LipidDB ID

LipidDB-9606-00445

Entry Name

UniProt Accession

P63092; A6NI00; E1P5G5; P04895; Q12927; Q14433; Q32P26; Q5JWD2; Q5JWD4; Q5JWD5; Q6NR75; Q6NXS0; Q8TBC0; Q96H70;

Theoretical PI

5.59

Molecular Weight

45664.58

Genbank Protein ID

CAA27996.1; CAA27997.1; AAA53147.1; AAA53147.1; AAA53147.1; AAA53147.1; AAA53147.1; AAA53147.1; AAA53146.1; AAA53146.1; AAA53146.1; AAA53146.1; AAA53146.1; AAA53146.1; AAA53148.1; AAA53148.1; AAA53148.1; AAA53148.1; AAA53148.1; AAA53149.1; AAA53149.1; AAA53149.1; AAA53149.1; AAA53149.1; AAB60334.2; CAA30084.1; AAM12611.1; AAM12612.1; AAP88907.1; CAI42914.1; CAI42914.1; CAI42915.1; CAI42915.1; CAI42916.1; CAI42916.1; CAI42917.1; CAI42917.1; CAI42546.1; CAI42546.1; CAI42547.1; CAI42547.1; CAI42548.1; CAI42548.1; CAI42549.1; CAI42549.1; EAW75468.1; EAW75460.1; EAW75463.1; AAH02722.1; AAH08855.1; AAH66923.1; AAH22875.1; AAI04929.1; AAI08316.2; AAA52583.1;

Genbank Nucleotide ID

X04408; X04409; M21142; M21139; M21740; M21140; M21741; M21141; M21142; M21139; M21740; M21140; M21741; M21141; M21142; M21139; M21141; M21740; M21741; M21142; M21139; M21740; M21741; M21141; U12466; X07036; AF493897; AF493898; BT009905; AL109840; AL121917; AL109840; AL121917; AL109840; AL121917; AL109840; AL121917; AL121917; AL109840; AL121917; AL109840; AL121917; AL109840; AL121917; AL109840; AL132655; CH471077; CH471077; CH471077; BC002722; BC008855; BC066923; BC022875; BC104928; BC108315; M14631;

Protein Name

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

Protein Synonyms/Alias

Adenylate cyclase-stimulating G alpha protein;

Gene Name

GNAS

Gene Synonyms/Alias

GNAS1; GSP;

Created Date

13-AUG-1987

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Mumby SM, Kleuss C, Gilman AG. Receptor regulation of G-proteinpalmitoylation. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2800-4.[PMID:8146194]
[2] Kleuss C, Krause E. Galpha(s) is palmitoylated at the N-terminal glycine. EMBOJ. 2003 Feb 17;22(4):826-32.[PMID:12574119]
[3] Forrester MT, Hess DT, Thompson JW, Hultman R, Moseley MA, Stamler JS, CaseyPJ. Site-specific analysis of protein S-acylation by resin-assisted capture. JLipid Res. 2011 Feb;52(2):393-8. doi: 10.1194/jlr.D011106. Epub 2010 Nov 2.[PMID:21044946]

Functional Description

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. Stimulates the Ras signaling pathway via RAPGEF2.

Sequence Annotation

Nucleotide-binding: 47 54 GTP.
Nucleotide-binding: 198 204 GTP.
Nucleotide-binding: 223 227 GTP.
Nucleotide-binding: 292 295 GTP.
Metal binding site: 54 54 Magnesium.
Metal binding site: 204 204 Magnesium.
Binding site: 366 366 GTP; via amide nitrogen.
Modified residue: 201 201 ADP-ribosylarginine; by cholera toxin.
Modified residue: 352 352 Phosphoserine.

Protein Length

394 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005737; C:cytoplasm; IDA:LIFEdb
GO:0005829; C:cytosol; IDA:UniProt
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005834; C:heterotrimeric G-protein complex; TAS:UniProtKB
GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProt
GO:0005886; C:plasma membrane; TAS:UniProtKB
GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB
GO:0004016; F:adenylate cyclase activity; TAS:Reactome
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; TAS:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; IDA:UniProtKB
GO:0007190; P:activation of adenylate cyclase activity; TAS:UniProtKB
GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IDA:UniProtKB
GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL
GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProt
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0060348; P:bone development; IDA:UniProt
GO:0006171; P:cAMP biosynthetic process; TAS:GOC
GO:0071870; P:cellular response to catecholamine stimulus; ISS:BHF-UCL
GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome
GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL
GO:0050890; P:cognition; IDA:UniProt
GO:0048589; P:developmental growth; IDA:UniProt
GO:0006112; P:energy reserve metabolic process; TAS:Reactome
GO:0060789; P:hair follicle placode formation; IDA:UniProt
GO:0046907; P:intracellular transport; NAS:UniProtKB
GO:0070527; P:platelet aggregation; IDA:UniProt
GO:0030819; P:positive regulation of cAMP biosynthetic process; IDA:UniProtKB
GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB
GO:0032320; P:positive regulation of Ras GTPase activity; IDA:UniProtKB
GO:0050796; P:regulation of insulin secretion; TAS:Reactome
GO:0007608; P:sensory perception of smell; TAS:UniProtKB
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0055085; P:transmembrane transport; TAS:Reactome
GO:0006833; P:water transport; TAS:Reactome

Interpro

InterPro; IPR000367; Gprotein_alpha_S
InterPro; IPR001019; Gprotein_alpha_su
InterPro; IPR011025; GproteinA_insert
InterPro; IPR027417; P-loop_NTPase

Pfam

Pfam; PF00503; G-alpha;

SMART

SMART; SM00275; G_alpha;

PROSITE

PRINTS

PRINTS; PR00318; GPROTEINA;
PRINTS; PR00443; GPROTEINAS;