CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005818
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine nucleotide-binding protein subunit alpha-11 
Protein Synonyms/Alias
 G alpha-11; G-protein subunit alpha-11; Guanine nucleotide-binding protein G(y) subunit alpha 
Gene Name
 GNA11 
Gene Synonyms/Alias
 GA11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27RINAEIEKQLRRDKRubiquitination[1, 2, 3]
98IRAMETLKILYKYEQubiquitination[3, 4]
102ETLKILYKYEQNKANubiquitination[1, 2, 3, 4, 5, 6, 7]
107LYKYEQNKANALLIRubiquitination[1, 2, 3, 4]
158YQLSDSAKYYLTDVDubiquitination[2, 3, 4]
252ENRMEESKALFRTIIubiquitination[2]
345RFVFAAVKDTILQLNubiquitination[4]
354TILQLNLKEYNLV**ubiquitination[2, 4]
Reference
 [1] 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]
 [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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
Functional Description
 Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C. 
Sequence Annotation
 NP_BIND 46 53 GTP (By similarity).
 NP_BIND 180 186 GTP (By similarity).
 NP_BIND 205 209 GTP (By similarity).
 NP_BIND 274 277 GTP (By similarity).
 METAL 53 53 Magnesium (By similarity).
 METAL 186 186 Magnesium (By similarity).
 BINDING 331 331 GTP; via amide nitrogen (By similarity).
 MOD_RES 183 183 ADP-ribosylarginine; by cholera toxin (By
 LIPID 9 9 S-palmitoyl cysteine.
 LIPID 10 10 S-palmitoyl cysteine.  
Keyword
 ADP-ribosylation; Cell membrane; Complete proteome; Direct protein sequencing; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Palmitate; Reference proteome; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 359 AA 
Protein Sequence
MTLESMMACC LSDEVKESKR INAEIEKQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR 60
IIHGAGYSEE DKRGFTKLVY QNIFTAMQAM IRAMETLKIL YKYEQNKANA LLIREVDVEK 120
VTTFEHQYVS AIKTLWEDPG IQECYDRRRE YQLSDSAKYY LTDVDRIATL GYLPTQQDVL 180
RVRVPTTGII EYPFDLENII FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV 240
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE DKILYSHLVD YFPEFDGPQR 300
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV 359 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome.
 GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome.
 GO:0001664; F:G-protein coupled receptor binding; IBA:RefGenome.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004871; F:signal transducer activity; IBA:RefGenome.
 GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome.
 GO:0048066; P:developmental pigmentation; IEA:Compara.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:RefGenome.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0001508; P:regulation of action potential; IBA:RefGenome.
 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.
 IPR011025; GproteinA_insert.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00503; G-alpha 
SMART
 SM00275; G_alpha 
PROSITE
  
PRINTS
 PR00318; GPROTEINA.
 PR00442; GPROTEINAQ.