CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041294
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine nucleotide binding protein (G protein), q polypeptide, isoform CRA_a 
Protein Synonyms/Alias
 Guanine nucleotide-binding protein G(q) subunit alpha 
Gene Name
 GNAQ 
Gene Synonyms/Alias
 hCG_1984513 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
50ENRMEESKALFRTIIubiquitination[1, 2, 3]
143RFVFAAVKDTILQLNubiquitination[4, 5]
152TILQLNLKEYNLV**ubiquitination[1, 5]
Reference
 [1] 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]
 [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] 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]
 [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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 157 AA 
Protein Sequence
MVDVGGQRSE RRKWIHCFEN VTSIMFLVAL SEYDQVLVES DNENRMEESK ALFRTIITYP 60
WFQNSSVILF LNKKDLLEEK IMYSHLVDYF PEYDGPQRDA QAAREFILKM FVDLNPDSDK 120
IIYSHFTCAT DTENIRFVFA AVKDTILQLN LKEYNLV 157 
Gene Ontology
 GO:0016020; C:membrane; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0004871; F:signal transducer activity; IEA:InterPro.
 GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IEA:Compara.
 GO:0007610; P:behavior; IEA:Compara.
 GO:0048066; P:developmental pigmentation; IEA:Compara.
 GO:0042733; P:embryonic digit morphogenesis; IEA:Compara.
 GO:0021884; P:forebrain neuron development; IEA:Compara.
 GO:0007215; P:glutamate receptor signaling pathway; IEA:Compara.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0016322; P:neuron remodeling; IEA:Compara.
 GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IEA:Compara.
 GO:0009791; P:post-embryonic development; IEA:Compara.
 GO:0001508; P:regulation of action potential; IEA:Compara.
 GO:0045634; P:regulation of melanocyte differentiation; IEA:Compara.
 GO:0001501; P:skeletal system development; IEA:Compara. 
Interpro
 IPR000654; Gprotein_alpha_Q.
 IPR001019; Gprotein_alpha_su.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00503; G-alpha 
SMART
 SM00275; G_alpha 
PROSITE
  
PRINTS
 PR00318; GPROTEINA.
 PR00442; GPROTEINAQ.