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Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (Adenylate cyclase-stimulating G alpha protein)

 GNAS2_HUMAN             Reviewed;         394 AA.
P63092; A6NI00; E1P5G5; P04895; Q12927; Q14433; Q32P26; Q5JWD2;
Q5JWD4; Q5JWD5; Q6NR75; Q6NXS0; Q8TBC0; Q96H70;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 155.
RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms short;
AltName: Full=Adenylate cyclase-stimulating G alpha protein;
Name=GNAS; Synonyms=GNAS1, GSP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GNAS-1 AND GNAS-2).
TISSUE=Liver;
PubMed=3093273; DOI=10.1016/0014-5793(86)81336-9;
Mattera R., Codina J., Crozat A., Kidd V., Woo S.L.C., Birnbaumer L.;
"Identification by molecular cloning of two forms of the alpha-subunit
of the human liver stimulatory (GS) regulatory component of adenylyl
cyclase.";
FEBS Lett. 206:36-42(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-1).
PubMed=3131741; DOI=10.1093/nar/16.8.3585;
Harris B.A.;
"Complete cDNA sequence of a human stimulatory GTP-binding protein
alpha subunit.";
Nucleic Acids Res. 16:3585-3585(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
GNAS-1 AND GNAS-2).
PubMed=3127824; DOI=10.1073/pnas.85.7.2081;
Kozasa T., Itoh H., Tsukamoto T., Kaziro Y.;
"Isolation and characterization of the human Gs alpha gene.";
Proc. Natl. Acad. Sci. U.S.A. 85:2081-2085(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GNAS-1 AND GNAS-2).
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GNAS-1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GNAS-1; 3 AND 4).
TISSUE=Bone marrow, Brain, Muscle, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-394 (ISOFORMS GNAS-1 AND 4).
PubMed=3024154; DOI=10.1073/pnas.83.23.8893;
Bray P., Carter A., Simons C., Guo V., Puckett C., Kamholz J.,
Spiegel A., Nirenberg M.;
"Human cDNA clones for four species of G alpha s signal transduction
protein.";
Proc. Natl. Acad. Sci. U.S.A. 83:8893-8897(1986).
[10]
PROTEIN SEQUENCE OF 187-199 AND 308-317.
TISSUE=Adipocyte;
PubMed=15242332; DOI=10.1042/BJ20040647;
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific
fragmentation of polymerase I and transcript release factor (PTRF) at
the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[11]
FUNCTION.
PubMed=12391161; DOI=10.1128/MCB.22.22.7942-7952.2002;
Pak Y., Pham N., Rotin D.;
"Direct binding of the beta1 adrenergic receptor to the cyclic AMP-
dependent guanine nucleotide exchange factor CNrasGEF leads to Ras
activation.";
Mol. Cell. Biol. 22:7942-7952(2002).
[12]
INTERACTION WITH ADCY5 AND ADCY6, AND FUNCTION.
PubMed=17110384; DOI=10.1074/jbc.M607522200;
Gao X., Sadana R., Dessauer C.W., Patel T.B.;
"Conditional stimulation of type V and VI adenylyl cyclases by G
protein betagamma subunits.";
J. Biol. Chem. 282:294-302(2007).
[13]
INTERACTION WITH CRY1.
PubMed=20852621; DOI=10.1038/nm.2214;
Zhang E.E., Liu Y., Dentin R., Pongsawakul P.Y., Liu A.C., Hirota T.,
Nusinow D.A., Sun X., Landais S., Kodama Y., Brenner D.A.,
Montminy M., Kay S.A.;
"Cryptochrome mediates circadian regulation of cAMP signaling and
hepatic gluconeogenesis.";
Nat. Med. 16:1152-1156(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PALMITOYLATION AT CYS-3.
PubMed=21044946; DOI=10.1194/jlr.D011106;
Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
Stamler J.S., Casey P.J.;
"Site-specific analysis of protein S-acylation by resin-assisted
capture.";
J. Lipid Res. 52:393-398(2011).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
INTERACTION WITH ADCY5, AND FUNCTION.
PubMed=26206488; DOI=10.1124/mol.115.099556;
Brand C.S., Sadana R., Malik S., Smrcka A.V., Dessauer C.W.;
"Adenylyl cyclase 5 regulation by Gbetagamma involves isoform specific
use of multiple interaction sites.";
Mol. Pharmacol. 88:758-767(2015).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
VARIANTS AHO PRO-99 AND CYS-165.
PubMed=8388883; DOI=10.1210/jcem.76.6.8388883;
Miric A., Vechio J.D., Levine M.A.;
"Heterogeneous mutations in the gene encoding the alpha-subunit of the
stimulatory G protein of adenylyl cyclase in Albright hereditary
osteodystrophy.";
J. Clin. Endocrinol. Metab. 76:1560-1568(1993).
[21]
VARIANT MAS HIS-201.
PubMed=1594625; DOI=10.1073/pnas.89.11.5152;
Schwindinger W.F., Francomano C.A., Levine M.A.;
"Identification of a mutation in the gene encoding the alpha subunit
of the stimulatory G protein of adenylyl cyclase in McCune-Albright
syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 89:5152-5156(1992).
[22]
VARIANTS MAS CYS-201 AND HIS-201.
PubMed=1944469; DOI=10.1056/NEJM199112123252403;
Weinstein L.S., Shenker A., Gejman P.V., Merino M.J., Friedman E.,
Spiegel A.M.;
"Activating mutations of the stimulatory G protein in the McCune-
Albright syndrome.";
N. Engl. J. Med. 325:1688-1695(1991).
[23]
VARIANTS SOMATOTROPHINOMA CYS-201; HIS-201 AND ARG-227.
PubMed=2549426; DOI=10.1038/340692a0;
Landis C.A., Masters S.B., Spada A., Pace A.M., Bourne H.R.,
Vallar L.;
"GTPase inhibiting mutations activate the alpha chain of Gs and
stimulate adenylyl cyclase in human pituitary tumours.";
Nature 340:692-696(1989).
[24]
VARIANT AHO HIS-385.
PubMed=7523385;
Schwindinger W.F., Miric A., Zimmerman D., Levine M.A.;
"A novel Gs alpha mutant in a patient with Albright hereditary
osteodystrophy uncouples cell surface receptors from adenylyl
cyclase.";
J. Biol. Chem. 269:25387-25391(1994).
[25]
CHARACTERIZATION OF VARIANT PHP1A SER-366.
PubMed=8072545; DOI=10.1038/371164a0;
Iiri T., Herzmark P., Nakamoto J.M., van Dop C., Bourne H.R.;
"Rapid GDP release from Gs alpha in patients with gain and loss of
endocrine function.";
Nature 371:164-168(1994).
[26]
VARIANT NON-MAS ENDOCRINE TUMORS LEU-201.
PubMed=7751320; DOI=10.1007/BF01366965;
Gorelov V.N., Dumon K., Barteneva N.S., Palm D., Roher H.-D.,
Goretzki P.E.;
"Overexpression of Gs alpha subunit in thyroid tumors bearing a
mutated Gs alpha gene.";
J. Cancer Res. Clin. Oncol. 121:219-224(1995).
[27]
VARIANT PITUITARY ADENOMA HIS-227.
PubMed=7737262; DOI=10.1111/j.1365-2362.1995.tb01537.x;
Williamson E.A., Ince P.G., Harrison D., Kendall-Taylor P.,
Harris P.E.;
"G-protein mutations in human pituitary adrenocorticotrophic hormone-
secreting adenomas.";
Eur. J. Clin. Invest. 25:128-131(1995).
[28]
VARIANT PITUITARY TUMOR SER-201.
PubMed=8766942; DOI=10.1530/eje.0.1340720;
Yang I., Park S., Ryu M., Woo J., Kim S., Kim J., Kim Y., Choi Y.;
"Characteristics of gsp-positive growth hormone-secreting pituitary
tumors in Korean acromegalic patients.";
Eur. J. Endocrinol. 134:720-726(1996).
[29]
CHARACTERIZATION OF VARIANT AHO HIS-231, AND FUNCTION.
PubMed=8702665; DOI=10.1074/jbc.271.33.19653;
Farfel Z., Iiri T., Shapira H., Roitman A., Mouallem M., Bourne H.R.;
"Pseudohypoparathyroidism, a novel mutation in the betagamma-contact
region of Gsalpha impairs receptor stimulation.";
J. Biol. Chem. 271:19653-19655(1996).
[30]
VARIANT POLYOSTOTIC FIBROUS DYSPLASIA SER-201.
PubMed=9267696; DOI=10.1016/S8756-3282(97)00107-5;
Candeliere G.A., Roughley P.J., Glorieux F.H.;
"Polymerase chain reaction-based technique for the selective
enrichment and analysis of mosaic arg201 mutations in G alpha s from
patients with fibrous dysplasia of bone.";
Bone 21:201-206(1997).
[31]
VARIANT AHO ARG-250.
PubMed=9328353; DOI=10.1210/mend.11.11.0013;
Warner D.R., Gejman P.V., Collins R.M., Weinstein L.S.;
"A novel mutation adjacent to the switch III domain of G(S alpha) in a
patient with pseudohypoparathyroidism.";
Mol. Endocrinol. 11:1718-1727(1997).
[32]
CHARACTERIZATION OF VARIANT AHO HIS-231.
PubMed=9159128; DOI=10.1073/pnas.94.11.5656;
Iiri T., Farfel Z., Bourne H.R.;
"Conditional activation defect of a human Gsalpha mutant.";
Proc. Natl. Acad. Sci. U.S.A. 94:5656-5661(1997).
[33]
VARIANT AHO TRP-258, MUTAGENESIS OF ARG-258, AND CHARACTERIZATION OF
VARIANT AHO TRP-258.
PubMed=9727013; DOI=10.1074/jbc.273.37.23976;
Warner D.R., Weng G., Yu S., Matalon R., Weinstein L.S.;
"A novel mutation in the switch 3 region of Gs-alpha in a patient with
Albright hereditary osteodystrophy impairs GDP binding and receptor
activation.";
J. Biol. Chem. 273:23976-23983(1998).
[34]
VARIANT MAS GLY-201.
PubMed=10571700; DOI=10.1359/jbmr.1999.14.11.1987;
Riminucci M., Fisher L.W., Majolagbe A., Corsi A., Lala R.,
De Sanctis C., Robey P.G., Bianco P.;
"A novel GNAS1 mutation, R201G, in McCune-albright syndrome.";
J. Bone Miner. Res. 14:1987-1989(1999).
[35]
MUTAGENESIS OF GLN-170 AND ARG-258.
PubMed=10200251; DOI=10.1073/pnas.96.8.4268;
Warner D.R., Weinstein L.S.;
"A mutation in the heterotrimeric stimulatory guanine nucleotide
binding protein alpha-subunit with impaired receptor-mediated
activation because of elevated GTPase activity.";
Proc. Natl. Acad. Sci. U.S.A. 96:4268-4272(1999).
[36]
INVOLVEMENT IN PHP1B.
PubMed=11067869; DOI=10.1172/JCI10431;
Liu J., Litman D., Rosenberg M.J., Yu S., Biesecker L.G.,
Weinstein L.S.;
"A GNAS1 imprinting defect in pseudohypoparathyroidism type IB.";
J. Clin. Invest. 106:1167-1174(2000).
[37]
INVOLVEMENT IN PHP1B.
PubMed=11294659; DOI=10.1086/320117;
Bastepe M., Lane A.H., Jueppner H.;
"Paternal uniparental isodisomy of chromosome 20q -- and the resulting
changes in GNAS1 methylation -- as a plausible cause of
pseudohypoparathyroidism.";
Am. J. Hum. Genet. 68:1283-1289(2001).
[38]
INVOLVEMENT IN PHP1B, VARIANT ILE-382 DEL, AND CHARACTERIZATION OF
VARIANT ILE-382 DEL.
PubMed=11029463; DOI=10.1074/jbc.M006032200;
Wu W.-I., Schwindinger W.F., Aparicio L.F., Levine M.A.;
"Selective resistance to parathyroid hormone caused by a novel
uncoupling mutation in the carboxyl terminus of G alpha(s). A cause of
pseudohypoparathyroidism type Ib.";
J. Biol. Chem. 276:165-171(2001).
[39]
VARIANT AHO HIS-231.
PubMed=11450852; DOI=10.1007/s100380170062;
Ishikawa Y., Tajima T., Nakae J., Nagashima T., Satoh K., Okuhara K.,
Fujieda K.;
"Two mutations of the Gsalpha gene in two Japanese patients with
sporadic pseudohypoparathyroidism type Ia.";
J. Hum. Genet. 46:426-430(2001).
[40]
VARIANT AHO LEU-115.
PubMed=11600516; DOI=10.1210/jcem.86.10.7946;
Ahrens W., Hiort O., Staedt P., Kirschner T., Marschke C., Kruse K.;
"Analysis of the GNAS1 gene in Albright's hereditary osteodystrophy.";
J. Clin. Endocrinol. Metab. 86:4630-4634(2001).
[41]
VARIANTS PHP1A ASN-156; MET-159 AND LYS-280.
PubMed=11788646; DOI=10.1210/jcem.87.1.8133;
Linglart A., Carel J.-C., Garabedian M., Le T., Mallet E.,
Kottler M.-L.;
"GNAS1 lesions in pseudohypoparathyroidism Ia and Ic: genotype
phenotype relationship and evidence of the maternal transmission of
the hormonal resistance.";
J. Clin. Endocrinol. Metab. 87:189-197(2002).
[42]
VARIANT PHP1A GLY-280.
PubMed=11926205; DOI=10.1515/JPEM.2002.15.3.259;
Lim S.H., Poh L.K., Cowell C.T., Tey B.H., Loke K.Y.;
"Mutational analysis of the GNAS1 exons encoding the stimulatory G
protein in five patients with pseudohypoparathyroidism type 1a.";
J. Pediatr. Endocrinol. Metab. 15:259-268(2002).
[43]
INVOLVEMENT IN PHP1B.
PubMed=12858292; DOI=10.1086/377136;
Jan de Beur S., Ding C., Germain-Lee E., Cho J., Maret A.,
Levine M.A.;
"Discordance between genetic and epigenetic defects in
pseudohypoparathyroidism type 1b revealed by inconsistent loss of
maternal imprinting at GNAS1.";
Am. J. Hum. Genet. 73:314-322(2003).
[44]
VARIANTS AHO ILE-242; SER-246 AND VAL-259.
PubMed=12624854; DOI=10.1086/374566;
Rickard S.J., Wilson L.C.;
"Analysis of GNAS1 and overlapping transcripts identifies the parental
origin of mutations in patients with sporadic Albright hereditary
osteodystrophy and reveals a model system in which to observe the
effects of splicing mutations on translated and untranslated messenger
RNA.";
Am. J. Hum. Genet. 72:961-974(2003).
[45]
VARIANT PHP1A ASN-338.
PubMed=12656668; DOI=10.1530/eje.0.1480463;
Pohlenz J., Ahrens W., Hiort O.;
"A new heterozygous mutation (L338N) in the human Gsalpha (GNAS1) gene
as a cause for congenital hypothyroidism in Albright's hereditary
osteodystrophy.";
Eur. J. Endocrinol. 148:463-468(2003).
[46]
VARIANTS AIMAH1 HIS-201 AND SER-201.
PubMed=12727968; DOI=10.1210/jc.2002-021362;
Fragoso M.C.B.V., Domenice S., Latronico A.C., Martin R.M.,
Pereira M.A.A., Zerbini M.C.N., Lucon A.M., Mendonca B.B.;
"Cushing's syndrome secondary to adrenocorticotropin-independent
macronodular adrenocortical hyperplasia due to activating mutations of
GNAS1 gene.";
J. Clin. Endocrinol. Metab. 88:2147-2151(2003).
[47]
INVOLVEMENT IN PHP1B.
PubMed=14561710; DOI=10.1172/JCI19159;
Bastepe M., Froehlich L.F., Hendy G.N., Indridason O.S., Josse R.G.,
Koshiyama H., Koerkkoe J., Nakamoto J.M., Rosenbloom A.L.,
Slyper A.H., Sugimoto T., Tsatsoulis A., Crawford J.D., Jueppner H.;
"Autosomal dominant pseudohypoparathyroidism type Ib is associated
with a heterozygous microdeletion that likely disrupts a putative
imprinting control element of GNAS.";
J. Clin. Invest. 112:1255-1263(2003).
[48]
VARIANT POH ARG-281.
PubMed=14723729; DOI=10.1111/j.1365-2230.2004.01439.x;
Chan I., Hamada T., Hardman C., McGrath J.A., Child F.J.;
"Progressive osseous heteroplasia resulting from a new mutation in the
GNAS1 gene.";
Clin. Exp. Dermatol. 29:77-80(2004).
[49]
INVOLVEMENT IN PHP1B.
PubMed=15800843; DOI=10.1086/429932;
Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.;
"A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism
type Ib redefines the boundaries of a cis-acting imprinting control
element of GNAS.";
Am. J. Hum. Genet. 76:804-814(2005).
[50]
VARIANT AHO/PHP1A SER-106.
PubMed=15817905; DOI=10.1530/eje.1.01879;
Riepe F.G., Ahrens W., Krone N., Foelster-Holst R., Brasch J.,
Sippell W.G., Hiort O., Partsch C.-J.;
"Early manifestation of calcinosis cutis in pseudohypoparathyroidism
type Ia associated with a novel mutation in the GNAS gene.";
Eur. J. Endocrinol. 152:515-519(2005).
[51]
INVOLVEMENT IN PHP1B.
PubMed=15592469; DOI=10.1038/ng1487;
Bastepe M., Froehlich L.F., Linglart A., Abu-Zahra H.S., Tojo K.,
Ward L.M., Jueppner H.;
"Deletion of the NESP55 differentially methylated region causes loss
of maternal GNAS imprints and pseudohypoparathyroidism type Ib.";
Nat. Genet. 37:25-27(2005).
[52]
VARIANTS PHP1C ARG-388 AND LYS-392, CHARACTERIZATION OF VARIANTS PHP1C
ARG-388 AND LYS-392, AND FUNCTION.
PubMed=21488135; DOI=10.1002/humu.21489;
Thiele S., de Sanctis L., Werner R., Grotzinger J., Aydin C.,
Juppner H., Bastepe M., Hiort O.;
"Functional characterization of GNAS mutations found in patients with
pseudohypoparathyroidism type Ic defines a new subgroup of
pseudohypoparathyroidism affecting selectively Gsalpha-receptor
interaction.";
Hum. Mutat. 32:653-660(2011).
-!- FUNCTION: Guanine nucleotide-binding proteins (G proteins)
function as transducers in numerous signaling pathways controlled
by G protein-coupled receptors (GPCRs) (PubMed:17110384).
Signaling involves the activation of adenylyl cyclases, resulting
in increased levels of the signaling molecule cAMP
(PubMed:26206488, PubMed:8702665). GNAS functions downstream of
several GPCRs, including beta-adrenergic receptors
(PubMed:21488135). Stimulates the Ras signaling pathway via
RAPGEF2 (PubMed:12391161). {ECO:0000269|PubMed:12391161,
ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:21488135,
ECO:0000269|PubMed:26206488, ECO:0000269|PubMed:8702665}.
-!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha,
beta and gamma. The alpha chain contains the guanine nucleotide
binding site. Interacts with CRY1; the interaction may block GPCR-
mediated regulation of cAMP concentrations (PubMed:20852621).
Interacts with ADCY5 and stimulates its adenylyl cyclase activity
(PubMed:17110384, PubMed:26206488). Interacts with ADCY6 and
stimulates its adenylyl cyclase activity (PubMed:17110384).
Interacts with ADCY2 (By similarity).
{ECO:0000250|UniProtKB:P04896, ECO:0000269|PubMed:17110384,
ECO:0000269|PubMed:20852621}.
-!- INTERACTION:
O89053:Coro1a (xeno); NbExp=2; IntAct=EBI-1047114, EBI-6665847;
P42866:Oprm1 (xeno); NbExp=2; IntAct=EBI-7607528, EBI-5282656;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P63094}; Lipid-anchor
{ECO:0000250|UniProtKB:P63094}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=Gnas-1; Synonyms=Alpha-S2, GNASl, Alpha-S-long;
IsoId=P63092-1, P04895-1;
Sequence=Displayed;
Name=Gnas-2; Synonyms=Alpha-S1, GNASs, Alpha-S-short;
IsoId=P63092-2, P04895-2;
Sequence=VSP_001833, VSP_001834;
Name=3;
IsoId=P63092-3; Sequence=VSP_026616, VSP_026617;
Note=No experimental confirmation available.;
Name=XLas-1;
IsoId=Q5JWF2-1; Sequence=External;
Note=Gene prediction confirmed by EST data.;
Name=XLas-2;
IsoId=Q5JWF2-2; Sequence=External;
Note=Gene prediction confirmed by EST data.;
Name=XLas-3;
IsoId=Q5JWF2-3; Sequence=External;
Name=Nesp55;
IsoId=O95467-1; Sequence=External;
Note=Shares no sequence similarity with other isoforms due to a
novel first exon containing the entire reading frame spliced to
shared exon 2 so that exons 2-13 make up the 3'-UTR.;
Name=4;
IsoId=P63092-4; Sequence=VSP_047325;
Note=Gene prediction based on EST data.;
-!- DISEASE: Albright hereditary osteodystrophy (AHO) [MIM:103580]: A
disorder characterized by short stature, obesity, round facies,
brachydactyly and subcutaneous calcification. It is often
associated with pseudohypoparathyoidism, hypocalcemia and elevated
PTH levels. {ECO:0000269|PubMed:11450852,
ECO:0000269|PubMed:11600516, ECO:0000269|PubMed:12624854,
ECO:0000269|PubMed:15817905, ECO:0000269|PubMed:7523385,
ECO:0000269|PubMed:8388883, ECO:0000269|PubMed:8702665,
ECO:0000269|PubMed:9159128, ECO:0000269|PubMed:9328353,
ECO:0000269|PubMed:9727013}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Pseudohypoparathyroidism 1A (PHP1A) [MIM:103580]: A
disorder characterized by end-organ resistance to parathyroid
hormone, hypocalcemia and hyperphosphatemia. It is commonly
associated with Albright hereditary osteodystrophy whose features
are short stature, obesity, round facies, short metacarpals and
ectopic calcification. {ECO:0000269|PubMed:11788646,
ECO:0000269|PubMed:11926205, ECO:0000269|PubMed:12656668,
ECO:0000269|PubMed:8072545}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: McCune-Albright syndrome (MAS) [MIM:174800]:
Characterized by polyostotic fibrous dysplasia, cafe-au-lait
lesions, and a variety of endocrine disorders, including
precocious puberty, hyperthyroidism, hypercortisolism, growth
hormone excess, and hyperprolactinemia. The mutations producing
MAS lead to constitutive activation of GS alpha.
{ECO:0000269|PubMed:10571700, ECO:0000269|PubMed:1594625,
ECO:0000269|PubMed:1944469, ECO:0000269|PubMed:7751320}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Pituitary adenoma, growth hormone-secreting, 1 (PAGH1)
[MIM:102200]: A growth hormone-secreting, benign neoplasm of the
anterior pituitary gland, also known as somatotropinoma. It
clinically results in acromegaly, a condition characterized by
coarse facial features, protruding jaw, and enlarged extremities.
Excessive production of growth hormone in children or adolescents
before the closure of epiphyses causes gigantism, a condition
characterized by abnormally tall stature. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Progressive osseous heteroplasia (POH) [MIM:166350]: Rare
autosomal dominant disorder characterized by extensive dermal
ossification during childhood, followed by disabling and
widespread heterotopic ossification of skeletal muscle and deep
connective tissue. {ECO:0000269|PubMed:14723729}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: ACTH-independent macronodular adrenal hyperplasia 1
(AIMAH1) [MIM:219080]: A rare adrenal defect characterized by
multiple, bilateral, non-pigmented, benign, adrenocortical
nodules. It results in excessive production of cortisol leading to
ACTH-independent Cushing syndrome. Clinical manifestations of
Cushing syndrome include facial and truncal obesity, abdominal
striae, muscular weakness, osteoporosis, arterial hypertension,
diabetes. {ECO:0000269|PubMed:12727968}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A
disorder characterized by end-organ resistance to parathyroid
hormone, hypocalcemia and hyperphosphatemia. Patients affected
with PHP1B lack developmental defects characteristic of Albright
hereditary osteodystrophy, and typically show no other endocrine
abnormalities besides resistance to PTH.
{ECO:0000269|PubMed:11029463, ECO:0000269|PubMed:11067869,
ECO:0000269|PubMed:11294659, ECO:0000269|PubMed:12858292,
ECO:0000269|PubMed:14561710, ECO:0000269|PubMed:15592469,
ECO:0000269|PubMed:15800843}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Most
affected individuals have defects in methylation of the gene. In
some cases microdeletions involving the STX16 appear to cause loss
of methylation at exon A/B of GNAS, resulting in PHP1B. Paternal
uniparental isodisomy have also been observed.
-!- DISEASE: GNAS hyperfunction (GNASHYP) [MIM:139320]: This condition
is characterized by increased trauma-related bleeding tendency,
prolonged bleeding time, brachydactyly and mental retardation.
Both the XLas isoforms and the ALEX protein are mutated which
strongly reduces the interaction between them and this may allow
unimpeded activation of the XLas isoforms. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Pseudohypoparathyroidism 1C (PHP1C) [MIM:612462]: A
disorder characterized by end-organ resistance to parathyroid
hormone, hypocalcemia and hyperphosphatemia. It is commonly
associated with Albright hereditary osteodystrophy whose features
are short stature, obesity, round facies, short metacarpals and
ectopic calcification. {ECO:0000269|PubMed:21488135}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: This protein is produced by a bicistronic gene
which also produces the ALEX protein from an overlapping reading
frame.
-!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner,
giving rise to distinct paternally, maternally and biallelically
expressed proteins. The XLas isoforms are paternally derived, the
Gnas isoforms are biallelically derived and the Nesp55 isoforms
are maternally derived.
-!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X04408; CAA27996.1; -; mRNA.
EMBL; X04409; CAA27997.1; -; mRNA.
EMBL; M21142; AAA53147.1; -; Genomic_DNA.
EMBL; M21139; AAA53147.1; JOINED; Genomic_DNA.
EMBL; M21740; AAA53147.1; JOINED; Genomic_DNA.
EMBL; M21140; AAA53147.1; JOINED; Genomic_DNA.
EMBL; M21741; AAA53147.1; JOINED; Genomic_DNA.
EMBL; M21141; AAA53147.1; JOINED; Genomic_DNA.
EMBL; M21142; AAA53146.1; -; Genomic_DNA.
EMBL; M21139; AAA53146.1; JOINED; Genomic_DNA.
EMBL; M21740; AAA53146.1; JOINED; Genomic_DNA.
EMBL; M21140; AAA53146.1; JOINED; Genomic_DNA.
EMBL; M21741; AAA53146.1; JOINED; Genomic_DNA.
EMBL; M21141; AAA53146.1; JOINED; Genomic_DNA.
EMBL; M21142; AAA53148.1; -; Genomic_DNA.
EMBL; M21139; AAA53148.1; JOINED; Genomic_DNA.
EMBL; M21141; AAA53148.1; JOINED; Genomic_DNA.
EMBL; M21740; AAA53148.1; JOINED; Genomic_DNA.
EMBL; M21741; AAA53148.1; JOINED; Genomic_DNA.
EMBL; M21142; AAA53149.1; -; Genomic_DNA.
EMBL; M21139; AAA53149.1; JOINED; Genomic_DNA.
EMBL; M21740; AAA53149.1; JOINED; Genomic_DNA.
EMBL; M21741; AAA53149.1; JOINED; Genomic_DNA.
EMBL; M21141; AAA53149.1; JOINED; Genomic_DNA.
EMBL; U12466; AAB60334.2; -; Genomic_DNA.
EMBL; X07036; CAA30084.1; -; mRNA.
EMBL; AF493897; AAM12611.1; -; mRNA.
EMBL; AF493898; AAM12612.1; -; mRNA.
EMBL; BT009905; AAP88907.1; -; mRNA.
EMBL; AL109840; CAI42914.1; -; Genomic_DNA.
EMBL; AL121917; CAI42914.1; JOINED; Genomic_DNA.
EMBL; AL109840; CAI42915.1; -; Genomic_DNA.
EMBL; AL121917; CAI42915.1; JOINED; Genomic_DNA.
EMBL; AL109840; CAI42916.1; -; Genomic_DNA.
EMBL; AL121917; CAI42916.1; JOINED; Genomic_DNA.
EMBL; AL109840; CAI42917.1; -; Genomic_DNA.
EMBL; AL121917; CAI42917.1; JOINED; Genomic_DNA.
EMBL; AL121917; CAI42546.1; -; Genomic_DNA.
EMBL; AL109840; CAI42546.1; JOINED; Genomic_DNA.
EMBL; AL121917; CAI42547.1; -; Genomic_DNA.
EMBL; AL109840; CAI42547.1; JOINED; Genomic_DNA.
EMBL; AL121917; CAI42548.1; -; Genomic_DNA.
EMBL; AL109840; CAI42548.1; JOINED; Genomic_DNA.
EMBL; AL121917; CAI42549.1; -; Genomic_DNA.
EMBL; AL109840; CAI42549.1; JOINED; Genomic_DNA.
EMBL; AL132655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75468.1; -; Genomic_DNA.
EMBL; CH471077; EAW75460.1; -; Genomic_DNA.
EMBL; CH471077; EAW75463.1; -; Genomic_DNA.
EMBL; BC002722; AAH02722.1; -; mRNA.
EMBL; BC008855; AAH08855.1; -; mRNA.
EMBL; BC066923; AAH66923.1; -; mRNA.
EMBL; BC022875; AAH22875.1; -; mRNA.
EMBL; BC104928; AAI04929.1; -; mRNA.
EMBL; BC108315; AAI08316.2; -; mRNA.
EMBL; M14631; AAA52583.1; -; mRNA.
CCDS; CCDS13472.1; -.
CCDS; CCDS42892.1; -. [P63092-3]
CCDS; CCDS46623.1; -. [P63092-4]
CCDS; CCDS46624.1; -. [P63092-2]
PIR; B31927; RGHUA2.
PIR; C31927; RGHUA1.
RefSeq; NP_000507.1; NM_000516.5. [P63092-1]
RefSeq; NP_001070956.1; NM_001077488.3. [P63092-4]
RefSeq; NP_001070957.1; NM_001077489.3. [P63092-3]
RefSeq; NP_001070958.1; NM_001077490.2.
RefSeq; NP_001296769.1; NM_001309840.1.
RefSeq; NP_536350.2; NM_080425.3.
RefSeq; NP_536351.1; NM_080426.3. [P63092-2]
UniGene; Hs.125898; -.
PDB; 5G53; X-ray; 3.40 A; C/D=26-60, C/D=204-394.
PDB; 5UZ7; EM; 4.10 A; A=1-394.
PDB; 5VAI; EM; 4.10 A; A=1-394.
PDBsum; 5G53; -.
PDBsum; 5UZ7; -.
PDBsum; 5VAI; -.
ProteinModelPortal; P63092; -.
SMR; P63092; -.
BioGrid; 109040; 91.
CORUM; P63092; -.
IntAct; P63092; 25.
MINT; MINT-262348; -.
ChEMBL; CHEMBL4377; -.
DrugBank; DB02587; Colforsin.
TCDB; 8.A.92.1.1; the g-protein AlphaBetaGama complex (gpc) family.
iPTMnet; P63092; -.
PhosphoSitePlus; P63092; -.
SwissPalm; P63092; -.
BioMuta; NPEPL1; -.
DMDM; 52000961; -.
EPD; P63092; -.
MaxQB; P63092; -.
PaxDb; P63092; -.
PeptideAtlas; P63092; -.
PRIDE; P63092; -.
DNASU; 2778; -.
Ensembl; ENST00000265620; ENSP00000265620; ENSG00000087460. [P63092-3]
Ensembl; ENST00000354359; ENSP00000346328; ENSG00000087460. [P63092-4]
Ensembl; ENST00000371085; ENSP00000360126; ENSG00000087460. [P63092-1]
Ensembl; ENST00000371095; ENSP00000360136; ENSG00000087460. [P63092-2]
GeneID; 2778; -.
KEGG; hsa:2778; -.
UCSC; uc002yaa.4; human.
CTD; 2778; -.
DisGeNET; 2778; -.
EuPathDB; HostDB:ENSG00000087460.23; -.
GeneCards; GNAS; -.
HGNC; HGNC:4392; GNAS.
HPA; CAB010337; -.
MalaCards; GNAS; -.
MIM; 102200; phenotype.
MIM; 103580; phenotype.
MIM; 139320; gene+phenotype.
MIM; 166350; phenotype.
MIM; 174800; phenotype.
MIM; 219080; phenotype.
MIM; 603233; phenotype.
MIM; 612462; phenotype.
neXtProt; NX_P63092; -.
OpenTargets; ENSG00000087460; -.
Orphanet; 562; McCune-Albright syndrome.
Orphanet; 93277; Monostotic fibrous dysplasia.
Orphanet; 93276; Polyostotic fibrous dysplasia.
Orphanet; 2762; Progressive osseous heteroplasia.
Orphanet; 79443; Pseudohypoparathyroidism type 1A.
Orphanet; 94089; Pseudohypoparathyroidism type 1B.
Orphanet; 79444; Pseudohypoparathyroidism type 1C.
Orphanet; 79445; Pseudopseudohypoparathyroidism.
PharmGKB; PA175; -.
eggNOG; KOG0099; Eukaryota.
eggNOG; ENOG410XPC4; LUCA.
GeneTree; ENSGT00770000120503; -.
HOGENOM; HOG000038729; -.
HOVERGEN; HBG063184; -.
KO; K04632; -.
OMA; TLWQDEG; -.
Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
Reactome; R-HSA-164378; PKA activation in glucagon signalling.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-HSA-392851; Prostacyclin signalling through prostacyclin receptor.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-418597; G alpha (z) signalling events.
Reactome; R-HSA-420092; Glucagon-type ligand receptors.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
SIGNOR; P63092; -.
ChiTaRS; GNAS; human.
GenomeRNAi; 2778; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000087460; -.
CleanEx; HS_GNAS; -.
ExpressionAtlas; P63092; baseline and differential.
Genevisible; P63092; HS.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005834; C:heterotrimeric G-protein complex; ISS:BHF-UCL.
GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004871; F:signal transducer activity; IDA:UniProtKB.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:UniProtKB.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0060348; P:bone development; IDA:UniProtKB.
GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:BHF-UCL.
GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL.
GO; GO:0050890; P:cognition; IDA:UniProtKB.
GO; GO:0048589; P:developmental growth; IDA:UniProtKB.
GO; GO:0060789; P:hair follicle placode formation; IDA:UniProtKB.
GO; GO:0046907; P:intracellular transport; NAS:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IDA:UniProtKB.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
GO; GO:0007608; P:sensory perception of smell; TAS:UniProtKB.
CDD; cd00066; G-alpha; 1.
Gene3D; 1.10.400.10; -; 1.
InterPro; IPR000367; Gprotein_alpha_S.
InterPro; IPR001019; Gprotein_alpha_su.
InterPro; IPR011025; GproteinA_insert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10218; PTHR10218; 1.
Pfam; PF00503; G-alpha; 1.
PRINTS; PR00318; GPROTEINA.
PRINTS; PR00443; GPROTEINAS.
SMART; SM00275; G_alpha; 1.
SUPFAM; SSF47895; SSF47895; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Alternative splicing; Cell membrane;
Complete proteome; Cushing syndrome; Direct protein sequencing;
Disease mutation; GTP-binding; Isopeptide bond; Lipoprotein;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Obesity;
Palmitate; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; Transducer; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P04896}.
CHAIN 2 394 Guanine nucleotide-binding protein G(s)
subunit alpha isoforms short.
/FTId=PRO_0000203721.
NP_BIND 47 55 GTP. {ECO:0000250|UniProtKB:P04896}.
NP_BIND 197 204 GTP. {ECO:0000250|UniProtKB:P04896}.
NP_BIND 223 227 GTP. {ECO:0000250|UniProtKB:P04896}.
NP_BIND 292 295 GTP. {ECO:0000250|UniProtKB:P04896}.
METAL 54 54 Magnesium.
{ECO:0000250|UniProtKB:P04896}.
METAL 204 204 Magnesium.
{ECO:0000250|UniProtKB:P04896}.
BINDING 366 366 GTP; via amide nitrogen.
{ECO:0000250|UniProtKB:P04896}.
MOD_RES 201 201 ADP-ribosylarginine; by cholera toxin.
{ECO:0000250}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
LIPID 2 2 N-palmitoyl glycine.
{ECO:0000250|UniProtKB:P04896}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:21044946}.
CROSSLNK 300 300 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 71 72 EG -> DS (in isoform Gnas-2).
{ECO:0000303|PubMed:3093273,
ECO:0000303|Ref.4}.
/FTId=VSP_001833.
VAR_SEQ 71 71 E -> D (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026616.
VAR_SEQ 72 86 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026617.
VAR_SEQ 73 86 Missing (in isoform Gnas-2).
{ECO:0000303|PubMed:3093273,
ECO:0000303|Ref.4}.
/FTId=VSP_001834.
VAR_SEQ 86 86 G -> GS (in isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3024154}.
/FTId=VSP_047325.
VARIANT 99 99 L -> P (in AHO; dbSNP:rs137854531).
{ECO:0000269|PubMed:8388883}.
/FTId=VAR_003439.
VARIANT 106 106 I -> S (in AHO/PHP1A).
{ECO:0000269|PubMed:15817905}.
/FTId=VAR_031872.
VARIANT 115 115 P -> L (in AHO; dbSNP:rs137854539).
{ECO:0000269|PubMed:11600516}.
/FTId=VAR_017843.
VARIANT 156 156 D -> N (in PHP1A).
{ECO:0000269|PubMed:11788646}.
/FTId=VAR_031873.
VARIANT 159 159 V -> M (in PHP1A).
{ECO:0000269|PubMed:11788646}.
/FTId=VAR_031874.
VARIANT 165 165 R -> C (in AHO; dbSNP:rs137854532).
{ECO:0000269|PubMed:8388883}.
/FTId=VAR_003440.
VARIANT 201 201 R -> C (in MAS; also found in
somatotrophinoma; dbSNP:rs11554273).
{ECO:0000269|PubMed:1944469,
ECO:0000269|PubMed:2549426}.
/FTId=VAR_003442.
VARIANT 201 201 R -> G (in MAS; dbSNP:rs11554273).
{ECO:0000269|PubMed:10571700}.
/FTId=VAR_017844.
VARIANT 201 201 R -> H (in MAS and AIMAH1; also found in
somatotrophinoma; dbSNP:rs121913495).
{ECO:0000269|PubMed:12727968,
ECO:0000269|PubMed:1594625,
ECO:0000269|PubMed:1944469,
ECO:0000269|PubMed:2549426}.
/FTId=VAR_003441.
VARIANT 201 201 R -> L (in non-MAS endocrine tumors;
dbSNP:rs121913495).
{ECO:0000269|PubMed:7751320}.
/FTId=VAR_017845.
VARIANT 201 201 R -> S (in AIMAH1; also found in
pituitary tumor and polyostotic fibrous
dysplasia; dbSNP:rs11554273).
{ECO:0000269|PubMed:12727968,
ECO:0000269|PubMed:8766942,
ECO:0000269|PubMed:9267696}.
/FTId=VAR_017846.
VARIANT 227 227 Q -> H (in pituitary adenomas; also found
in a patient with severe Cushing
syndrome; dbSNP:rs137854533).
{ECO:0000269|PubMed:7737262}.
/FTId=VAR_017847.
VARIANT 227 227 Q -> R (in somatotrophinoma;
dbSNP:rs121913494).
{ECO:0000269|PubMed:2549426}.
/FTId=VAR_003443.
VARIANT 231 231 R -> H (in AHO; impairs the ability to
mediate hormonal stimulation;
dbSNP:rs137854538).
{ECO:0000269|PubMed:11450852,
ECO:0000269|PubMed:8702665,
ECO:0000269|PubMed:9159128}.
/FTId=VAR_017848.
VARIANT 242 242 T -> I (in AHO).
{ECO:0000269|PubMed:12624854}.
/FTId=VAR_031875.
VARIANT 246 246 F -> S (in AHO).
{ECO:0000269|PubMed:12624854}.
/FTId=VAR_031876.
VARIANT 250 250 S -> R (in AHO; may alter guanine
nucleotide binding which could lead to
thermolability and impaired function;
dbSNP:rs137854534).
{ECO:0000269|PubMed:9328353}.
/FTId=VAR_017849.
VARIANT 258 258 R -> W (in AHO; defective GDP binding
resulting in increased thermolability and
decreased activation; dbSNP:rs137854535).
{ECO:0000269|PubMed:9727013}.
/FTId=VAR_015388.
VARIANT 259 259 E -> V (in AHO).
{ECO:0000269|PubMed:12624854}.
/FTId=VAR_031877.
VARIANT 280 280 R -> G (in PHP1A).
{ECO:0000269|PubMed:11926205}.
/FTId=VAR_031878.
VARIANT 280 280 R -> K (in PHP1A).
{ECO:0000269|PubMed:11788646}.
/FTId=VAR_031879.
VARIANT 281 281 W -> R (in POH).
{ECO:0000269|PubMed:14723729}.
/FTId=VAR_031880.
VARIANT 338 338 K -> N (in PHP1A).
{ECO:0000269|PubMed:12656668}.
/FTId=VAR_031881.
VARIANT 366 366 A -> S (in PHP1A; the patient also shows
testotoxicosis; constitutively activates
adenylyl cyclase in vitro; rapidly
degraded at 37 degrees resulting in loss
of Gs activity; dbSNP:rs137854537).
{ECO:0000269|PubMed:8072545}.
/FTId=VAR_017850.
VARIANT 380 380 R -> L (in dbSNP:rs8986).
/FTId=VAR_049358.
VARIANT 382 382 Missing (unable to interact with the
receptor for PTH).
{ECO:0000269|PubMed:11029463}.
/FTId=VAR_034744.
VARIANT 385 385 R -> H (in AHO; uncouples receptors from
adenylyl cyclases).
{ECO:0000269|PubMed:7523385}.
/FTId=VAR_003444.
VARIANT 388 388 L -> R (in PHP1C; significantly reduces
receptor-mediated activation; displays
normal receptor-independent activation;
dbSNP:rs397514457).
{ECO:0000269|PubMed:21488135}.
/FTId=VAR_066387.
VARIANT 392 392 E -> K (in PHP1C; significantly reduces
receptor-mediated activation; displays
normal receptor-independent activation;
dbSNP:rs397514456).
{ECO:0000269|PubMed:21488135}.
/FTId=VAR_066388.
MUTAGEN 170 170 Q->A: Increases GDP release but does not
affect receptor-mediated activation.
{ECO:0000269|PubMed:10200251}.
MUTAGEN 258 258 R->A: Increases GDP release and impairs
receptor-mediated activation; markedly
elevated intrinsic GTPase rate which will
lead to more rapid inactivation.
{ECO:0000269|PubMed:10200251,
ECO:0000269|PubMed:9727013}.
CONFLICT 3 3 C -> Y (in Ref. 8; AAH66923).
{ECO:0000305}.
CONFLICT 6 6 N -> T (in Ref. 3; CAA30084).
{ECO:0000305}.
CONFLICT 72 72 Missing (in Ref. 8; AAH66923).
{ECO:0000305}.
CONFLICT 167 167 N -> D (in Ref. 8; AAH22875).
{ECO:0000305}.
CONFLICT 230 230 E -> Q (in Ref. 9; AAA52583).
{ECO:0000305}.
STRAND 41 47 {ECO:0000244|PDB:5G53}.
HELIX 53 60 {ECO:0000244|PDB:5G53}.
STRAND 209 214 {ECO:0000244|PDB:5G53}.
STRAND 217 223 {ECO:0000244|PDB:5G53}.
STRAND 226 230 {ECO:0000244|PDB:5G53}.
HELIX 231 235 {ECO:0000244|PDB:5G53}.
STRAND 242 251 {ECO:0000244|PDB:5G53}.
HELIX 265 278 {ECO:0000244|PDB:5G53}.
TURN 281 284 {ECO:0000244|PDB:5G53}.
STRAND 286 292 {ECO:0000244|PDB:5G53}.
HELIX 294 303 {ECO:0000244|PDB:5G53}.
HELIX 308 311 {ECO:0000244|PDB:5G53}.
HELIX 313 317 {ECO:0000244|PDB:5G53}.
HELIX 332 351 {ECO:0000244|PDB:5G53}.
STRAND 359 363 {ECO:0000244|PDB:5G53}.
HELIX 371 390 {ECO:0000244|PDB:5G53}.
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


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