CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009681
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 
Gene Name
 GNAS 
Gene Synonyms/Alias
 GNAS1; GSP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17EDQRNEEKAQREANKubiquitination[1]
53LGAGESGKSTIVKQMubiquitination[1]
58SGKSTIVKQMRILHVubiquitination[1]
74GFNGDSEKATKVQDIubiquitination[1, 2, 3, 4, 5]
77GDSEKATKVQDIKNNubiquitination[4]
82ATKVQDIKNNLKEAIubiquitination[1]
172LDKIDVIKQADYVPSubiquitination[1]
197TSGIFETKFQVDKVNubiquitination[1]
202ETKFQVDKVNFHMFDubiquitination[1]
260QEALNLFKSIWNNRWubiquitination[1]
279SVILFLNKQDLLAEKubiquitination[1]
286KQDLLAEKVLAGKSKubiquitination[1]
291AEKVLAGKSKIEDYFubiquitination[1]
293KVLAGKSKIEDYFPEubiquitination[1]
324DPRVTRAKYFIRDEFubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
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 201 201 ADP-ribosylarginine; by cholera toxin (By
 MOD_RES 352 352 Phosphoserine.
 LIPID 2 2 N-palmitoyl glycine (By similarity).
 LIPID 3 3 S-palmitoyl cysteine.
 CROSSLNK 300 300 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 ADP-ribosylation; Alternative splicing; Cell membrane; Complete proteome; Cushing syndrome; Direct protein sequencing; Disease mutation; GTP-binding; Isopeptide bond; Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein; Polymorphism; Proto-oncogene; 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 DSEKATKVQD IKNNLKEAIE TIVAAMSNLV PPVELANPEN QFRVDYILSV 120
MNVPDFDFPP EFYEHAKALW EDEGVRACYE RSNEYQLIDC AQYFLDKIDV IKQADYVPSD 180
QDLLRCRVLT SGIFETKFQV DKVNFHMFDV GGQRDERRKW IQCFNDVTAI IFVVASSSYN 240
MVIREDNQTN RLQEALNLFK SIWNNRWLRT ISVILFLNKQ DLLAEKVLAG KSKIEDYFPE 300
FARYTTPEDA TPEPGEDPRV TRAKYFIRDE FLRISTASGD GRHYCYPHFT CAVDTENIRR 360
VFNDCRDIIQ RMHLRQYELL 380 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:LIFEdb.
 GO:0005834; C:heterotrimeric G-protein complex; TAS:UniProtKB.
 GO:0031224; C:intrinsic to membrane; IDA: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; IEA:UniProtKB-KW.
 GO:0007190; P:activation of adenylate cyclase activity; TAS:UniProtKB.
 GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 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:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:0046907; P:intracellular transport; NAS:UniProtKB.
 GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
 GO:0007608; P:sensory perception of smell; TAS:UniProtKB.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0006833; P:water transport; TAS:Reactome. 
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.