of the beta1 adrenergic receptor to the cyclic AMP- RT dependent guanine nucleotide exchange factor CNrasGEF leads to Ras RT activation."; RL Mol. Cell. Biol. 22:7942-7952(2002). RN [12] RP INTERACTION WITH ADCY5 AND ADCY6, AND FUNCTION. RX PubMed=17110384; DOI=10.1074/jbc.m607522200; RA Gao X., Sadana R., Dessauer C.W., Patel T.B.; RT "Conditional stimulation of type V and VI adenylyl cyclases by G protein RT betagamma subunits."; RL J. Biol. Chem. 282:294-302(2007). RN [13] RP INTERACTION WITH CRY1. RX PubMed=20852621; DOI=10.1038/nm.2214; RA Zhang E.E., Liu Y., Dentin R., Pongsawakul P.Y., Liu A.C., Hirota T., RA Nusinow D.A., Sun X., Landais S., Kodama Y., Brenner D.A., Montminy M., RA Kay S.A.; RT "Cryptochrome mediates circadian regulation of cAMP signaling and hepatic RT gluconeogenesis."; RL Nat. Med. 16:1152-1156(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). 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 PALMITOYLATION AT CYS-3. RX PubMed=21044946; DOI=10.1194/jlr.d011106; RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., RA Stamler J.S., Casey P.J.; RT "Site-specific analysis of protein S-acylation by resin-assisted capture."; RL J. Lipid Res. 52:393-398(2011). RN [17] RP INTERACTION WITH GAS2L2, AND MUTAGENESIS OF GLN-227 AND ASP-295. 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 INTERACTION WITH SASH1. RX PubMed=23333244; DOI=10.1016/j.cellsig.2012.12.025; RA Zhou D., Wei Z., Deng S., Wang T., Zai M., Wang H., Guo L., Zhang J., RA Zhong H., He L., Xing Q.; RT "SASH1 regulates melanocyte transepithelial migration through a novel RT Galphas-SASH1-IQGAP1-E-cadherin dependent pathway."; RL Cell. Signal. 25:1526-1538(2013). RN [19] 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 [20] RP INTERACTION WITH ADCY5, AND FUNCTION. RX PubMed=26206488; DOI=10.1124/mol.115.099556; RA Brand C.S., Sadana R., Malik S., Smrcka A.V., Dessauer C.W.; RT "Adenylyl cyclase 5 regulation by Gbetagamma involves isoform specific use RT of multiple interaction sites."; RL Mol. Pharmacol. 88:758-767(2015). 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 VARIANTS AHO PRO-99 AND CYS-165. RX PubMed=8388883; DOI=10.1210/jcem.76.6.8388883; RA Miric A., Vechio J.D., Levine M.A.; RT "Heterogeneous mutations in the gene encoding the alpha-subunit of the RT stimulatory G protein of adenylyl cyclase in Albright hereditary RT osteodystrophy."; RL J. Clin. Endocrinol. Metab. 76:1560-1568(1993). RN [23] RP VARIANT MAS HIS-201. RX PubMed=1594625; DOI=10.1073/pnas.89.11.5152; RA Schwindinger W.F., Francomano C.A., Levine M.A.; RT "Identification of a mutation in the gene encoding the alpha subunit of the RT stimulatory G protein of adenylyl cyclase in McCune-Albright syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 89:5152-5156(1992). RN [24] RP VARIANTS MAS CYS-201 AND HIS-201. RX PubMed=1944469; DOI=10.1056/nejm199112123252403; RA Weinstein L.S., Shenker A., Gejman P.V., Merino M.J., Friedman E., RA Spiegel A.M.; RT "Activating mutations of the stimulatory G protein in the McCune-Albright RT syndrome."; RL N. Engl. J. Med. 325:1688-1695(1991). RN [25] RP VARIANTS SOMATOTROPHINOMA CYS-201; HIS-201 AND ARG-227. RX PubMed=2549426; DOI=10.1038/340692a0; RA Landis C.A., Masters S.B., Spada A., Pace A.M., Bourne H.R., Vallar L.; RT "GTPase inhibiting mutations activate the alpha chain of Gs and stimulate RT adenylyl cyclase in human pituitary tumours."; RL Nature 340:692-696(1989). RN [26] RP VARIANT AHO HIS-385. RX PubMed=7523385; DOI=10.1016/s0021-9258(18)47261-4; RA Schwindinger W.F., Miric A., Zimmerman D., Levine M.A.; RT "A novel Gs alpha mutant in a patient with Albright hereditary RT osteodystrophy uncouples cell surface receptors from adenylyl cyclase."; RL J. Biol. Chem. 269:25387-25391(1994). RN [27] RP CHARACTERIZATION OF VARIANT PHP1A SER-366. RX PubMed=8072545; DOI=10.1038/371164a0; RA Iiri T., Herzmark P., Nakamoto J.M., van Dop C., Bourne H.R.; RT "Rapid GDP release from Gs alpha in patients with gain and loss of RT endocrine function."; RL Nature 371:164-168(1994). RN [28] RP VARIANT NON-MAS ENDOCRINE TUMORS LEU-201. RX PubMed=7751320; DOI=10.1007/bf01366965; RA Gorelov V.N., Dumon K., Barteneva N.S., Palm D., Roher H.-D., RA Goretzki P.E.; RT "Overexpression of Gs alpha subunit in thyroid tumors bearing a mutated Gs RT alpha gene."; RL J. Cancer Res. Clin. Oncol. 121:219-224(1995). RN [29] RP VARIANT PITUITARY ADENOMA HIS-227. RX PubMed=7737262; DOI=10.1111/j.1365-2362.1995.tb01537.x; RA Williamson E.A., Ince P.G., Harrison D., Kendall-Taylor P., Harris P.E.; RT "G-protein mutations in human pituitary adrenocorticotrophic hormone- RT secreting adenomas."; RL Eur. J. Clin. Invest. 25:128-131(1995). RN [30] RP VARIANT PITUITARY TUMOR SER-201. RX PubMed=8766942; DOI=10.1530/eje.0.1340720; RA Yang I., Park S., Ryu M., Woo J., Kim S., Kim J., Kim Y., Choi Y.; RT "Characteristics of gsp-positive growth hormone-secreting pituitary tumors RT in Korean acromegalic patients."; RL Eur. J. Endocrinol. 134:720-726(1996). RN [31] RP CHARACTERIZATION OF VARIANT AHO HIS-231, AND FUNCTION. RX PubMed=8702665; DOI=10.1074/jbc.271.33.19653; RA Farfel Z., Iiri T., Shapira H., Roitman A., Mouallem M., Bourne H.R.; RT "Pseudohypoparathyroidism, a novel mutation in the betagamma-contact region RT of Gsalpha impairs receptor stimulation."; RL J. Biol. Chem. 271:19653-19655(1996). RN [32] RP VARIANT POLYOSTOTIC FIBROUS DYSPLASIA SER-201. RX PubMed=9267696; DOI=10.1016/s8756-3282(97)00107-5; RA Candeliere G.A., Roughley P.J., Glorieux F.H.; RT "Polymerase chain reaction-based technique for the selective enrichment and RT analysis of mosaic arg201 mutations in G alpha s from patients with fibrous RT dysplasia of bone."; RL Bone 21:201-206(1997). RN [33] RP VARIANT AHO ARG-250. RX PubMed=9328353; DOI=10.1210/mend.11.11.0013; RA Warner D.R., Gejman P.V., Collins R.M., Weinstein L.S.; RT "A novel mutation adjacent to the switch III domain of G(S alpha) in a RT patient with pseudohypoparathyroidism."; RL Mol. Endocrinol. 11:1718-1727(1997). RN [34] RP CHARACTERIZATION OF VARIANT AHO HIS-231. RX PubMed=9159128; DOI=10.1073/pnas.94.11.5656; RA Iiri T., Farfel Z., Bourne H.R.; RT "Conditional activation defect of a human Gsalpha mutant."; RL Proc. Natl. Acad. Sci. U.S.A. 94:5656-5661(1997). RN [35] RP VARIANT AHO TRP-258, MUTAGENESIS OF ARG-258, AND CHARACTERIZATION OF RP VARIANT AHO TRP-258. RX PubMed=9727013; DOI=10.1074/jbc.273.37.23976; RA Warner D.R., Weng G., Yu S., Matalon R., Weinstein L.S.; RT "A novel mutation in the switch 3 region of Gs-alpha in a patient with RT Albright hereditary osteodystrophy impairs GDP binding and receptor RT activation."; RL J. Biol. Chem. 273:23976-23983(1998). RN [36] RP VARIANT MAS GLY-201. RX PubMed=10571700; DOI=10.1359/jbmr.1999.14.11.1987; RA Riminucci M., Fisher L.W., Majolagbe A., Corsi A., Lala R., De Sanctis C., RA Robey P.G., Bianco P.; RT "A novel GNAS1 mutation, R201G, in McCune-albright syndrome."; RL J. Bone Miner. Res. 14:1987-1989(1999). RN [37] RP MUTAGENESIS OF GLN-170 AND ARG-258. RX PubMed=10200251; DOI=10.1073/pnas.96.8.4268; RA Warner D.R., Weinstein L.S.; RT "A mutation in the heterotrimeric stimulatory guanine nucleotide binding RT protein alpha-subunit with impaired receptor-mediated activation because of RT elevated GTPase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 96:4268-4272(1999). RN [38] RP INVOLVEMENT IN PHP1B. RX PubMed=11067869; DOI=10.1172/jci10431; RA Liu J., Litman D., Rosenberg M.J., Yu S., Biesecker L.G., Weinstein L.S.; RT "A GNAS1 imprinting defect in pseudohypoparathyroidism type IB."; RL J. Clin. Invest. 106:1167-1174(2000). RN [39] RP INVOLVEMENT IN PHP1B. RX PubMed=11294659; DOI=10.1086/320117; RA Bastepe M., Lane A.H., Jueppner H.; RT "Paternal uniparental isodisomy of chromosome 20q -- and the resulting RT changes in GNAS1 methylation -- as a plausible cause of RT pseudohypoparathyroidism."; RL Am. J. Hum. Genet. 68:1283-1289(2001). RN [40] RP INVOLVEMENT IN PHP1B, VARIANT ILE-382 DEL, AND CHARACTERIZATION OF VARIANT RP ILE-382 DEL. RX PubMed=11029463; DOI=10.1074/jbc.m006032200; RA Wu W.-I., Schwindinger W.F., Aparicio L.F., Levine M.A.; RT "Selective resistance to parathyroid hormone caused by a novel uncoupling RT mutation in the carboxyl terminus of G alpha(s). A cause of RT pseudohypoparathyroidism type Ib."; RL J. Biol. Chem. 276:165-171(2001). RN [41] RP VARIANT AHO HIS-231. RX PubMed=11450852; DOI=10.1007/s100380170062; RA Ishikawa Y., Tajima T., Nakae J., Nagashima T., Satoh K., Okuhara K., RA Fujieda K.; RT "Two mutations of the Gsalpha gene in two Japanese patients with sporadic RT pseudohypoparathyroidism type Ia."; RL J. Hum. Genet. 46:426-430(2001). RN [42] RP VARIANT AHO LEU-115. RX PubMed=11600516; DOI=10.1210/jcem.86.10.7946; RA Ahrens W., Hiort O., Staedt P., Kirschner T., Marschke C., Kruse K.; RT "Analysis of the GNAS1 gene in Albright's hereditary osteodystrophy."; RL J. Clin. Endocrinol. Metab. 86:4630-4634(2001). RN [43] RP VARIANTS PHP1A ASN-156; MET-159 AND LYS-280. RX PubMed=11788646; DOI=10.1210/jcem.87.1.8133; RA Linglart A., Carel J.-C., Garabedian M., Le T., Mallet E., Kottler M.-L.; RT "GNAS1 lesions in pseudohypoparathyroidism Ia and Ic: genotype phenotype RT relationship and evidence of the maternal transmission of the hormonal RT resistance."; RL J. Clin. Endocrinol. Metab. 87:189-197(2002). RN [44] RP VARIANT PHP1A GLY-280. RX PubMed=11926205; DOI=10.1515/jpem.2002.15.3.259; RA Lim S.H., Poh L.K., Cowell C.T., Tey B.H., Loke K.Y.; RT "Mutational analysis of the GNAS1 exons encoding the stimulatory G protein RT in five patients with pseudohypoparathyroidism type 1a."; RL J. Pediatr. Endocrinol. Metab. 15:259-268(2002). RN [45] RP INVOLVEMENT IN PHP1B. RX PubMed=12858292; DOI=10.1086/377136; RA Jan de Beur S., Ding C., Germain-Lee E., Cho J., Maret A., Levine M.A.; RT "Discordance between genetic and epigenetic defects in RT pseudohypoparathyroidism type 1b revealed by inconsistent loss of maternal RT imprinting at GNAS1."; RL Am. J. Hum. Genet. 73:314-322(2003). RN [46] RP VARIANTS AHO ILE-242; SER-246 AND VAL-259. RX PubMed=12624854; DOI=10.1086/374566; RA Rickard S.J., Wilson L.C.; RT "Analysis of GNAS1 and overlapping transcripts identifies the parental RT origin of mutations in patients with sporadic Albright hereditary RT osteodystrophy and reveals a model system in which to observe the effects RT of splicing mutations on translated and untranslated messenger RNA."; RL Am. J. Hum. Genet. 72:961-974(2003). RN [47] RP VARIANT PHP1A ASN-338. RX PubMed=12656668; DOI=10.1530/eje.0.1480463; RA Pohlenz J., Ahrens W., Hiort O.; RT "A new heterozygous mutation (L338N) in the human Gsalpha (GNAS1) gene as a RT cause for congenital hypothyroidism in Albright's hereditary RT osteodystrophy."; RL Eur. J. Endocrinol. 148:463-468(2003). RN [48] RP VARIANTS AIMAH1 HIS-201 AND SER-201. RX PubMed=12727968; DOI=10.1210/jc.2002-021362; RA Fragoso M.C.B.V., Domenice S., Latronico A.C., Martin R.M., Pereira M.A.A., RA Zerbini M.C.N., Lucon A.M., Mendonca B.B.; RT "Cushing's syndrome secondary to adrenocorticotropin-independent RT macronodular adrenocortical hyperplasia due to activating mutations of RT GNAS1 gene."; RL J. Clin. Endocrinol. Metab. 88:2147-2151(2003). RN [49] RP INVOLVEMENT IN PHP1B. RX PubMed=14561710; DOI=10.1172/jci19159; RA Bastepe M., Froehlich L.F., Hendy G.N., Indridason O.S., Josse R.G., RA Koshiyama H., Koerkkoe J., Nakamoto J.M., Rosenbloom A.L., Slyper A.H., RA Sugimoto T., Tsatsoulis A., Crawford J.D., Jueppner H.; RT "Autosomal dominant pseudohypoparathyroidism type Ib is associated with a RT heterozygous microdeletion that likely disrupts a putative imprinting RT control element of GNAS."; RL J. Clin. Invest. 112:1255-1263(2003). RN [50] RP VARIANT POH ARG-281. RX PubMed=14723729; DOI=10.1111/j.1365-2230.2004.01439.x; RA Chan I., Hamada T., Hardman C., McGrath J.A., Child F.J.; RT "Progressive osseous heteroplasia resulting from a new mutation in the RT GNAS1 gene."; RL Clin. Exp. Dermatol. 29:77-80(2004). RN [51] RP INVOLVEMENT IN PHP1B. RX PubMed=15800843; DOI=10.1086/429932; RA Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.; RT "A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type RT Ib redefines the boundaries of a cis-acting imprinting control element of RT GNAS."; RL Am. J. Hum. Genet. 76:804-814(2005). RN [52] RP VARIANT AHO/PHP1A SER-106. RX PubMed=15817905; DOI=10.1530/eje.1.01879; RA Riepe F.G., Ahrens W., Krone N., Foelster-Holst R., Brasch J., RA Sippell W.G., Hiort O., Partsch C.-J.; RT "Early manifestation of calcinosis cutis in pseudohypoparathyroidism type RT Ia associated with a novel mutation in the GNAS gene."; RL Eur. J. Endocrinol. 152:515-519(2005). RN [53] RP INVOLVEMENT IN PHP1B. RX PubMed=15592469; DOI=10.1038/ng1487; RA Bastepe M., Froehlich L.F., Linglart A., Abu-Zahra H.S., Tojo K., RA Ward L.M., Jueppner H.; RT "Deletion of the NESP55 differentially methylated region causes loss of RT maternal GNAS imprints and pseudohypoparathyroidism type Ib."; RL Nat. Genet. 37:25-27(2005). RN [54] RP VARIANTS PHP1C ARG-388 AND LYS-392, CHARACTERIZATION OF VARIANTS PHP1C RP ARG-388 AND LYS-392, AND FUNCTION. RX PubMed=21488135; DOI=10.1002/humu.21489; RA Thiele S., de Sanctis L., Werner R., Grotzinger J., Aydin C., Juppner H., RA Bastepe M., Hiort O.; RT "Functional characterization of GNAS mutations found in patients with RT pseudohypoparathyroidism type Ic defines a new subgroup of RT pseudohypoparathyroidism affecting selectively Gsalpha-receptor RT interaction."; RL Hum. Mutat. 32:653-660(2011). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as CC transducers in numerous signaling pathways controlled by G protein- CC coupled receptors (GPCRs) (PubMed:17110384). Signaling involves the CC activation of adenylyl cyclases, resulting in increased levels of the CC signaling molecule cAMP (PubMed:26206488, PubMed:8702665). GNAS CC functions downstream of several GPCRs, including beta-adrenergic CC receptors (PubMed:21488135). Stimulates the Ras signaling pathway via CC RAPGEF2 (PubMed:12391161). {ECO:0000269|PubMed:12391161, CC ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:21488135, CC ECO:0000269|PubMed:26206488, ECO:0000269|PubMed:8702665}. CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta CC and gamma. The alpha chain contains the guanine nucleotide binding CC site. Interacts with CRY1; the interaction may block GPCR-mediated CC regulation of cAMP concentrations (PubMed:20852621). Interacts with CC ADCY5 and stimulates its adenylyl cyclase activity (PubMed:17110384, CC PubMed:26206488). Interacts with ADCY6 and stimulates its adenylyl CC cyclase activity (PubMed:17110384). Interacts with ADCY2 (By CC similarity). Interaction with SASH1 (PubMed:23333244). Interacts with CC GAS2L2 (PubMed:23994616). {ECO:0000250|UniProtKB:P04896, CC ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:20852621, CC ECO:0000269|PubMed:23333244, ECO:0000269|PubMed:23994616}. CC -!- INTERACTION: CC P63092; O89053: Coro1a; Xeno; NbExp=2; IntAct=EBI-1047114, EBI-6665847; CC P63092-2; P42866: Oprm1; Xeno; NbExp=2; IntAct=EBI-7607528, EBI-5282656; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63094}; CC Lipid-anchor {ECO:0000250|UniProtKB:P63094}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=Gnas-1; Synonyms=Alpha-S2, GNASl, Alpha-S-long; CC IsoId=P63092-1, P04895-1; Sequence=Displayed; CC Name=Gnas-2; Synonyms=Alpha-S1, GNASs, Alpha-S-short; CC IsoId=P63092-2, P04895-2; Sequence=VSP_001833, VSP_001834; CC Name=3; CC IsoId=P63092-3; Sequence=VSP_026616, VSP_026617; CC Name=XLas-1; CC IsoId=Q5JWF2-1; Sequence=External; CC Name=XLas-2; CC IsoId=Q5JWF2-2; Sequence=External; CC Name=XLas-3; CC IsoId=Q5JWF2-3; Sequence=External; CC Name=Nesp55; CC IsoId=O95467-1; Sequence=External; CC Name=4; CC IsoId=P63092-4; Sequence=VSP_047325; CC -!- DISEASE: Albright hereditary osteodystrophy (AHO) [MIM:103580]: A CC disorder characterized by short stature, obesity, round facies, CC brachydactyly and subcutaneous calcification. It is often associated CC with pseudohypoparathyoidism, hypocalcemia and elevated PTH levels. CC {ECO:0000269|PubMed:11450852, ECO:0000269|PubMed:11600516, CC ECO:0000269|PubMed:12624854, ECO:0000269|PubMed:15817905, CC ECO:0000269|PubMed:7523385, ECO:0000269|PubMed:8388883, CC ECO:0000269|PubMed:8702665, ECO:0000269|PubMed:9159128, CC ECO:0000269|PubMed:9328353, ECO:0000269|PubMed:9727013}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Pseudohypoparathyroidism 1A (PHP1A) [MIM:103580]: A disorder CC characterized by end-organ resistance to parathyroid hormone, CC hypocalcemia and hyperphosphatemia. It is commonly associated with CC Albright hereditary osteodystrophy whose features are short stature, CC obesity, round facies, short metacarpals and ectopic calcification. CC {ECO:0000269|PubMed:21488135}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: McCune-Albright syndrome (MAS) [MIM:174800]: Characterized by CC polyostotic fibrous dysplasia, cafe-au-lait lesions, and a variety of CC endocrine disorders, including precocious puberty, hyperthyroidism, CC hypercortisolism, growth hormone excess, and hyperprolactinemia. The CC mutations producing MAS lead to constitutive activation of GS alpha. CC {ECO:0000269|PubMed:10571700, ECO:0000269|PubMed:1594625, CC ECO:0000269|PubMed:1944469, ECO:0000269|PubMed:7751320}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Progressive osseous heteroplasia (POH) [MIM:166350]: Rare CC autosomal dominant disorder characterized by extensive dermal CC ossification during childhood, followed by disabling and widespread CC heterotopic ossification of skeletal muscle and deep connective tissue. CC {ECO:0000269|PubMed:14723729}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: ACTH-independent macronodular adrenal hyperplasia 1 (AIMAH1) CC [MIM:219080]: A rare adrenal defect characterized by multiple, CC bilateral, non-pigmented, benign, adrenocortical nodules. It results in CC excessive production of cortisol leading to ACTH-independent Cushing CC syndrome. Clinical manifestations of Cushing syndrome include facial CC and truncal obesity, abdominal striae, muscular weakness, osteoporosis, CC arterial hypertension, diabetes. {ECO:0000269|PubMed:12727968}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A disorder CC characterized by end-organ resistance to parathyroid hormone, CC hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack CC developmental defects characteristic of Albright hereditary CC osteodystrophy, and typically show no other endocrine abnormalities CC besides resistance to PTH. {ECO:0000269|PubMed:11029463, CC ECO:0000269|PubMed:11067869, ECO:0000269|PubMed:11294659, CC ECO:0000269|PubMed:12858292, ECO:0000269|PubMed:14561710, CC ECO:0000269|PubMed:15592469, ECO:0000269|PubMed:15800843}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. Most affected individuals have defects in methylation of the CC gene. In some cases microdeletions involving the STX16 appear to cause CC loss of methylation at exon A/B of GNAS, resulting in PHP1B. Paternal CC uniparental isodisomy have also been observed. CC -!- DISEASE: GNAS hyperfunction (GNASHYP) [MIM:139320]: This condition is CC characterized by increased trauma-related bleeding tendency, prolonged CC bleeding time, brachydactyly and intellectual disability. Both the XLas CC isoforms and the ALEX protein are mutated which strongly reduces the CC interaction between them and this may allow unimpeded activation of the CC XLas isoforms. Note=The disease is caused by variants affecting the CC gene represented in this entry. CC -!- DISEASE: Pseudohypoparathyroidism 1C (PHP1C) [MIM:612462]: A disorder CC characterized by end-organ resistance to parathyroid hormone, CC hypocalcemia and hyperphosphatemia. It is commonly associated with CC Albright hereditary osteodystrophy whose features are short stature, CC obesity, round facies, short metacarpals and ectopic calcification. CC {ECO:0000269|PubMed:21488135}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which CC also produces the ALEX protein from an overlapping reading frame. CC -!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner, giving CC rise to distinct paternally, maternally and biallelically expressed CC proteins. The XLas isoforms are paternally derived, the Gnas isoforms CC are biallelically derived and the Nesp55 isoforms are maternally CC derived. CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily. CC {ECO:0000305}. 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; X04408; CAA27996.1; -; mRNA. DR EMBL; X04409; CAA27997.1; -; mRNA. DR EMBL; M21142; AAA53147.1; -; Genomic_DNA. DR EMBL; M21139; AAA53147.1; JOINED; Genomic_DNA. DR EMBL; M21740; AAA53147.1; JOINED; Genomic_DNA. DR EMBL; M21140; AAA53147.1; JOINED; Genomic_DNA. DR EMBL; M21741; AAA53147.1; JOINED; Genomic_DNA. DR EMBL; M21141; AAA53147.1; JOINED; Genomic_DNA. DR EMBL; M21142; AAA53146.1; -; Genomic_DNA. DR EMBL; M21139; AAA53146.1; JOINED; Genomic_DNA. DR EMBL; M21740; AAA53146.1; JOINED; Genomic_DNA. DR EMBL; M21140; AAA53146.1; JOINED; Genomic_DNA. DR EMBL; M21741; AAA53146.1; JOINED; Genomic_DNA. DR EMBL; M21141; AAA53146.1; JOINED; Genomic_DNA. DR EMBL; M21142; AAA53148.1; -; Genomic_DNA. DR EMBL; M21139; AAA53148.1; JOINED; Genomic_DNA. DR EMBL; M21141; AAA53148.1; JOINED; Genomic_DNA. DR EMBL; M21740; AAA53148.1; JOINED; Genomic_DNA. DR EMBL; M21741; AAA53148.1; JOINED; Genomic_DNA. DR EMBL; M21142; AAA53149.1; -; Genomic_DNA. DR EMBL; M21139; AAA53149.1; JOINED; Genomic_DNA. DR EMBL; M21740; AAA53149.1; JOINED; Genomic_DNA. DR EMBL; M21741; AAA53149.1; JOINED; Genomic_DNA. DR EMBL; M21141; AAA53149.1; JOINED; Genomic_DNA. DR EMBL; U12466; AAB60334.2; -; Genomic_DNA. DR EMBL; X07036; CAA30084.1; -; mRNA. DR EMBL; AF493897; AAM12611.1; -; mRNA. DR EMBL; AF493898; AAM12612.1; -; mRNA. DR EMBL; BT009905; AAP88907.1; -; mRNA. DR EMBL; AL109840; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121917; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL132655; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75468.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75460.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75463.1; -; Genomic_DNA. DR EMBL; BC002722; AAH02722.1; -; mRNA. DR EMBL; BC008855; AAH08855.1; -; mRNA. DR EMBL; BC066923; AAH66923.1; -; mRNA. DR EMBL; BC022875; AAH22875.1; -; mRNA. DR EMBL; BC104928; AAI04929.1; -; mRNA. DR EMBL; BC108315; AAI08316.2; -; mRNA. DR EMBL; M14631; AAA52583.1; -; mRNA. DR CCDS; CCDS13472.1; -. DR CCDS; CCDS42892.1; -. [P63092-3] DR CCDS; CCDS46623.1; -. [P63092-4] DR CCDS; CCDS46624.1; -. [P63092-2] DR PIR; B31927; RGHUA2. DR PIR; C31927; RGHUA1. DR RefSeq; NP_000507.1; NM_000516.5. [P63092-1] DR RefSeq; NP_001070956.1; NM_001077488.3. [P63092-4] DR RefSeq; NP_001070957.1; NM_001077489.3. [P63092-3] DR RefSeq; NP_001070958.1; NM_001077490.2. DR RefSeq; NP_001296769.1; NM_001309840.1. DR RefSeq; NP_536350.2; NM_080425.3. DR RefSeq; NP_536351.1; NM_080426.3. [P63092-2] DR PDB; 5G53; X-ray; 3.40 A; C/D=26-60, C/D=204-394. DR PDB; 5UZ7; EM; 4.10 A; A=1-394. DR PDB; 5VAI; EM; 4.10 A; A=1-394. DR PDB; 6AU6; X-ray; 1.70 A; A=7-394. DR PDB; 6B3J; EM; 3.30 A; A=1-394. DR PDB; 6E3Y; EM; 3.30 A; A=1-394. DR PDB; 6E67; X-ray; 3.70 A; A/B=381-393. DR PDB; 6EG8; X-ray; 2.80 A; I/J/K/L=4-394. DR PDB; 6GDG; EM; 4.11 A; D=6-64, D=204-394. DR PDB; 6LI3; EM; 3.32 A; A=6-64, A=204-394. DR PDB; 6LMK; EM; 3.70 A; A=1-394. DR PDB; 6LPB; EM; 3.90 A; A=5-394. DR PDB; 6M1H; EM; 3.60 A; F=1-394. DR PDB; 6M1I; EM; 3.50 A; F=1-394. DR PDB; 6NI3; EM; 3.80 A; A=1-394. DR PDB; 6NIY; EM; 3.34 A; A=1-394. DR PDB; 6ORV; EM; 3.00 A; AP=1-394. DR PDB; 6P9X; EM; 2.91 A; A=1-394. DR PDB; 6P9Y; EM; 3.01 A; A=1-394. DR PDB; 6PB0; EM; 3.00 A; A=1-67, A=208-394. DR PDB; 6PB1; EM; 2.80 A; A=1-67, A=208-394. DR PDB; 6UUN; EM; 3.00 A; A=1-394. DR PDB; 6UUS; EM; 2.40 A; A=1-394. DR PDB; 6UVA; EM; 2.30 A; A=1-394. DR PDB; 6VCB; EM; 3.30 A; A=1-394. DR PDB; 6VN7; EM; 3.20 A; A=1-394. DR PDB; 6WHC; EM; 3.40 A; A=1-394. DR PDB; 6WI9; EM; 4.30 A; A=1-394. DR PDB; 6WPW; EM; 3.10 A; C=1-394. DR PDB; 6WZG; EM; 2.30 A; A=1-394. DR PDB; 6X18; EM; 2.10 A; A=1-394. DR PDB; 6X19; EM; 2.10 A; A=1-394. DR PDB; 6X1A; EM; 2.50 A; A=1-394. DR PDB; 6XOX; EM; 3.10 A; A=27-394. DR PDB; 7AUE; EM; 2.97 A; A=1-394. DR PDB; 7BB6; EM; 4.20 A; E=1-394. DR PDB; 7BB7; EM; 4.40 A; E=1-394. DR PDB; 7BPH; X-ray; 1.57 A; A=7-394. DR PDB; 7BW0; EM; 3.90 A; A=26-394. DR PDB; 7BZ2; EM; 3.82 A; A=1-394. DR PDB; 7C2E; EM; 4.20 A; A=1-394. DR PDB; 7CFM; EM; 3.00 A; A=1-394. DR PDB; 7CFN; EM; 3.00 A; A=1-394. DR PDB; 7CKW; EM; 3.22 A; A=1-394. DR PDB; 7CKX; EM; 3.54 A; A=1-394. DR PDB; 7CKY; EM; 3.20 A; A=1-394. DR PDB; 7CKZ; EM; 3.10 A; A=1-394. DR PDB; 7CRH; EM; 3.30 A; A=1-394. DR PDB; 7CX2; EM; 2.80 A; A=1-394. DR PDB; 7CX3; EM; 2.80 A; A=1-394. DR PDB; 7CX4; EM; 2.90 A; A=1-394. DR PDB; 7CZ5; EM; 2.60 A; A=1-394. DR PDB; 7D3S; EM; 2.90 A; A=5-394. DR PDB; 7D7M; EM; 3.30 A; D=5-64, D=204-394. DR PDB; 7DH5; EM; 3.16 A; A=5-64, A=204-394. DR PDB; 7DHI; EM; 3.26 A; A=1-394. DR PDB; 7DHR; EM; 3.80 A; A=1-394. DR PDB; 7DUQ; EM; 2.50 A; A=1-394. DR PDB; 7DUR; EM; 3.30 A; A=1-394. DR PDB; 7DW9; EM; 2.60 A; A=27-67, A=205-251, A=266-394. DR PDB; 7E14; EM; 2.90 A; A=1-394. DR PDB; 7E5E; X-ray; 1.95 A; A/B/C/D=35-394. DR PDB; 7EPT; EM; 3.00 A; A=1-394. DR PDB; 7EVM; EM; 2.50 A; A=1-394. DR PDB; 7EVW; EM; 3.22 A; A=6-394. DR PDB; 7EZK; EM; 3.10 A; A=27-67, A=205-251, A=266-394. DR PDB; 7F0T; EM; 3.10 A; A=6-64, A=204-394. DR PDB; 7F16; EM; 2.80 A; A=1-394. DR PDB; 7F1O; EM; 3.13 A; A=6-64, A=204-394. DR PDB; 7F1Z; EM; 3.46 A; A=6-64, A=204-394. DR PDB; 7F23; EM; 3.58 A; A=6-64, A=204-394. DR PDB; 7F24; EM; 4.16 A; A=6-64, A=204-394. DR PDB; 7F4D; EM; 3.00 A; A=27-67, A=205-251, A=266-394. DR PDB; 7F4F; EM; 2.90 A; A=27-67, A=205-251, A=266-394. DR PDB; 7F4H; EM; 2.70 A; A=27-67, A=205-251, A=266-394. DR PDB; 7F4I; EM; 3.10 A; A=27-67, A=205-251, A=266-394. DR PDB; 7F53; EM; 3.00 A; A=1-394. DR PDB; 7F54; EM; 3.00 A; A=1-394. DR PDB; 7F55; EM; 3.10 A; A=1-394. DR PDB; 7F58; EM; 3.10 A; A=1-394. DR PDB; 7JOZ; X-ray; 3.80 A; A=1-394. DR PDB; 7JV5; EM; 3.00 A; A=2-394. DR PDB; 7JVP; EM; 2.90 A; A=2-394. DR PDB; 7JVQ; EM; 3.00 A; A=1-394. DR PDB; 7KH0; EM; 2.80 A; A=27-394. DR PDB; 7KI0; EM; 2.50 A; A=1-394. DR PDB; 7KI1; EM; 2.50 A; A=1-394. DR PDB; 7LCI; EM; 2.90 A; A=1-394. DR PDB; 7LJC; EM; 3.00 A; A=1-394. DR PDB; 7LJD; EM; 3.20 A; A=1-394. DR PDB; 7LLL; EM; 3.70 A; A=1-394. DR PDB; 7LLY; EM; 3.30 A; A=1-394. DR PDB; 7MBX; EM; 1.95 A; A=1-394. DR PDB; 7P02; EM; 2.87 A; A=204-251, A=266-394. DR PDB; 7PIU; EM; 2.58 A; A=1-394. DR PDB; 7PIV; EM; 2.86 A; A=1-394. DR PDB; 7RA3; EM; 3.24 A; A=27-394. DR PDB; 7RBT; EM; 3.08 A; A=26-394. DR PDB; 7RG9; EM; 3.20 A; A=26-394. DR PDB; 7RGP; EM; 2.90 A; A=27-394. DR PDB; 7RMH; EM; 3.10 A; A=6-64, A=204-394. DR PDB; 7RTB; EM; 2.14 A; A=1-394. DR PDB; 7S1M; EM; 2.41 A; A=1-394. DR PDB; 7S3I; EM; 2.51 A; A=1-394. DR PDB; 7T9I; EM; 2.90 A; X=204-394. DR PDB; 7T9N; EM; 2.90 A; X=204-394. DR PDB; 7TMW; EM; 3.20 A; R=204-394. DR PDB; 7TYF; EM; 2.20 A; A=1-394. DR PDB; 7TYH; EM; 3.30 A; A=1-394. DR PDB; 7TYI; EM; 3.30 A; A=1-394. DR PDB; 7TYL; EM; 3.30 A; A=1-394. DR PDB; 7TYN; EM; 2.60 A; A=1-394. DR PDB; 7TYO; EM; 2.70 A; A=1-394. DR PDB; 7TYW; EM; 3.00 A; A=1-394. DR PDB; 7TYX; EM; 2.55 A; A=1-394. DR PDB; 7TYY; EM; 3.00 A; A=1-394. DR PDB; 7TZF; EM; 2.40 A; A=1-394. DR PDB; 7UTZ; EM; 2.40 A; X=204-394. DR PDB; 7V35; EM; 3.40 A; A=1-394. DR PDB; 7V9L; EM; 2.60 A; A=27-67, A=205-251, A=266-394. DR PDB; 7V9M; EM; 3.29 A; A=1-394. DR PDB; 7VAB; EM; 3.20 A; A=27-67, A=205-251, A=266-394. DR PDB; 7VBH; EM; 3.00 A; A=1-394. DR PDB; 7VBI; EM; 3.00 A; A=12-394. DR PDB; 7VUH; EM; 3.22 A; A=5-64, A=204-371. DR PDB; 7VUI; EM; 3.30 A; A=5-64, A=204-371. DR PDB; 7VUJ; EM; 3.80 A; A=5-64, A=204-371. DR PDB; 7VVJ; EM; 3.20 A; A=5-394. DR PDB; 7VVK; EM; 3.30 A; A=5-394. DR PDB; 7VVL; EM; 2.80 A; A=5-394. DR PDB; 7VVM; EM; 3.20 A; A=5-394. DR PDB; 7VVN; EM; 3.80 A; A=5-394. DR PDB; 7VVO; EM; 4.10 A; A=5-394. DR PDB; 7WCM; EM; 2.33 A; A=1-394. DR PDB; 7WCN; EM; 2.87 A; A=1-394. DR PDB; 7WQ4; EM; 2.60 A; A=1-394. DR PDB; 7WU2; EM; 2.80 A; A=204-394. DR PDB; 7WU3; EM; 3.10 A; A=204-394. DR PDB; 7WUI; EM; 3.10 A; A=27-67, A=205-251, A=266-394. DR PDB; 7WUJ; EM; 3.30 A; A=27-67, A=205-251, A=266-394. DR PDB; 7WUQ; EM; 2.90 A; A=1-394. DR PDB; 7X2C; EM; 3.20 A; A=6-394. DR PDB; 7X2D; EM; 3.30 A; A=6-394. DR PDB; 7X2F; EM; 3.00 A; A=6-394. DR PDB; 7X8R; EM; 2.61 A; A=1-394. DR PDB; 7X8S; EM; 3.09 A; A=1-394. DR PDB; 7XJH; EM; 3.30 A; A=5-394. DR PDB; 7XJI; EM; 3.90 A; A=5-394. DR PDB; 7XKD; EM; 2.40 A; A=1-394. DR PDB; 7XKF; EM; 2.40 A; A=1-394. DR PDB; 7XOU; EM; 3.20 A; A=1-394. DR PDB; 7XOV; EM; 3.00 A; A=1-394. DR PDB; 7XP4; EM; 3.01 A; A=5-389. DR PDB; 7XP5; EM; 3.08 A; A=5-389. DR PDB; 7XP6; EM; 3.01 A; A=5-389. DR PDB; 7XT8; EM; 3.10 A; A=1-394. DR PDB; 7XT9; EM; 3.20 A; A=1-394. DR PDB; 7XTB; EM; 3.30 A; A=1-394. DR PDB; 7XTC; EM; 3.20 A; A=1-394. DR PDB; 7XTQ; EM; 3.20 A; A=1-394. DR PDB; 7XW6; EM; 2.78 A; A=6-394. DR PDB; 7XY6; EM; 2.99 A; A=151-190, A=204-394. DR PDB; 7XY7; EM; 3.26 A; A=151-190, A=204-394. DR PDB; 7XZ5; EM; 3.10 A; A=1-394. DR PDB; 7XZ6; EM; 2.80 A; A=1-394. DR PDB; 7Y35; EM; 2.90 A; A=1-394. DR PDB; 7Y36; EM; 2.80 A; A=1-394. DR PDB; 7Y3G; EM; 2.77 A; A=1-394. DR PDB; 7YP7; EM; 3.10 A; A=1-394. DR PDB; 8E3X; EM; 2.30 A; A=1-394. DR PDB; 8E3Y; EM; 2.30 A; A=1-394. DR PDB; 8E3Z; EM; 2.70 A; A=1-394. DR PDB; 8EL7; EM; 2.80 A; A=1-394. DR PDB; 8F0J; EM; 2.00 A; A=1-394. DR PDB; 8F0K; EM; 1.90 A; A=1-394. DR PDB; 8F2A; EM; 2.20 A; A=1-394. DR PDB; 8F2B; EM; 2.00 A; A=1-394. DR PDB; 8F76; EM; 3.10 A; X=5-64, X=204-394. DR PDB; 8FLQ; EM; 2.55 A; A=1-394. DR PDB; 8FLR; EM; 2.94 A; A=1-394. DR PDB; 8FLS; EM; 3.09 A; A=1-394. DR PDB; 8FLT; EM; 3.03 A; A=1-394. DR PDB; 8FLU; EM; 2.76 A; A=1-394. DR PDB; 8FU6; EM; 2.90 A; A=1-394. DR PDB; 8GW8; EM; 2.90 A; A=12-394. DR PDB; 8HDO; EM; 2.87 A; A=1-394. DR PDB; 8HDP; EM; 3.20 A; A=1-394. DR PDB; 8HIX; EM; 3.12 A; A=5-64, A=204-394. DR PDB; 8HJ0; EM; 3.12 A; A=5-64, A=204-381. DR PDB; 8HJ2; EM; 3.80 A; A=5-64, A=204-381. DR PDB; 8HMP; EM; 2.77 A; A=5-64, A=204-394. DR PDB; 8HMV; EM; 2.91 A; C=11-394. DR PDB; 8INR; EM; 2.73 A; A=27-67, A=205-251, A=266-394. DR PDB; 8IOC; EM; 2.86 A; A=27-67, A=205-251, A=266-394. DR PDB; 8IOD; EM; 2.59 A; A=27-67, A=205-251, A=266-394. DR PDB; 8IRV; EM; 3.10 A; A=27-67, A=205-251, A=266-394. DR PDB; 8IW7; EM; 2.97 A; A=27-67, A=205-251, A=266-394. DR PDB; 8IW9; EM; 3.08 A; A=27-67, A=205-251, A=266-394. DR PDB; 8IZB; EM; 3.06 A; A=1-394. DR PDB; 8JIT; EM; 2.91 A; A=1-394. DR PDB; 8JIU; EM; 2.76 A; A=1-394. DR PDB; 8JLO; EM; 3.52 A; A=1-394. DR PDB; 8JLZ; EM; 3.09 A; A=1-394. DR PDB; 8KGK; EM; 3.16 A; B=13-64, B=211-394. DR PDB; 8KH4; EM; 3.10 A; B=13-64, B=211-394. DR PDB; 8KH5; EM; 2.83 A; B=6-64, B=204-394. DR PDB; 8TB0; EM; 3.47 A; R=26-394. DR PDB; 8U26; EM; 2.50 A; A=204-394. DR PDB; 8W88; EM; 2.60 A; A=1-394. DR PDBsum; 5G53; -. DR PDBsum; 5UZ7; -. DR PDBsum; 5VAI; -. DR PDBsum; 6AU6; -. DR PDBsum; 6B3J; -. DR PDBsum; 6E3Y; -. DR PDBsum; 6E67; -. DR PDBsum; 6EG8; -. DR PDBsum; 6GDG; -. DR PDBsum; 6LI3; -. DR PDBsum; 6LMK; -. DR PDBsum; 6LPB; -. DR PDBsum; 6M1H; -. DR PDBsum; 6M1I; -. DR PDBsum; 6NI3; -. DR PDBsum; 6NIY; -. DR PDBsum; 6ORV; -. DR PDBsum; 6P9X; -. DR PDBsum; 6P9Y; -. DR PDBsum; 6PB0; -. DR PDBsum; 6PB1; -. DR PDBsum; 6UUN; -. DR PDBsum; 6UUS; -. DR PDBsum; 6UVA; -. DR PDBsum; 6VCB; -. DR PDBsum; 6VN7; -. DR PDBsum; 6WHC; -. DR PDBsum; 6WI9; -. DR PDBsum; 6WPW; -. DR PDBsum; 6WZG; -. DR PDBsum; 6X18; -. DR PDBsum; 6X19; -. DR PDBsum; 6X1A; -. DR PDBsum; 6XOX; -. DR PDBsum; 7AUE; -. DR PDBsum; 7BB6; -. DR PDBsum; 7BB7; -. DR PDBsum; 7BPH; -. DR PDBsum; 7BW0; -. DR PDBsum; 7BZ2; -. DR PDBsum; 7C2E; -. DR PDBsum; 7CFM; -. DR PDBsum; 7CFN; -. DR PDBsum; 7CKW; -. DR PDBsum; 7CKX; -. DR PDBsum; 7CKY; -. DR PDBsum; 7CKZ; -. DR PDBsum; 7CRH; -. DR PDBsum; 7CX2; -. DR PDBsum; 7CX3; -. DR PDBsum; 7CX4; -. DR PDBsum; 7CZ5; -. DR PDBsum; 7D3S; -. DR PDBsum; 7D7M; -. DR PDBsum; 7DH5; -. DR PDBsum; 7DHI; -. DR PDBsum; 7DHR; -. DR PDBsum; 7DUQ; -. DR PDBsum; 7DUR; -. DR PDBsum; 7DW9; -. DR PDBsum; 7E14; -. DR PDBsum; 7E5E; -. DR PDBsum; 7EPT; -. DR PDBsum; 7EVM; -. DR PDBsum; 7EVW; -. DR PDBsum; 7EZK; -. DR PDBsum; 7F0T; -. DR PDBsum; 7F16; -. DR PDBsum; 7F1O; -. DR PDBsum; 7F1Z; -. DR PDBsum; 7F23; -. DR PDBsum; 7F24; -. DR PDBsum; 7F4D; -. DR PDBsum; 7F4F; -. DR PDBsum; 7F4H; -. DR PDBsum; 7F4I; -. DR PDBsum; 7F53; -. DR PDBsum; 7F54; -. DR PDBsum; 7F55; -. DR PDBsum; 7F58; -. DR PDBsum; 7JOZ; -. DR PDBsum; 7JV5; -. DR PDBsum; 7JVP; -. DR PDBsum; 7JVQ; -. DR PDBsum; 7KH0; -. DR PDBsum; 7KI0; -. DR PDBsum; 7KI1; -. DR PDBsum; 7LCI; -. DR PDBsum; 7LJC; -. DR PDBsum; 7LJD; -. DR PDBsum; 7LLL; -. DR PDBsum; 7LLY; -. DR PDBsum; 7MBX; -. DR PDBsum; 7P02; -. DR PDBsum; 7PIU; -. DR PDBsum; 7PIV; -. DR PDBsum; 7RA3; -. DR PDBsum; 7RBT; -. DR PDBsum; 7RG9; -. DR PDBsum; 7RGP; -. DR PDBsum; 7RMH; -. DR PDBsum; 7RTB; -. DR PDBsum; 7S1M; -. DR PDBsum; 7S3I; -. DR PDBsum; 7T9I; -. DR PDBsum; 7T9N; -. DR PDBsum; 7TMW; -. DR PDBsum; 7TYF; -. DR PDBsum; 7TYH; -. DR PDBsum; 7TYI; -. DR PDBsum; 7TYL; -. DR PDBsum; 7TYN; -. DR PDBsum; 7TYO; -. DR PDBsum; 7TYW; -. DR PDBsum; 7TYX; -. DR PDBsum; 7TYY; -. DR PDBsum; 7TZF; -. DR PDBsum; 7UTZ; -. DR PDBsum; 7V35; -. DR PDBsum; 7V9L; -. DR PDBsum; 7V9M; -. DR PDBsum; 7VAB; -. DR PDBsum; 7VBH; -. DR PDBsum; 7VBI; -. DR PDBsum; 7VUH; -. DR PDBsum; 7VUI; -. DR PDBsum; 7VUJ; -. DR PDBsum; 7VVJ; -. DR PDBsum; 7VVK; -. DR PDBsum; 7VVL; -. DR PDBsum; 7VVM; -. DR PDBsum; 7VVN; -. DR PDBsum; 7VVO; -. DR PDBsum; 7WCM; -. DR PDBsum; 7WCN; -. DR PDBsum; 7WQ4; -. DR PDBsum; 7WU2; -. DR PDBsum; 7WU3; -. DR PDBsum; 7WUI; -. DR PDBsum; 7WUJ; -. DR PDBsum; 7WUQ; -. DR PDBsum; 7X2C; -. DR PDBsum; 7X2D; -. DR PDBsum; 7X2F; -. DR PDBsum; 7X8R; -. DR PDBsum; 7X8S; -. DR PDBsum; 7XJH; -. DR PDBsum; 7XJI; -. DR PDBsum; 7XKD; -. DR PDBsum; 7XKF; -. DR PDBsum; 7XOU; -. DR PDBsum; 7XOV; -. DR PDBsum; 7XP4; -. DR PDBsum; 7XP5; -. DR PDBsum; 7XP6; -. DR PDBsum; 7XT8; -. DR PDBsum; 7XT9; -. DR PDBsum; 7XTB; -. DR PDBsum; 7XTC; -. DR PDBsum; 7XTQ; -. DR PDBsum; 7XW6; -. DR PDBsum; 7XY6; -. DR PDBsum; 7XY7; -. DR PDBsum; 7XZ5; -. DR PDBsum; 7XZ6; -. DR PDBsum; 7Y35; -. DR PDBsum; 7Y36; -. DR PDBsum; 7Y3G; -. DR PDBsum; 7YP7; -. DR PDBsum; 8E3X; -. DR PDBsum; 8E3Y; -. DR PDBsum; 8E3Z; -. DR PDBsum; 8EL7; -. DR PDBsum; 8F0J; -. DR PDBsum; 8F0K; -. DR PDBsum; 8F2A; -. DR PDBsum; 8F2B; -. DR PDBsum; 8F76; -. DR PDBsum; 8FLQ; -. DR PDBsum; 8FLR; -. DR PDBsum; 8FLS; -. DR PDBsum; 8FLT; -. DR PDBsum; 8FLU; -. DR PDBsum; 8FU6; -. DR PDBsum; 8GW8; -. DR PDBsum; 8HDO; -. DR PDBsum; 8HDP; -. DR PDBsum; 8HIX; -. DR PDBsum; 8HJ0; -. DR PDBsum; 8HJ2; -. DR PDBsum; 8HMP; -. DR PDBsum; 8HMV; -. DR PDBsum; 8INR; -. DR PDBsum; 8IOC; -. DR PDBsum; 8IOD; -. DR PDBsum; 8IRV; -. DR PDBsum; 8IW7; -. DR PDBsum; 8IW9; -. DR PDBsum; 8IZB; -. DR PDBsum; 8JIT; -. DR PDBsum; 8JIU; -. DR PDBsum; 8JLO; -. DR PDBsum; 8JLZ; -. DR PDBsum; 8KGK; -. DR PDBsum; 8KH4; -. DR PDBsum; 8KH5; -. DR PDBsum; 8TB0; -. DR PDBsum; 8U26; -. DR PDBsum; 8W88; -. DR AlphaFoldDB; P63092; -. DR EMDB; EMD-0902; -. DR EMDB; EMD-0917; -. DR EMDB; EMD-0940; -. DR EMDB; EMD-11927; -. DR EMDB; EMD-12128; -. DR EMDB; EMD-12129; -. DR EMDB; EMD-13141; -. DR EMDB; EMD-17756; -. DR EMDB; EMD-20179; -. DR EMDB; EMD-20277; -. DR EMDB; EMD-20278; -. DR EMDB; EMD-20284; -. DR EMDB; EMD-20285; -. DR EMDB; EMD-20883; -. DR EMDB; EMD-20901; -. DR EMDB; EMD-20906; -. DR EMDB; EMD-21147; -. DR EMDB; EMD-21249; -. DR EMDB; EMD-21669; -. DR EMDB; EMD-21671; -. DR EMDB; EMD-21683; -. DR EMDB; EMD-21866; -. DR EMDB; EMD-21972; -. DR EMDB; EMD-21992; -. DR EMDB; EMD-21993; -. DR EMDB; EMD-21994; -. DR EMDB; EMD-22493; -. DR EMDB; EMD-22509; -. DR EMDB; EMD-22510; -. DR EMDB; EMD-22882; -. DR EMDB; EMD-22883; -. DR EMDB; EMD-23274; -. DR EMDB; EMD-23390; -. DR EMDB; EMD-23391; -. DR EMDB; EMD-23425; -. DR EMDB; EMD-23436; -. DR EMDB; EMD-23749; -. DR EMDB; EMD-24378; -. DR EMDB; EMD-24570; -. DR EMDB; EMD-24680; -. DR EMDB; EMD-24805; -. DR EMDB; EMD-24825; -. DR EMDB; EMD-24896; -. DR EMDB; EMD-24898; -. DR EMDB; EMD-24900; -. DR EMDB; EMD-25402; -. DR EMDB; EMD-25758; -. DR EMDB; EMD-25763; -. DR EMDB; EMD-26003; -. DR EMDB; EMD-26004; -. DR EMDB; EMD-26178; -. DR EMDB; EMD-26179; -. DR EMDB; EMD-26180; -. DR EMDB; EMD-26184; -. DR EMDB; EMD-26188; -. DR EMDB; EMD-26190; -. DR EMDB; EMD-26196; -. DR EMDB; EMD-26197; -. DR EMDB; EMD-26199; -. DR EMDB; EMD-26208; -. DR EMDB; EMD-26795; -. DR EMDB; EMD-27633; -. DR EMDB; EMD-27634; -. DR EMDB; EMD-27635; -. DR EMDB; EMD-27636; -. DR EMDB; EMD-27752; -. DR EMDB; EMD-27753; -. DR EMDB; EMD-27754; -. DR EMDB; EMD-27872; -. DR EMDB; EMD-27873; -. DR EMDB; EMD-27874; -. DR EMDB; EMD-27966; -. DR EMDB; EMD-27968; -. DR EMDB; EMD-27969; -. DR EMDB; EMD-28164; -. DR EMDB; EMD-28177; -. DR EMDB; EMD-28185; -. DR EMDB; EMD-28223; -. DR EMDB; EMD-28758; -. DR EMDB; EMD-28759; -. DR EMDB; EMD-28810; -. DR EMDB; EMD-28812; -. DR EMDB; EMD-28896; -. DR EMDB; EMD-29283; -. DR EMDB; EMD-29284; -. DR EMDB; EMD-29285; -. DR EMDB; EMD-29286; -. DR EMDB; EMD-29287; -. DR EMDB; EMD-29453; -. DR EMDB; EMD-30047; -. DR EMDB; EMD-30048; -. DR EMDB; EMD-30221; -. DR EMDB; EMD-30249; -. DR EMDB; EMD-30274; -. DR EMDB; EMD-30344; -. DR EMDB; EMD-30345; -. DR EMDB; EMD-30392; -. DR EMDB; EMD-30393; -. DR EMDB; EMD-30394; -. DR EMDB; EMD-30395; -. DR EMDB; EMD-30452; -. DR EMDB; EMD-30489; -. DR EMDB; EMD-30490; -. DR EMDB; EMD-30491; -. DR EMDB; EMD-30505; -. DR EMDB; EMD-30566; -. DR EMDB; EMD-30608; -. DR EMDB; EMD-30678; -. DR EMDB; EMD-30681; -. DR EMDB; EMD-30682; -. DR EMDB; EMD-30866; -. DR EMDB; EMD-30867; -. DR EMDB; EMD-30877; -. DR EMDB; EMD-31145; -. DR EMDB; EMD-31329; -. DR EMDB; EMD-31340; -. DR EMDB; EMD-31405; -. DR EMDB; EMD-31429; -. DR EMDB; EMD-31500; -. DR EMDB; EMD-31501; -. DR EMDB; EMD-31676; -. DR EMDB; EMD-31825; -. DR EMDB; EMD-31836; -. DR EMDB; EMD-31879; -. DR EMDB; EMD-31880; -. DR EMDB; EMD-32141; -. DR EMDB; EMD-32142; -. DR EMDB; EMD-32143; -. DR EMDB; EMD-32144; -. DR EMDB; EMD-32145; -. DR EMDB; EMD-32146; -. DR EMDB; EMD-32424; -. DR EMDB; EMD-32425; -. DR EMDB; EMD-32565; -. DR EMDB; EMD-32699; -. DR EMDB; EMD-32817; -. DR EMDB; EMD-32818; -. DR EMDB; EMD-32836; -. DR EMDB; EMD-32837; -. DR EMDB; EMD-32838; -. DR EMDB; EMD-32881; -. DR EMDB; EMD-32882; -. DR EMDB; EMD-32884; -. DR EMDB; EMD-32887; -. DR EMDB; EMD-32949; -. DR EMDB; EMD-32950; -. DR EMDB; EMD-33057; -. DR EMDB; EMD-33058; -. DR EMDB; EMD-33227; -. DR EMDB; EMD-33228; -. DR EMDB; EMD-33248; -. DR EMDB; EMD-33249; -. DR EMDB; EMD-33250; -. DR EMDB; EMD-33442; -. DR EMDB; EMD-33443; -. DR EMDB; EMD-33445; -. DR EMDB; EMD-33446; -. DR EMDB; EMD-33452; -. DR EMDB; EMD-33479; -. DR EMDB; EMD-33480; -. DR EMDB; EMD-33481; -. DR EMDB; EMD-33482; -. DR EMDB; EMD-33497; -. DR EMDB; EMD-33512; -. DR EMDB; EMD-33513; -. DR EMDB; EMD-33588; -. DR EMDB; EMD-33590; -. DR EMDB; EMD-33594; -. DR EMDB; EMD-33753; -. DR EMDB; EMD-33755; -. DR EMDB; EMD-33785; -. DR EMDB; EMD-33786; -. DR EMDB; EMD-33924; -. DR EMDB; EMD-33928; -. DR EMDB; EMD-33995; -. DR EMDB; EMD-34305; -. DR EMDB; EMD-34371; -. DR EMDB; EMD-34413; -. DR EMDB; EMD-34414; -. DR EMDB; EMD-34478; -. DR EMDB; EMD-34479; -. DR EMDB; EMD-34480; -. DR EMDB; EMD-34663; -. DR EMDB; EMD-34667; -. DR EMDB; EMD-34676; -. DR EMDB; EMD-34677; -. DR EMDB; EMD-34833; -. DR EMDB; EMD-34902; -. DR EMDB; EMD-34903; -. DR EMDB; EMD-35135; -. DR EMDB; EMD-35263; -. DR EMDB; EMD-35345; -. DR EMDB; EMD-35346; -. DR EMDB; EMD-35601; -. DR EMDB; EMD-35615; -. DR EMDB; EMD-35616; -. DR EMDB; EMD-35683; -. DR EMDB; EMD-35686; -. DR EMDB; EMD-35687; -. DR EMDB; EMD-35705; -. DR EMDB; EMD-35724; -. DR EMDB; EMD-35725; -. DR EMDB; EMD-35726; -. DR EMDB; EMD-35762; -. DR EMDB; EMD-35763; -. DR EMDB; EMD-35764; -. DR EMDB; EMD-35838; -. DR EMDB; EMD-36323; -. DR EMDB; EMD-36324; -. DR EMDB; EMD-36325; -. DR EMDB; EMD-36326; -. DR EMDB; EMD-36327; -. DR EMDB; EMD-36328; -. DR EMDB; EMD-36399; -. DR EMDB; EMD-36400; -. DR EMDB; EMD-36401; -. DR EMDB; EMD-36402; -. DR EMDB; EMD-36403; -. DR EMDB; EMD-36404; -. DR EMDB; EMD-36405; -. DR EMDB; EMD-36409; -. DR EMDB; EMD-36593; -. DR EMDB; EMD-36625; -. DR EMDB; EMD-37224; -. DR EMDB; EMD-37236; -. DR EMDB; EMD-37237; -. DR EMDB; EMD-37347; -. DR EMDB; EMD-37348; -. DR EMDB; EMD-37349; -. DR EMDB; EMD-37350; -. DR EMDB; EMD-37724; -. DR EMDB; EMD-41144; -. DR EMDB; EMD-41840; -. DR EMDB; EMD-4390; -. DR EMDB; EMD-7039; -. DR EMDB; EMD-8623; -. DR EMDB; EMD-8653; -. DR EMDB; EMD-8978; -. DR EMDB; EMD-9376; -. DR EMDB; EMD-9382; -. DR SMR; P63092; -. DR BioGRID; 109040; 243. DR CORUM; P63092; -. DR IntAct; P63092; 60. DR MINT; P63092; -. DR ChEMBL; CHEMBL4377; -. DR DrugBank; DB06843; 2',5'-DIDEOXY-ADENOSINE 3'-MONOPHOSPHATE. DR DrugBank; DB02587; Colforsin. DR TCDB; 8.A.92.1.1; the g-protein AlphaBetaGama complex (gpc) family. DR iPTMnet; P63092; -. DR PhosphoSitePlus; P63092; -. DR SwissPalm; P63092; -. DR BioMuta; GNAS; -. DR DMDM; 52000961; -. DR EPD; P63092; -. DR jPOST; P63092; -. DR MassIVE; P63092; -. DR MaxQB; P63092; -. DR PeptideAtlas; P63092; -. DR ProteomicsDB; 1235; -. DR ProteomicsDB; 57472; -. DR ProteomicsDB; 57473; -. [P63092-2] DR ProteomicsDB; 57474; -. [P63092-3] DR Pumba; P63092; -. DR Antibodypedia; 4152; 879 antibodies from 44 providers. DR DNASU; 2778; -. DR Ensembl; ENST00000265620.11; ENSP00000265620.7; ENSG00000087460.29. [P63092-3] DR Ensembl; ENST00000354359.12; ENSP00000346328.7; ENSG00000087460.29. [P63092-4] DR Ensembl; ENST00000371085.8; ENSP00000360126.3; ENSG00000087460.29. [P63092-1] DR Ensembl; ENST00000371095.7; ENSP00000360136.3; ENSG00000087460.29. [P63092-2] DR GeneID; 2778; -. DR KEGG; hsa:2778; -. DR MANE-Select; ENST00000371085.8; ENSP00000360126.3; NM_000516.7; NP_000507.1. DR UCSC; uc002yaa.4; human. DR AGR; HGNC:4392; -. DR CTD; 2778; -. DR DisGeNET; 2778; -. DR GeneCards; GNAS; -. DR GeneReviews; GNAS; -. DR HGNC; HGNC:4392; GNAS. DR HPA; ENSG00000087460; Low tissue specificity. DR MalaCards; GNAS; -. DR MIM; 103580; phenotype. DR MIM; 139320; gene+phenotype. DR MIM; 166350; phenotype. DR MIM; 174800; phenotype. DR MIM; 219080; phenotype. DR MIM; 603233; phenotype. DR MIM; 612462; phenotype. DR neXtProt; NX_P63092; -. DR OpenTargets; ENSG00000087460; -. DR Orphanet; 189427; Cushing syndrome due to bilateral macronodular adrenocortical disease. DR Orphanet; 57782; Mazabraud syndrome. DR Orphanet; 562; McCune-Albright syndrome. DR Orphanet; 93277; Monostotic fibrous dysplasia. DR Orphanet; 93276; Polyostotic fibrous dysplasia. DR Orphanet; 2762; Progressive osseous heteroplasia. DR Orphanet; 79443; Pseudohypoparathyroidism type 1A. DR Orphanet; 94089; Pseudohypoparathyroidism type 1B. DR Orphanet; 79444; Pseudohypoparathyroidism type 1C. DR Orphanet; 79445; Pseudopseudohypoparathyroidism. DR PharmGKB; PA175; -. DR VEuPathDB; HostDB:ENSG00000087460; -. DR GeneTree; ENSGT00940000156300; -. DR HOGENOM; CLU_014184_3_0_1; -. DR OMA; DHVAKCW; -. DR OrthoDB; 5264971at2759; -. DR PathwayCommons; P63092; -. DR Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation. DR Reactome; R-HSA-164378; PKA activation in glucagon signalling. DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-HSA-392851; Prostacyclin signalling through prostacyclin receptor. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-418597; G alpha (z) signalling events. DR Reactome; R-HSA-420092; Glucagon-type ligand receptors. DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-HSA-5610787; Hedgehog 'off' state. DR Reactome; R-HSA-9634597; GPER1 signaling. DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production. DR SignaLink; P63092; -. DR SIGNOR; P63092; -. DR BioGRID-ORCS; 2778; 33 hits in 1176 CRISPR screens. DR ChiTaRS; GNAS; human. DR GenomeRNAi; 2778; -. DR Pharos; P63092; Tbio. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000087460; Expressed in type B pancreatic cell and 215 other cell types or tissues. DR ExpressionAtlas; P63092; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISS:BHF-UCL. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB. DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB. DR GO; GO:0010856; F:adenylate cyclase activator activity; ISS:UniProtKB. DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:ARUK-UCL. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; TAS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:UniProtKB. DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0060348; P:bone development; IDA:UniProtKB. DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:BHF-UCL. DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL. DR GO; GO:0050890; P:cognition; IDA:UniProtKB. DR GO; GO:0048589; P:developmental growth; IDA:UniProtKB. DR GO; GO:0060789; P:hair follicle placode formation; IDA:UniProtKB. DR GO; GO:0046907; P:intracellular transport; NAS:UniProtKB. DR GO; GO:0070527; P:platelet aggregation; IDA:UniProtKB. DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB. DR GO; GO:0007608; P:sensory perception of smell; TAS: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; IPR000367; Gprotein_alpha_S. 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:SF365; GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA XL; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00443; GPROTEINAS. 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; P63092; HS. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Alternative splicing; Cell membrane; KW Cushing syndrome; Direct protein sequencing; Disease variant; Dwarfism; KW GTP-binding; Isopeptide bond; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Obesity; Palmitate; Phosphoprotein; KW Proto-oncogene; Reference proteome; Transducer; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P04896" FT CHAIN 2..394 FT /note="Guanine nucleotide-binding protein G(s) subunit FT alpha isoforms short" FT /id="PRO_0000203721" FT DOMAIN 39..394 FT /note="G-alpha" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 42..55 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 68..91 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 196..204 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 219..228 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 288..295 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 364..369 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT COMPBIAS 9..23 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 47..55 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P04896" FT BINDING 54 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P04896" FT BINDING 197..204 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P04896" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P04896" FT BINDING 223..227 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P04896" FT BINDING 292..295 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P04896" FT BINDING 366 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P04896" FT MOD_RES 201 FT /note="ADP-ribosylarginine; by cholera toxin" FT /evidence="ECO:0000250" FT MOD_RES 352 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT LIPID 2 FT /note="N-palmitoyl glycine" FT /evidence="ECO:0000250|UniProtKB:P04896" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:21044946" FT CROSSLNK 300 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT VAR_SEQ 71..72 FT /note="EG -> DS (in isoform Gnas-2)" FT /evidence="ECO:0000303|PubMed:3093273, ECO:0000303|Ref.4" FT /id="VSP_001833" FT VAR_SEQ 71 FT /note="E -> D (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026616" FT VAR_SEQ 72..86 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026617" FT VAR_SEQ 73..86 FT /note="Missing (in isoform Gnas-2)" FT /evidence="ECO:0000303|PubMed:3093273, ECO:0000303|Ref.4" FT /id="VSP_001834" FT VAR_SEQ 86 FT /note="G -> GS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:3024154" FT /id="VSP_047325" FT VARIANT 99 FT /note="L -> P (in AHO; dbSNP:rs137854531)" FT /evidence="ECO:0000269|PubMed:8388883" FT /id="VAR_003439" FT VARIANT 106 FT /note="I -> S (in AHO/PHP1A)" FT /evidence="ECO:0000269|PubMed:15817905" FT /id="VAR_031872" FT VARIANT 115 FT /note="P -> L (in AHO; dbSNP:rs137854539)" FT /evidence="ECO:0000269|PubMed:11600516" FT /id="VAR_017843" FT VARIANT 156 FT /note="D -> N (in PHP1A)" FT /evidence="ECO:0000269|PubMed:11788646" FT /id="VAR_031873" FT VARIANT 159 FT /note="V -> M (in PHP1A)" FT /evidence="ECO:0000269|PubMed:11788646" FT /id="VAR_031874" FT VARIANT 165 FT /note="R -> C (in AHO; dbSNP:rs137854532)" FT /evidence="ECO:0000269|PubMed:8388883" FT /id="VAR_003440" FT VARIANT 201 FT /note="R -> C (in MAS; also found in somatotrophinoma; FT dbSNP:rs11554273)" FT /evidence="ECO:0000269|PubMed:1944469, FT ECO:0000269|PubMed:2549426" FT /id="VAR_003442" FT VARIANT 201 FT /note="R -> G (in MAS; dbSNP:rs11554273)" FT /evidence="ECO:0000269|PubMed:10571700" FT /id="VAR_017844" FT VARIANT 201 FT /note="R -> H (in MAS and AIMAH1; also found in FT somatotrophinoma; dbSNP:rs121913495)" FT /evidence="ECO:0000269|PubMed:12727968, FT ECO:0000269|PubMed:1594625, ECO:0000269|PubMed:1944469, FT ECO:0000269|PubMed:2549426" FT /id="VAR_003441" FT VARIANT 201 FT /note="R -> L (in non-MAS endocrine tumors; FT dbSNP:rs121913495)" FT /evidence="ECO:0000269|PubMed:7751320" FT /id="VAR_017845" FT VARIANT 201 FT /note="R -> S (in AIMAH1; also found in pituitary tumor and FT polyostotic fibrous dysplasia; dbSNP:rs11554273)" FT /evidence="ECO:0000269|PubMed:12727968, FT ECO:0000269|PubMed:8766942, ECO:0000269|PubMed:9267696" FT /id="VAR_017846" FT VARIANT 227 FT /note="Q -> H (in pituitary adenomas; also found in a FT patient with severe Cushing syndrome; dbSNP:rs137854533)" FT /evidence="ECO:0000269|PubMed:7737262" FT /id="VAR_017847" FT VARIANT 227 FT /note="Q -> R (in somatotrophinoma; dbSNP:rs121913494)" FT /evidence="ECO:0000269|PubMed:2549426" FT /id="VAR_003443" FT VARIANT 231 FT /note="R -> H (in AHO; impairs the ability to mediate FT hormonal stimulation; dbSNP:rs137854538)" FT /evidence="ECO:0000269|PubMed:11450852, FT ECO:0000269|PubMed:8702665, ECO:0000269|PubMed:9159128" FT /id="VAR_017848" FT VARIANT 242 FT /note="T -> I (in AHO)" FT /evidence="ECO:0000269|PubMed:12624854" FT /id="VAR_031875" FT VARIANT 246 FT /note="F -> S (in AHO)" FT /evidence="ECO:0000269|PubMed:12624854" FT /id="VAR_031876" FT VARIANT 250 FT /note="S -> R (in AHO; may alter guanine nucleotide binding FT which could lead to thermolability and impaired function; FT dbSNP:rs137854534)" FT /evidence="ECO:0000269|PubMed:9328353" FT /id="VAR_017849" FT VARIANT 258 FT /note="R -> W (in AHO; defective GDP binding resulting in FT increased thermolability and decreased activation; FT dbSNP:rs137854535)" FT /evidence="ECO:0000269|PubMed:9727013" FT /id="VAR_015388" FT VARIANT 259 FT /note="E -> V (in AHO)" FT /evidence="ECO:0000269|PubMed:12624854" FT /id="VAR_031877" FT VARIANT 280 FT /note="R -> G (in PHP1A)" FT /evidence="ECO:0000269|PubMed:11926205" FT /id="VAR_031878" FT VARIANT 280 FT /note="R -> K (in PHP1A)" FT /evidence="ECO:0000269|PubMed:11788646" FT /id="VAR_031879" FT VARIANT 281 FT /note="W -> R (in POH)" FT /evidence="ECO:0000269|PubMed:14723729" FT /id="VAR_031880" FT VARIANT 338 FT /note="K -> N (in PHP1A)" FT /evidence="ECO:0000269|PubMed:12656668" FT /id="VAR_031881" FT VARIANT 366 FT /note="A -> S (in PHP1A; the patient also shows FT testotoxicosis; constitutively activates adenylyl cyclase FT in vitro; rapidly degraded at 37 degrees resulting in loss FT of Gs activity; dbSNP:rs137854537)" FT /evidence="ECO:0000269|PubMed:8072545" FT /id="VAR_017850" FT VARIANT 380 FT /note="R -> L (in dbSNP:rs8986)" FT /id="VAR_049358" FT VARIANT 382 FT /note="Missing (unable to interact with the receptor for FT PTH)" FT /evidence="ECO:0000269|PubMed:11029463" FT /id="VAR_034744" FT VARIANT 385 FT /note="R -> H (in AHO; uncouples receptors from adenylyl FT cyclases)" FT /evidence="ECO:0000269|PubMed:7523385" FT /id="VAR_003444" FT VARIANT 388 FT /note="L -> R (in PHP1C; significantly reduces FT receptor-mediated activation; displays normal FT receptor-independent activation; dbSNP:rs397514457)" FT /evidence="ECO:0000269|PubMed:21488135" FT /id="VAR_066387" FT VARIANT 392 FT /note="E -> K (in PHP1C; significantly reduces FT receptor-mediated activation; displays normal FT receptor-independent activation; dbSNP:rs397514456)" FT /evidence="ECO:0000269|PubMed:21488135" FT /id="VAR_066388" FT MUTAGEN 170 FT /note="Q->A: Increases GDP release but does not affect FT receptor-mediated activation." FT /evidence="ECO:0000269|PubMed:10200251" FT MUTAGEN 227 FT /note="Q->L: Increases binding to GAS2L2; when associated FT with N-295." FT /evidence="ECO:0000269|PubMed:23994616" FT MUTAGEN 258 FT /note="R->A: Increases GDP release and impairs FT receptor-mediated activation; markedly elevated intrinsic FT GTPase rate which will lead to more rapid inactivation." FT /evidence="ECO:0000269|PubMed:10200251, FT ECO:0000269|PubMed:9727013" FT MUTAGEN 295 FT /note="D->N: Increases binding to GAS2L2; when associated FT with L-227." FT /evidence="ECO:0000269|PubMed:23994616" FT CONFLICT 3 FT /note="C -> Y (in Ref. 8; AAH66923)" FT /evidence="ECO:0000305" FT CONFLICT 6 FT /note="N -> T (in Ref. 3; CAA30084)" FT /evidence="ECO:0000305" FT CONFLICT 72 FT /note="Missing (in Ref. 8; AAH66923)" FT /evidence="ECO:0000305" FT CONFLICT 167 FT /note="N -> D (in Ref. 8; AAH22875)" FT /evidence="ECO:0000305" FT CONFLICT 230 FT /note="E -> Q (in Ref. 9; AAA52583)" FT /evidence="ECO:0000305" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:7CKZ" FT HELIX 18..39 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 40..48 FT /evidence="ECO:0007829|PDB:7BPH" FT TURN 49..52 FT /evidence="ECO:0007829|PDB:7RTB" FT HELIX 53..64 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 92..112 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 125..133 FT /evidence="ECO:0007829|PDB:7BPH" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 144..154 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 157..163 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 164..168 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 175..179 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 194..199 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 206..214 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 217..224 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:7CFM" FT HELIX 228..237 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 243..249 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 250..254 FT /evidence="ECO:0007829|PDB:7BPH" FT TURN 258..260 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 265..277 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 287..292 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:7CKZ" FT HELIX 308..310 FT /evidence="ECO:0007829|PDB:7BPH" FT HELIX 313..317 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:7CZ5" FT STRAND 328..330 FT /evidence="ECO:0007829|PDB:7KI0" FT HELIX 332..349 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:6PB1" FT TURN 354..356 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 359..363 FT /evidence="ECO:0007829|PDB:7BPH" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:7CKZ" FT HELIX 369..393 FT /evidence="ECO:0007829|PDB:7BPH" SQ SEQUENCE 394 AA; 45665 MW; CD541181FC4412EF CRC64; MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK EAIETIVAAM SNLVPPVELA NPENQFRVDY ILSVMNVPDF DFPPEFYEHA KALWEDEGVR ACYERSNEYQ LIDCAQYFLD KIDVIKQADY VPSDQDLLRC RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND VTAIIFVVAS SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST ASGDGRHYCY PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL //