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Protein ALEX (Alternative gene product encoded by XL-exon)

 ALEX_HUMAN              Reviewed;         626 AA.
P84996; A2A2S4;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
05-DEC-2018, entry version 94.
RecName: Full=Protein ALEX;
AltName: Full=Alternative gene product encoded by XL-exon;
Name=GNAS {ECO:0000312|HGNC:HGNC:4392};
Synonyms=GNAS1 {ECO:0000312|HGNC:HGNC:4392};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
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).
[2] {ECO:0000305}
PUTATIVE FUNCTION, AND VARIANTS GNASHYP THR-374;
GLN-PRO-ILE-PRO-THR-PRO-GLY-ARG-PRO-LEU-THR-PRO-375 INS AND VAL-397.
PubMed=12719376; DOI=10.1093/hmg/ddg130;
Freson K., Jaeken J., Van Helvoirt M., de Zegher F., Wittevrongel C.,
Thys C., Hoylaerts M.F., Vermylen J., Van Geet C.;
"Functional polymorphisms in the paternally expressed XLalphas and its
cofactor ALEX decrease their mutual interaction and enhance receptor-
mediated cAMP formation.";
Hum. Mol. Genet. 12:1121-1130(2003).
[3] {ECO:0000305}
IDENTIFICATION.
PubMed=15148396; DOI=10.1073/pnas.0308758101;
Abramowitz J., Grenet D., Birnbaumer M., Torres H.N., Birnbaumer L.;
"XL alpha-s, the extra-long form of the alpha subunit of the Gs G
protein, is significantly longer than suspected, and so is its
companion Alex.";
Proc. Natl. Acad. Sci. U.S.A. 101:8366-8371(2004).
[4]
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).
[5]
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).
[6]
INVOLVEMENT IN PHP1B.
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).
[7]
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).
[8]
INVOLVEMENT IN AIMAH1.
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).
[9]
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).
[10]
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).
[11]
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).
[12]
VARIANTS [LARGE SCALE ANALYSIS] CYS-201 AND HIS-201.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: May inhibit the adenylyl cyclase-stimulating activity of
guanine nucleotide-binding protein G(s) subunit alpha which is
produced from the same locus in a different open reading frame.
{ECO:0000269|PubMed:12719376}.
-!- SUBUNIT: Interacts with the N-terminal region of the XLas isoforms
of guanine nucleotide-binding protein G(s) subunit alpha.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
Cell projection, ruffle {ECO:0000250}. Note=Predominantly
associated with cell membrane ruffles. {ECO:0000250}.
-!- 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.
{ECO:0000269|PubMed:12719376}. 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: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of
the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: This protein is produced by a bicistronic gene
which also produces guanine nucleotide-binding protein G(s)
subunit alpha from an overlapping reading frame.
{ECO:0000269|PubMed:15148396}.
-!- SIMILARITY: Belongs to the ALEX family. {ECO:0000305}.
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EMBL; AL132655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001070958.1; NM_001077490.2.
RefSeq; NP_001296812.1; NM_001309883.1.
UniGene; Hs.125898; -.
ProteinModelPortal; P84996; -.
BioGrid; 109040; 97.
IntAct; P84996; 5.
iPTMnet; P84996; -.
SwissPalm; P84996; -.
DMDM; 116242967; -.
PeptideAtlas; P84996; -.
PRIDE; P84996; -.
ProteomicsDB; 57761; -.
DNASU; 2778; -.
Ensembl; ENST00000306120; ENSP00000302237; ENSG00000087460.
GeneID; 2778; -.
UCSC; uc061ybz.1; human.
CTD; 2778; -.
DisGeNET; 2778; -.
EuPathDB; HostDB:ENSG00000087460.23; -.
GeneCards; GNAS; -.
GeneReviews; GNAS; -.
HGNC; HGNC:4392; GNAS.
HPA; CAB010337; -.
MalaCards; GNAS; -.
MIM; 114500; phenotype.
MIM; 139320; gene+phenotype.
MIM; 219080; phenotype.
MIM; 603233; phenotype.
neXtProt; NX_P84996; -.
PharmGKB; PA175; -.
HOGENOM; HOG000293422; -.
SIGNOR; P84996; -.
ChiTaRS; GNAS; human.
GenomeRNAi; 2778; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000087460; Expressed in 252 organ(s), highest expression level in telencephalon.
CleanEx; HS_GNAS; -.
ExpressionAtlas; P84996; baseline and differential.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0060348; P:bone development; IMP:UniProtKB.
GO; GO:0050890; P:cognition; IMP:UniProtKB.
GO; GO:0048589; P:developmental growth; IMP:UniProtKB.
GO; GO:0060789; P:hair follicle placode formation; IMP:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0009966; P:regulation of signal transduction; IMP:CACAO.
1: Evidence at protein level;
Cell membrane; Cell projection; Complete proteome; Cushing syndrome;
Disease mutation; Membrane; Polymorphism; Reference proteome.
CHAIN 1 626 Protein ALEX.
/FTId=PRO_0000253964.
COMPBIAS 238 476 Pro-rich. {ECO:0000255}.
VARIANT 201 201 R -> C (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035788.
VARIANT 201 201 R -> H (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035789.
VARIANT 374 374 P -> T (in GNASHYP).
{ECO:0000269|PubMed:12719376}.
/FTId=VAR_028774.
VARIANT 375 375 P -> PQPIPTPGRPLTP (in GNASHYP).
/FTId=VAR_028775.
VARIANT 397 397 L -> V (in GNASHYP).
{ECO:0000269|PubMed:12719376}.
/FTId=VAR_028776.
SEQUENCE 626 AA; 67948 MW; F4CEFA7FA5917EEC CRC64;
MMARPVDPQR SPDPTFRSST RHSGKLEPME ATAHLLRKQC PSRLNSPAWE ASGLHWSSLD
SPVGSMQALR PSAQHSWSPE PSVVPDQAWE DTALHQKKLC PLSLTSLPRE AAVNFSYRSQ
TLLQEAQVLQ GSPELLPRSP KPSGLQRLAP EEATALPLRR LCHLSLMEKD LGTTAHPRGF
PELSHKSTAA ASSRQSRPRV RSASLPPRTR LPSGSQAPSA AHPKRLSDLL LTSRAAAPGW
RSPDPRSRLA APPLGSTTLP STWTAPQSRL TARPSRSPEP QIRESEQRDP QLRRKQQRWK
EPLMPRREEK YPLRGTDPLP PGQPQRIPLP GQPLQPQPIL TPGQPQKIPT PGQHQPILTP
GHSQPIPTPG QPLPPQPIPT PGRPLTPQPI PTPGRPLTPQ PIQMPGRPLR LPPPLRLLRP
GQPMSPQLRQ TQGLPLPQPL LPPGQPKSAG RPLQPLPPGP DARSISDPPA PRSRLPIRLL
RGLLARLPGG ASPRAAAAAA CTTMKGWPAA TMTPAETSPT MGPPDASAGF SIGEIAAAES
PSATYSATFS CKPSGAASVD LRVPSPKPRA LSRSRRYPWR RSADRCAKKP WRSGPRSAQR
RNAVSSSTNN SRTKRWATCV RTACCF


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