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Q5JWF2 (GNAS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
Alternative name(s):
Adenylate cyclase-stimulating G alpha protein
Extra large alphas protein
Short name=XLalphas
Gene names
Name:GNAS
Synonyms:GNAS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1037 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. XLas isoforms interact with the same set of receptors as Gnas isoforms By similarity. UniProtKB Q63803 UniProtKB Q6R0H7

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts through its N-terminal region with ALEX which is produced from the same locus in a different open reading frame. This interaction may inhibit its adenylyl cyclase-stimulating activity By similarity. UniProtKB Q63803 UniProtKB Q6R0H7

Subcellular location

Cell membrane; Peripheral membrane protein By similarity UniProtKB Q63803.

Involvement in 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. Ref.13 Ref.15

ACTH-independent macronodular adrenal hyperplasia (AIMAH) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

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.
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. Ref.8 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Miscellaneous

This protein is produced by a bicistronic gene which also produces the ALEX protein from an overlapping reading frame By similarity. UniProtKB Q63803

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.

Sequence similarities

Belongs to the G-alpha family. G(s) subfamily.

Sequence caution

The sequence CAB83215.1 differs from that shown. Reason: Frameshift at position 40.

The sequence CAM28315.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCushing syndrome
Disease mutation
   DomainCoiled coil
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMADP-ribosylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from mutant phenotype Ref.15. Source: UniProt

adenylate cyclase-activating dopamine receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

bone development

Inferred from mutant phenotype Ref.15. Source: UniProt

cartilage development

Inferred from electronic annotation. Source: Ensembl

cognition

Inferred from mutant phenotype Ref.15. Source: UniProt

developmental growth

Inferred from mutant phenotype Ref.15. Source: UniProt

embryonic cranial skeleton morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

energy reserve metabolic process

Inferred from electronic annotation. Source: Ensembl

genetic imprinting

Inferred from electronic annotation. Source: Ensembl

hair follicle placode formation

Inferred from mutant phenotype Ref.15. Source: UniProt

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

platelet aggregation

Inferred from mutant phenotype Ref.15. Source: UniProt

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

post-embryonic body morphogenesis

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

sensory perception of chemical stimulus

Inferred from Biological aspect of Ancestor. Source: RefGenome

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay Ref.15. Source: UniProt

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 20458337. Source: UniProt

extrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from direct assay Ref.15. Source: UniProt

   Molecular_functionG-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ionotropic glutamate receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

mu-type opioid receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transducer activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARRB1P494075EBI-4400880,EBI-743313

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform XLas-1 Ref.1 (identifier: Q5JWF2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Gene prediction confirmed by EST data.
Isoform XLas-2 Ref.1 (identifier: Q5JWF2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     714-729: EGGEEDPQAARSNSDG → DS
Note: Gene prediction confirmed by EST data.
Isoform XLas-3 Ref.4 (identifier: Q5JWF2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     691-752: AGESGKSTIV...KEAIETIVAA → RKVVPSDTEG...VLENLVKAPL
     753-1037: Missing.
Isoform Gnas-1 (identifier: P63092-1)

Also known as: Alpha-S2; GNASl; Alpha-S-long;

The sequence of this isoform can be found in the external entry P63092.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform 3 (identifier: P63092-3)

The sequence of this isoform can be found in the external entry P63092.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: No experimental confirmation available.
Isoform Gnas-2 (identifier: P63092-2)

Also known as: Alpha-S1; GNASs; Alpha-S-short;

The sequence of this isoform can be found in the external entry P63092.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform Nesp55 (identifier: O95467-1)

The sequence of this isoform can be found in the external entry O95467.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10371037Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
PRO_0000253984

Regions

Nucleotide binding690 – 6978GTP By similarity UniProtKB P63096
Nucleotide binding841 – 8477GTP By similarity
Nucleotide binding866 – 8705GTP By similarity UniProtKB P63096
Nucleotide binding935 – 9384GTP By similarity UniProtKB P63096
Coiled coil641 – 66727 Potential
Coiled coil730 – 75627 Potential
Compositional bias358 – 522165Ala-rich

Sites

Metal binding6971Magnesium By similarity
Metal binding8471Magnesium By similarity
Binding site10091GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue8441ADP-ribosylarginine; by cholera toxin By similarity UniProtKB P63094
Modified residue9951Phosphoserine Ref.11

Natural variations

Alternative sequence691 – 75262AGESG…TIVAA → RKVVPSDTEGRFRLDRPAPA TVSWTGRGFSVSSLLIRSPN PPAFTVEKPDTQVLENLVKA PL in isoform XLas-3. Ref.4
VSP_052173
Alternative sequence714 – 72916EGGEE…SNSDG → DS in isoform XLas-2. Ref.1
VSP_052174
Alternative sequence753 – 1037285Missing in isoform XLas-3. Ref.4
VSP_052175
Natural variant4361A → D in GNASHYP. Ref.13 Ref.15
Corresponds to variant rs61749698 [ dbSNP | Ensembl ].
VAR_028777
Natural variant4371A → APADPDSGAAPDA in GNAS hyperfunction. Ref.13 Ref.15
VAR_028778
Natural variant4591P → R in GNASHYP. Ref.13 Ref.15
Corresponds to variant rs148033592 [ dbSNP | Ensembl ].
VAR_028779
Natural variant10231R → L.
Corresponds to variant rs8986 [ dbSNP | Ensembl ].
VAR_059656

Experimental info

Sequence conflict151Q → E in CAB83215. Ref.3
Sequence conflict461A → S in CAB83215. Ref.3
Sequence conflict1321E → A in CAB83215. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform XLas-1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 02CB52383015E75D

FASTA1,037111,025
        10         20         30         40         50         60 
MGVRNCLYGN NMSGQRDIPP EIGEQPEQPP LEAPGAAAPG AGPSPAEEME TEPPHNEPIP 

        70         80         90        100        110        120 
VENDGEACGP PEVSRPNFQV LNPAFREAGA HGSYSPPPEE AMPFEAEQPS LGGFWPTLEQ 

       130        140        150        160        170        180 
PGFPSGVHAG LEAFGPALME PGAFSGARPG LGGYSPPPEE AMPFEFDQPA QRGCSQLLLQ 

       190        200        210        220        230        240 
VPDLAPGGPG AAGVPGAPPE EPQALRPAKA GSRGGYSPPP EETMPFELDG EGFGDDSPPP 

       250        260        270        280        290        300 
GLSRVIAQVD GSSQFAAVAA SSAVRLTPAA NAPPLWVPGA IGSPSQEAVR PPSNFTGSSP 

       310        320        330        340        350        360 
WMEISGPPFE IGSAPAGVDD TPVNMDSPPI ALDGPPIKVS GAPDKRERAE RPPVEEEAAE 

       370        380        390        400        410        420 
MEGAADAAEG GKVPSPGYGS PAAGAASADT AARAAPAAPA DPDSGATPED PDSGTAPADP 

       430        440        450        460        470        480 
DSGAFAADPD SGAAPAAPAD PDSGAAPDAP ADPDSGAAPD APADPDAGAA PEAPAAPAAA 

       490        500        510        520        530        540 
ETRAAHVAPA APDAGAPTAP AASATRAAQV RRAASAAPAS GARRKIHLRP PSPEIQAADP 

       550        560        570        580        590        600 
PTPRPTRASA WRGKSESSRG RRVYYDEGVA SSDDDSSGDE SDDGTSGCLR WFQHRRNRRR 

       610        620        630        640        650        660 
RKPQRNLLRN FLVQAFGGCF GRSESPQPKA SRSLKVKKVP LAEKRRQMRK EALEKRAQKR 

       670        680        690        700        710        720 
AEKKRSKLID KQLQDEKMGY MCTHRLLLLG AGESGKSTIV KQMRILHVNG FNGEGGEEDP 

       730        740        750        760        770        780 
QAARSNSDGE KATKVQDIKN NLKEAIETIV AAMSNLVPPV ELANPENQFR VDYILSVMNV 

       790        800        810        820        830        840 
PDFDFPPEFY EHAKALWEDE GVRACYERSN EYQLIDCAQY FLDKIDVIKQ ADYVPSDQDL 

       850        860        870        880        890        900 
LRCRVLTSGI FETKFQVDKV NFHMFDVGGQ RDERRKWIQC FNDVTAIIFV VASSSYNMVI 

       910        920        930        940        950        960 
REDNQTNRLQ EALNLFKSIW NNRWLRTISV ILFLNKQDLL AEKVLAGKSK IEDYFPEFAR 

       970        980        990       1000       1010       1020 
YTTPEDATPE PGEDPRVTRA KYFIRDEFLR ISTASGDGRH YCYPHFTCAV DTENIRRVFN 

      1030 
DCRDIIQRMH LRQYELL 

« Hide

Isoform XLas-2 [UniParc].

Checksum: 22DBCF510AEF25D6
Show »

FASTA1,023109,626
Isoform XLas-3 [UniParc].

Checksum: 65A9202D681E861F
Show »

FASTA75277,643
Isoform Gnas-1 (Alpha-S2) (GNASl) (Alpha-S-long) [UniParc] [UniParc].

See P63092.

Isoform 3 [UniParc].

See P63092.

Isoform Gnas-2 (Alpha-S1) (GNASs) (Alpha-S-short) [UniParc] [UniParc].

See P63092.

Isoform Nesp55 [UniParc].

See O95467.

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"An imprinted antisense transcript at the human GNAS1 locus."
Hayward B.E., Bonthron D.T.
Hum. Mol. Genet. 9:835-841(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-689.
[4]"The human GNAS1 gene is imprinted and encodes distinct paternally and biallelically expressed G proteins."
Hayward B.E., Kamiya M., Strain L., Moran V., Campbell R., Hayashizaki Y., Bonthron D.T.
Proc. Natl. Acad. Sci. U.S.A. 95:10038-10043(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 197-1037 (ISOFORM XLAS-3).
[5]"Oscillating evolution of a mammalian locus with overlapping reading frames: an XLalphas/ALEX relay."
Nekrutenko A., Wadhawan S., Goetting-Minesky P., Makova K.D.
PLoS Genet. 1:197-204(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-689.
[6]"GNAS1 lesions in pseudohypoparathyroidism Ia and Ic: genotype phenotype relationship and evidence of the maternal transmission of the hormonal resistance."
Linglart A., Carel J.-C., Garabedian M., Le T., Mallet E., Kottler M.-L.
J. Clin. Endocrinol. Metab. 87:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHP1C.
[7]"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."
Abramowitz J., Grenet D., Birnbaumer M., Torres H.N., Birnbaumer L.
Proc. Natl. Acad. Sci. U.S.A. 101:8366-8371(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[8]"A GNAS1 imprinting defect in pseudohypoparathyroidism type IB."
Liu J., Litman D., Rosenberg M.J., Yu S., Biesecker L.G., Weinstein L.S.
J. Clin. Invest. 106:1167-1174(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
[9]"Paternal uniparental isodisomy of chromosome 20q -- and the resulting changes in GNAS1 methylation -- as a plausible cause of pseudohypoparathyroidism."
Bastepe M., Lane A.H., Jueppner H.
Am. J. Hum. Genet. 68:1283-1289(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
[10]"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."
Wu W.-I., Schwindinger W.F., Aparicio L.F., Levine M.A.
J. Biol. Chem. 276:165-171(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Genetic variation of the extra-large stimulatory G protein alpha-subunit leads to Gs hyperfunction in platelets and is a risk factor for bleeding."
Freson K., Hoylaerts M.F., Jaeken J., Eyssen M., Arnout J., Vermylen J., Van Geet C.
Thromb. Haemost. 86:733-738(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GNASHYP ASP-436; PRO-ALA-ASP-PRO-ASP-SER-GLY-ALA-ALA-PRO-ASP-ALA-437 INS AND ARG-459.
[14]"Discordance between genetic and epigenetic defects in pseudohypoparathyroidism type 1b revealed by inconsistent loss of maternal imprinting at GNAS1."
Jan de Beur S., Ding C., Germain-Lee E., Cho J., Maret A., Levine M.A.
Am. J. Hum. Genet. 73:314-322(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
[15]"Functional polymorphisms in the paternally expressed XLalphas and its cofactor ALEX decrease their mutual interaction and enhance receptor-mediated cAMP formation."
Freson K., Jaeken J., Van Helvoirt M., de Zegher F., Wittevrongel C., Thys C., Hoylaerts M.F., Vermylen J., Van Geet C.
Hum. Mol. Genet. 12:1121-1130(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GNASHYP ASP-436; PRO-ALA-ASP-PRO-ASP-SER-GLY-ALA-ALA-PRO-ASP-ALA-437 INS AND ARG-459.
[16]"Cushing's syndrome secondary to adrenocorticotropin-independent macronodular adrenocortical hyperplasia due to activating mutations of GNAS1 gene."
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.
J. Clin. Endocrinol. Metab. 88:2147-2151(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AIMAH.
[17]"Autosomal dominant pseudohypoparathyroidism type Ib is associated with a heterozygous microdeletion that likely disrupts a putative imprinting control element of GNAS."
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.
J. Clin. Invest. 112:1255-1263(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
[18]"A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type Ib redefines the boundaries of a cis-acting imprinting control element of GNAS."
Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.
Am. J. Hum. Genet. 76:804-814(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
[19]"Deletion of the NESP55 differentially methylated region causes loss of maternal GNAS imprints and pseudohypoparathyroidism type Ib."
Bastepe M., Froehlich L.F., Linglart A., Abu-Zahra H.S., Tojo K., Ward L.M., Jueppner H.
Nat. Genet. 37:25-27(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL109840, AL121917, AL132655 Genomic DNA. Translation: CAI42932.2.
AL109840, AL121917, AL132655 Genomic DNA. Translation: CAI42933.2.
AL121917, AL109840, AL132655 Genomic DNA. Translation: CAI42566.2.
AL121917, AL109840, AL132655 Genomic DNA. Translation: CAI42567.2.
AL132655, AL109840, AL121917 Genomic DNA. Translation: CAI43073.2.
AL132655, AL109840, AL121917 Genomic DNA. Translation: CAI43074.2.
AL132655 Genomic DNA. Translation: CAM28315.1. Sequence problems.
CH471077 Genomic DNA. Translation: EAW75462.1.
CH471077 Genomic DNA. Translation: EAW75469.1.
AJ251760 Genomic DNA. Translation: CAB83215.1. Frameshift.
AJ224867 mRNA. Translation: CAA12164.1.
AJ224868 Genomic DNA. Translation: CAA12165.1.
AY898804 Genomic DNA. Translation: AAX51890.1.
RefSeqNP_536350.2. NM_080425.2.
UniGeneHs.125898.

3D structure databases

ProteinModelPortalQ5JWF2.
SMRQ5JWF2. Positions 654-1037.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109040. 36 interactions.
IntActQ5JWF2. 1 interaction.
MINTMINT-4998906.

Polymorphism databases

DMDM116248089.

Proteomic databases

PRIDEQ5JWF2.

Protocols and materials databases

DNASU2778.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371100; ENSP00000360141; ENSG00000087460. [Q5JWF2-1]
ENST00000371102; ENSP00000360143; ENSG00000087460. [Q5JWF2-2]
GeneID2778.
KEGGhsa:2778.
UCSCuc002xzw.3. human. [Q5JWF2-1]

Organism-specific databases

CTD2778.
GeneCardsGC20P057414.
HGNCHGNC:4392. GNAS.
HPACAB010337.
HPA027478.
HPA028386.
MIM139320. gene+phenotype.
219080. phenotype.
603233. phenotype.
612462. phenotype.
neXtProtNX_Q5JWF2.
PharmGKBPA175.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG079975.
InParanoidQ5JWF2.
KOK04632.
PhylomeDBQ5JWF2.
TreeFamTF300673.

Gene expression databases

ArrayExpressQ5JWF2.
BgeeQ5JWF2.
CleanExHS_GNAS.
GenevestigatorQ5JWF2.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR000367. Gprotein_alpha_S.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR00443. GPROTEINAS.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSGNAS. human.
GenomeRNAi2778.
NextBio10928.
PROQ5JWF2.
SOURCESearch...

Entry information

Entry nameGNAS1_HUMAN
AccessionPrimary (citable) accession number: Q5JWF2
Secondary accession number(s): A2A2S3 expand/collapse secondary AC list , E1P5G3, O75684, O75685, Q5JW67, Q5JWF1, Q9NY42
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM