CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009684
UniProt Accession
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
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
186LDKIDVIKQADYVPSubiquitination[1]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
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. 
Sequence Annotation
 NP_BIND 47 54 GTP (By similarity).
 NP_BIND 198 204 GTP (By similarity).
 NP_BIND 223 227 GTP (By similarity).
 NP_BIND 292 295 GTP (By similarity).
 METAL 54 54 Magnesium (By similarity).
 METAL 204 204 Magnesium (By similarity).
 BINDING 366 366 GTP; via amide nitrogen (By similarity).
 MOD_RES 51 51 Phosphoserine (By similarity).
 MOD_RES 352 352 Phosphoserine (By similarity).
 LIPID 2 2 N-palmitoyl glycine (By similarity).
 LIPID 3 3 S-palmitoyl cysteine.
 CROSSLNK 300 300 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; GTP-binding; Isopeptide bond; Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome; Transducer; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 394 AA 
Protein Sequence
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 
Gene Ontology
 GO:0005829; C:cytosol; IDA:BHF-UCL.
 GO:0005768; C:endosome; IDA:RGD.
 GO:0005834; C:heterotrimeric G-protein complex; IDA:BHF-UCL.
 GO:0045121; C:membrane raft; IDA:RGD.
 GO:0001726; C:ruffle; IDA:RGD.
 GO:0031982; C:vesicle; IDA:RGD.
 GO:0043014; F:alpha-tubulin binding; IDA: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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0031852; F:mu-type opioid receptor binding; IDA:RGD.
 GO:0004871; F:signal transducer activity; IDA:RGD.
 GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:BHF-UCL.
 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: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:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
 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
 IPR000367; Gprotein_alpha_S.
 IPR001019; Gprotein_alpha_su.
 IPR011025; GproteinA_insert.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00503; G-alpha 
SMART
 SM00275; G_alpha 
PROSITE
  
PRINTS
 PR00318; GPROTEINA.
 PR00443; GPROTEINAS.