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Q5JWF2

- GNAS1_HUMAN

UniProt

Q5JWF2 - GNAS1_HUMAN

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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

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. 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
Complete GO annotation...

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: UniProtKB
  4. heterotrimeric G-protein complex Source: RefGenome
  5. membrane Source: UniProtKB
Complete GO annotation...

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 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.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

BgeeiQ5JWF2.
CleanExiHS_GNAS.
ExpressionAtlasiQ5JWF2. baseline and differential.
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. 51 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

GeneTreeiENSGT00690000102066.
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

        10         20         30         40         50
MGVRNCLYGN NMSGQRDIPP EIGEQPEQPP LEAPGAAAPG AGPSPAEEME
60 70 80 90 100
TEPPHNEPIP VENDGEACGP PEVSRPNFQV LNPAFREAGA HGSYSPPPEE
110 120 130 140 150
AMPFEAEQPS LGGFWPTLEQ PGFPSGVHAG LEAFGPALME PGAFSGARPG
160 170 180 190 200
LGGYSPPPEE AMPFEFDQPA QRGCSQLLLQ VPDLAPGGPG AAGVPGAPPE
210 220 230 240 250
EPQALRPAKA GSRGGYSPPP EETMPFELDG EGFGDDSPPP GLSRVIAQVD
260 270 280 290 300
GSSQFAAVAA SSAVRLTPAA NAPPLWVPGA IGSPSQEAVR PPSNFTGSSP
310 320 330 340 350
WMEISGPPFE IGSAPAGVDD TPVNMDSPPI ALDGPPIKVS GAPDKRERAE
360 370 380 390 400
RPPVEEEAAE MEGAADAAEG GKVPSPGYGS PAAGAASADT AARAAPAAPA
410 420 430 440 450
DPDSGATPED PDSGTAPADP DSGAFAADPD SGAAPAAPAD PDSGAAPDAP
460 470 480 490 500
ADPDSGAAPD APADPDAGAA PEAPAAPAAA ETRAAHVAPA APDAGAPTAP
510 520 530 540 550
AASATRAAQV RRAASAAPAS GARRKIHLRP PSPEIQAADP PTPRPTRASA
560 570 580 590 600
WRGKSESSRG RRVYYDEGVA SSDDDSSGDE SDDGTSGCLR WFQHRRNRRR
610 620 630 640 650
RKPQRNLLRN FLVQAFGGCF GRSESPQPKA SRSLKVKKVP LAEKRRQMRK
660 670 680 690 700
EALEKRAQKR AEKKRSKLID KQLQDEKMGY MCTHRLLLLG AGESGKSTIV
710 720 730 740 750
KQMRILHVNG FNGEGGEEDP QAARSNSDGE KATKVQDIKN NLKEAIETIV
760 770 780 790 800
AAMSNLVPPV ELANPENQFR VDYILSVMNV PDFDFPPEFY EHAKALWEDE
810 820 830 840 850
GVRACYERSN EYQLIDCAQY FLDKIDVIKQ ADYVPSDQDL LRCRVLTSGI
860 870 880 890 900
FETKFQVDKV NFHMFDVGGQ RDERRKWIQC FNDVTAIIFV VASSSYNMVI
910 920 930 940 950
REDNQTNRLQ EALNLFKSIW NNRWLRTISV ILFLNKQDLL AEKVLAGKSK
960 970 980 990 1000
IEDYFPEFAR YTTPEDATPE PGEDPRVTRA KYFIRDEFLR ISTASGDGRH
1010 1020 1030
YCYPHFTCAV DTENIRRVFN DCRDIIQRMH LRQYELL

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. 51 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

GeneTreei ENSGT00690000102066.
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

Bgeei Q5JWF2.
CleanExi HS_GNAS.
ExpressionAtlasi Q5JWF2. baseline and differential.
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

« Hide 'large scale' publications
  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 AIMAH1.
  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 29, 2014
This is version 107 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