CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009680
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
8MGCLGNSKTEDQRNEubiquitination[1, 2, 3]
17EDQRNEEKAQREANKubiquitination[4, 5]
53LGAGESGKSTIVKQMubiquitination[4]
58SGKSTIVKQMRILHVubiquitination[4]
88RSNSDGEKATKVQDIubiquitination[4]
91SDGEKATKVQDIKNNubiquitination[4]
96ATKVQDIKNNLKEAIubiquitination[4]
181CAQYFLDKIDVIKQAubiquitination[4]
186LDKIDVIKQADYVPSubiquitination[2, 3, 4, 5, 6, 7]
211TSGIFETKFQVDKVNubiquitination[4, 5, 6, 7]
216ETKFQVDKVNFHMFDubiquitination[5, 7, 8]
274QEALNLFKSIWNNRWubiquitination[2, 3, 4, 5, 6, 7, 8, 9, 10]
293SVILFLNKQDLLAEKubiquitination[4, 5, 7, 11]
300KQDLLAEKVLAGKSKubiquitination[2, 3, 4, 5, 6, 7, 11, 12, 13]
305AEKVLAGKSKIEDYFubiquitination[2, 4, 6, 7]
307KVLAGKSKIEDYFPEubiquitination[1, 2, 3, 4, 6, 7, 8]
338DPRVTRAKYFIRDEFubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] 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]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [12] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [13] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
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 EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK EAIETIVAAM SNLVPPVELA 120
NPENQFRVDY ILSVMNVPDF 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: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.