Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00450
Entry Name
UniProt Accession
Theoretical PI
5.69
Molecular Weight
45663.6
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Protein Synonyms/Alias
Adenylate cyclase-stimulating G alpha protein; G-alpha-8;
Gene Name
Gnas
Gene Synonyms/Alias
Gnas1;
Created Date
13-AUG-1987
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
3
Canonical
*****MGCLGNSKTE
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Degtyarev MY, Spiegel AM, Jones TL. The G protein alpha s subunit incorporates[3H]palmitic acid and mutation of cysteine-3 prevents this modification.Biochemistry. 1993 Aug 17;32(32):8057-61.[PMID:8347607]
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 (By similarity).
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: 352 352 Phosphoserine.
Protein Length
394 AA.
Protein Sequence
(Canonical)
MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM  60
RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK EAIETIVAAM SNLVPPVELA  120
NPENQFRVDY ILSVMNVPNF DFPPEFYEHA KALWEDEGVR ACYERSNEYQ LIDCAQYFLD  180
KIDVIKQADY VPSDQDLLRC RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND  240
VTAIIFVVAS SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK  300
VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST ASGDGRHYCY  360
PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL                              394
FASTA
(Canonical)
>LipidDB-10116-00450|P63095
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPNFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
Gene Ontology
GO:0005737; C:cytoplasm; IDA:RGD
GO:0005829; C:cytosol; IDA:BHF-UCL
GO:0005768; C:endosome; IDA:RGD
GO:0005834; C:heterotrimeric G-protein complex; IDA:BHF-UCL
GO:0016020; C:membrane; IDA:BHF-UCL
GO:0045121; C:membrane raft; IDA:RGD
GO:0005886; C:plasma membrane; IDA:RGD
GO:0001726; C:ruffle; IDA:RGD
GO:0031982; C:vesicle; IDA:RGD
GO:0043014; F:alpha-tubulin binding; IDA:RGD
GO:0031698; F:beta-2 adrenergic receptor binding; IPI:RGD
GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IPI:RGD
GO:0031748; F:D1 dopamine receptor binding; IPI:RGD
GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD
GO:0031681; F:G-protein beta-subunit binding; IDA:RGD
GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome
GO:0005525; F:GTP binding; IDA:RGD
GO:0003924; F:GTPase activity; IBA:RefGenome
GO:0005159; F:insulin-like growth factor receptor binding; IPI:RGD
GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0031852; F:mu-type opioid receptor binding; IDA:RGD
GO:0019904; F:protein domain specific binding; IPI:RGD
GO:0004871; F:signal transducer activity; IDA:RGD
GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB
GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:BHF-UCL
GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:RGD
GO:0055074; P:calcium ion homeostasis; IMP:RGD
GO:0071870; P:cellular response to catecholamine stimulus; IDA:BHF-UCL
GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:BHF-UCL
GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:RGD
GO:0045776; P:negative regulation of blood pressure; IMP:RGD
GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD
GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:RGD
GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB
GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD
GO:0032320; P:positive regulation of Ras GTPase activity; ISS:UniProtKB
GO:0010765; P:positive regulation of sodium ion transport; IMP:RGD
GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:RGD
GO:0007606; P:sensory perception of chemical stimulus; IBA:RefGenome
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;