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Q5JWF2

- GNAS1_HUMAN

UniProt

Q5JWF2 - GNAS1_HUMAN

Protein

Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas

Gene

GNAS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi697 – 6971MagnesiumBy similarity
    Metal bindingi847 – 8471MagnesiumBy similarity
    Binding sitei1009 – 10091GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi690 – 6978GTPBy similarity
    Nucleotide bindingi841 – 8477GTPBy similarity
    Nucleotide bindingi866 – 8705GTPBy similarity
    Nucleotide bindingi935 – 9384GTPBy similarity

    GO - Molecular functioni

    1. beta-2 adrenergic receptor binding Source: RefGenome
    2. corticotropin-releasing hormone receptor 1 binding Source: RefGenome
    3. D1 dopamine receptor binding Source: RefGenome
    4. G-protein beta/gamma-subunit complex binding Source: RefGenome
    5. GTPase activity Source: RefGenome
    6. GTP binding Source: UniProtKB-KW
    7. insulin-like growth factor receptor binding Source: RefGenome
    8. ionotropic glutamate receptor binding Source: RefGenome
    9. metal ion binding Source: UniProtKB-KW
    10. mu-type opioid receptor binding Source: RefGenome
    11. protein binding Source: IntAct
    12. signal transducer activity Source: RefGenome

    GO - Biological processi

    1. adenylate cyclase-activating dopamine receptor signaling pathway Source: RefGenome
    2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: UniProt
    3. bone development Source: UniProt
    4. cartilage development Source: Ensembl
    5. cognition Source: UniProt
    6. developmental growth Source: UniProt
    7. DNA methylation Source: Ensembl
    8. embryonic cranial skeleton morphogenesis Source: Ensembl
    9. embryonic hindlimb morphogenesis Source: Ensembl
    10. endochondral ossification Source: Ensembl
    11. energy reserve metabolic process Source: Ensembl
    12. genetic imprinting Source: Ensembl
    13. hair follicle placode formation Source: UniProt
    14. multicellular organism growth Source: Ensembl
    15. platelet aggregation Source: UniProt
    16. positive regulation of osteoblast differentiation Source: Ensembl
    17. positive regulation of osteoclast differentiation Source: Ensembl
    18. post-embryonic body morphogenesis Source: Ensembl
    19. response to drug Source: Ensembl
    20. sensory perception of chemical stimulus Source: RefGenome
    21. tissue homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Transducer

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:GNAS
    Synonyms:GNAS11 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:4392. GNAS.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProt
    2. dendrite Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. heterotrimeric G-protein complex Source: RefGenome
    5. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti436 – 4361A → D in GNASHYP. 2 Publications
    Corresponds to variant rs61749698 [ dbSNP | Ensembl ].
    VAR_028777
    Natural varianti459 – 4591P → R in GNASHYP. 2 Publications
    Corresponds to variant rs148033592 [ dbSNP | Ensembl ].
    VAR_028779
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.7 Publications
    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.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Cushing syndrome, Disease mutation

    Organism-specific databases

    MIMi139320. gene+phenotype.
    219080. phenotype.
    603233. phenotype.
    612462. phenotype.
    PharmGKBiPA175.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10371037Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLasPRO_0000253984Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei844 – 8441ADP-ribosylarginine; by cholera toxinBy similarity
    Modified residuei995 – 9951Phosphoserine1 Publication

    Keywords - PTMi

    ADP-ribosylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ5JWF2.
    PRIDEiQ5JWF2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5JWF2.
    BgeeiQ5JWF2.
    CleanExiHS_GNAS.
    GenevestigatoriQ5JWF2.

    Organism-specific databases

    HPAiCAB010337.
    HPA027478.
    HPA028386.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARRB1P494075EBI-4400880,EBI-743313

    Protein-protein interaction databases

    BioGridi109040. 36 interactions.
    IntActiQ5JWF2. 1 interaction.
    MINTiMINT-4998906.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5JWF2.
    SMRiQ5JWF2. Positions 654-1037.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili641 – 66727Sequence AnalysisAdd
    BLAST
    Coiled coili730 – 75627Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi358 – 522165Ala-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    HOVERGENiHBG079975.
    InParanoidiQ5JWF2.
    KOiK04632.
    PhylomeDBiQ5JWF2.
    TreeFamiTF300673.

    Family and domain databases

    Gene3Di1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR000367. Gprotein_alpha_S.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10218. PTHR10218. 1 hit.
    PfamiPF00503. G-alpha. 1 hit.
    [Graphical view]
    PRINTSiPR00318. GPROTEINA.
    PR00443. GPROTEINAS.
    SMARTiSM00275. G_alpha. 1 hit.
    [Graphical view]
    SUPFAMiSSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform XLas-1 (identifier: Q5JWF2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGVRNCLYGN NMSGQRDIPP EIGEQPEQPP LEAPGAAAPG AGPSPAEEME     50
    TEPPHNEPIP VENDGEACGP PEVSRPNFQV LNPAFREAGA HGSYSPPPEE 100
    AMPFEAEQPS LGGFWPTLEQ PGFPSGVHAG LEAFGPALME PGAFSGARPG 150
    LGGYSPPPEE AMPFEFDQPA QRGCSQLLLQ VPDLAPGGPG AAGVPGAPPE 200
    EPQALRPAKA GSRGGYSPPP EETMPFELDG EGFGDDSPPP GLSRVIAQVD 250
    GSSQFAAVAA SSAVRLTPAA NAPPLWVPGA IGSPSQEAVR PPSNFTGSSP 300
    WMEISGPPFE IGSAPAGVDD TPVNMDSPPI ALDGPPIKVS GAPDKRERAE 350
    RPPVEEEAAE MEGAADAAEG GKVPSPGYGS PAAGAASADT AARAAPAAPA 400
    DPDSGATPED PDSGTAPADP DSGAFAADPD SGAAPAAPAD PDSGAAPDAP 450
    ADPDSGAAPD APADPDAGAA PEAPAAPAAA ETRAAHVAPA APDAGAPTAP 500
    AASATRAAQV RRAASAAPAS GARRKIHLRP PSPEIQAADP PTPRPTRASA 550
    WRGKSESSRG RRVYYDEGVA SSDDDSSGDE SDDGTSGCLR WFQHRRNRRR 600
    RKPQRNLLRN FLVQAFGGCF GRSESPQPKA SRSLKVKKVP LAEKRRQMRK 650
    EALEKRAQKR AEKKRSKLID KQLQDEKMGY MCTHRLLLLG AGESGKSTIV 700
    KQMRILHVNG FNGEGGEEDP QAARSNSDGE KATKVQDIKN NLKEAIETIV 750
    AAMSNLVPPV ELANPENQFR VDYILSVMNV PDFDFPPEFY EHAKALWEDE 800
    GVRACYERSN EYQLIDCAQY FLDKIDVIKQ ADYVPSDQDL LRCRVLTSGI 850
    FETKFQVDKV NFHMFDVGGQ RDERRKWIQC FNDVTAIIFV VASSSYNMVI 900
    REDNQTNRLQ EALNLFKSIW NNRWLRTISV ILFLNKQDLL AEKVLAGKSK 950
    IEDYFPEFAR YTTPEDATPE PGEDPRVTRA KYFIRDEFLR ISTASGDGRH 1000
    YCYPHFTCAV DTENIRRVFN DCRDIIQRMH LRQYELL 1037

    Note: Gene prediction confirmed by EST data.Curated

    Length:1,037
    Mass (Da):111,025
    Last modified:October 17, 2006 - v2
    Checksum:i02CB52383015E75D
    GO
    Isoform XLas-2 (identifier: Q5JWF2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         714-729: EGGEEDPQAARSNSDG → DS

    Note: Gene prediction confirmed by EST data.Curated

    Show »
    Length:1,023
    Mass (Da):109,626
    Checksum:i22DBCF510AEF25D6
    GO
    Isoform XLas-3 (identifier: Q5JWF2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         691-752: AGESGKSTIV...KEAIETIVAA → RKVVPSDTEG...VLENLVKAPL
         753-1037: Missing.

    Show »
    Length:752
    Mass (Da):77,643
    Checksum:i65A9202D681E861F
    GO
    Isoform Gnas-1Curated (identifier: P63092-1) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: Alpha-S2Curated, GNASlCurated, Alpha-S-longCurated

    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.
    Length:394
    Mass (Da):45,665
    GO
    Isoform 3 (identifier: P63092-3) [UniParc]FASTAAdd to Basket

    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.

    Length:379
    Mass (Da):44,179
    GO
    Isoform Gnas-2Curated (identifier: P63092-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: Alpha-S1Curated, GNASsCurated, Alpha-S-shortCurated

    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.
    Length:380
    Mass (Da):44,266
    GO
    Isoform Nesp55Curated (identifier: O95467-1) [UniParc]FASTAAdd to Basket

    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.

    Length:245
    Mass (Da):28,029
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151Q → E in CAB83215. (PubMed:10749992)Curated
    Sequence conflicti46 – 461A → S in CAB83215. (PubMed:10749992)Curated
    Sequence conflicti132 – 1321E → A in CAB83215. (PubMed:10749992)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti436 – 4361A → D in GNASHYP. 2 Publications
    Corresponds to variant rs61749698 [ dbSNP | Ensembl ].
    VAR_028777
    Natural varianti437 – 4371A → APADPDSGAAPDA in GNAS hyperfunction. 2 Publications
    VAR_028778
    Natural varianti459 – 4591P → R in GNASHYP. 2 Publications
    Corresponds to variant rs148033592 [ dbSNP | Ensembl ].
    VAR_028779
    Natural varianti1023 – 10231R → L.
    Corresponds to variant rs8986 [ dbSNP | Ensembl ].
    VAR_059656

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei691 – 75262AGESG…TIVAA → RKVVPSDTEGRFRLDRPAPA TVSWTGRGFSVSSLLIRSPN PPAFTVEKPDTQVLENLVKA PL in isoform XLas-3. 1 PublicationVSP_052173Add
    BLAST
    Alternative sequencei714 – 72916EGGEE…SNSDG → DS in isoform XLas-2. CuratedVSP_052174Add
    BLAST
    Alternative sequencei753 – 1037285Missing in isoform XLas-3. 1 PublicationVSP_052175Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS46622.1. [Q5JWF2-1]
    RefSeqiNP_536350.2. NM_080425.2. [Q5JWF2-1]
    UniGeneiHs.125898.

    Genome annotation databases

    EnsembliENST00000371100; ENSP00000360141; ENSG00000087460. [Q5JWF2-1]
    ENST00000371102; ENSP00000360143; ENSG00000087460. [Q5JWF2-2]
    GeneIDi2778.
    KEGGihsa:2778.
    UCSCiuc002xzw.3. human. [Q5JWF2-1]

    Polymorphism databases

    DMDMi116248089.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS46622.1. [Q5JWF2-1 ]
    RefSeqi NP_536350.2. NM_080425.2. [Q5JWF2-1 ]
    UniGenei Hs.125898.

    3D structure databases

    ProteinModelPortali Q5JWF2.
    SMRi Q5JWF2. Positions 654-1037.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109040. 36 interactions.
    IntActi Q5JWF2. 1 interaction.
    MINTi MINT-4998906.

    Polymorphism databases

    DMDMi 116248089.

    Proteomic databases

    MaxQBi Q5JWF2.
    PRIDEi Q5JWF2.

    Protocols and materials databases

    DNASUi 2778.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371100 ; ENSP00000360141 ; ENSG00000087460 . [Q5JWF2-1 ]
    ENST00000371102 ; ENSP00000360143 ; ENSG00000087460 . [Q5JWF2-2 ]
    GeneIDi 2778.
    KEGGi hsa:2778.
    UCSCi uc002xzw.3. human. [Q5JWF2-1 ]

    Organism-specific databases

    CTDi 2778.
    GeneCardsi GC20P057414.
    HGNCi HGNC:4392. GNAS.
    HPAi CAB010337.
    HPA027478.
    HPA028386.
    MIMi 139320. gene+phenotype.
    219080. phenotype.
    603233. phenotype.
    612462. phenotype.
    neXtProti NX_Q5JWF2.
    PharmGKBi PA175.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG079975.
    InParanoidi Q5JWF2.
    KOi K04632.
    PhylomeDBi Q5JWF2.
    TreeFami TF300673.

    Miscellaneous databases

    ChiTaRSi GNAS. human.
    GenomeRNAii 2778.
    NextBioi 10928.
    PROi Q5JWF2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5JWF2.
    Bgeei Q5JWF2.
    CleanExi HS_GNAS.
    Genevestigatori Q5JWF2.

    Family and domain databases

    Gene3Di 1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR000367. Gprotein_alpha_S.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10218. PTHR10218. 1 hit.
    Pfami PF00503. G-alpha. 1 hit.
    [Graphical view ]
    PRINTSi PR00318. GPROTEINA.
    PR00443. GPROTEINAS.
    SMARTi SM00275. G_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiGNAS1_HUMAN
    AccessioniPrimary (citable) accession number: Q5JWF2
    Secondary accession number(s): A2A2S3
    , E1P5G3, O75684, O75685, Q5JW67, Q5JWF1, Q9NY42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3