Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9913-01063
Entry Name
UniProt Accession
Theoretical PI
5.5
Molecular Weight
45708.59
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;
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
Bos taurus (Bovine)
NCBI Taxa ID
9913
Reference
[1] Kleuss C, Krause E. Galpha(s) is palmitoylated at the N-terminal glycine. EMBOJ. 2003 Feb 17;22(4):826-32.[PMID:12574119]
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 ILSVMNVPDF DFPPEFYEHA KALWEDEGVR ACYERSNEYQ LIDCAQYFLD  180
KIDVIKQDDY 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-9913-01063|P04896
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
Gene Ontology
GO:0030425; C:dendrite; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IEA:InterPro
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; ISS:UniProtKB
GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB
GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IEA:Ensembl
GO:0051216; P:cartilage development; IEA:Ensembl
GO:0050890; P:cognition; IEA:Ensembl
GO:0048589; P:developmental growth; IEA:Ensembl
GO:0006306; P:DNA methylation; IEA:Ensembl
GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl
GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl
GO:0001958; P:endochondral ossification; IEA:Ensembl
GO:0006112; P:energy reserve metabolic process; IEA:Ensembl
GO:0071514; P:genetic imprinting; IEA:Ensembl
GO:0060789; P:hair follicle placode formation; IEA:Ensembl
GO:0035264; P:multicellular organism growth; IEA:Ensembl
GO:0070527; P:platelet aggregation; IEA:Ensembl
GO:0030819; P:positive regulation of cAMP biosynthetic process; ISS:UniProtKB
GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB
GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl
GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl
GO:0032320; P:positive regulation of Ras GTPase activity; ISS:UniProtKB
GO:0040032; P:post-embryonic body morphogenesis; IEA:Ensembl
GO:0042493; P:response to drug; IEA:Ensembl
GO:0001894; P:tissue homeostasis; IEA:Ensembl
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;