CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002178
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine nucleotide-binding protein G(i) subunit alpha-2 
Protein Synonyms/Alias
 Adenylate cyclase-inhibiting G alpha protein 
Gene Name
 GNAI2 
Gene Synonyms/Alias
 GNAI2B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21ERSKMIDKNLREDGEubiquitination[1, 2]
35EKAAREVKLLLLGAGubiquitination[1, 2, 3, 4]
46LGAGESGKSTIVKQMubiquitination[1, 2]
51SGKSTIVKQMKIIHEubiquitination[2]
54STIVKQMKIIHEDGYubiquitination[2]
193VETHFTFKDLHFKMFubiquitination[2, 5]
198TFKDLHFKMFDVGGQubiquitination[1, 2, 5]
249NRMHESMKLFDSICNubiquitination[1, 2]
272IILFLNKKDLFEEKIubiquitination[2]
296PEYTGANKYDEAASYubiquitination[1, 2, 6]
307AASYIQSKFEDLNKRubiquitination[1, 3, 5]
313SKFEDLNKRKDTKEIubiquitination[2]
315FEDLNKRKDTKEIYTubiquitination[2]
318LNKRKDTKEIYTHFTubiquitination[2]
350VIIKNNLKDCGLF**ubiquitination[2, 6]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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] 
Functional Description
 Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division. 
Sequence Annotation
 NP_BIND 40 47 GTP (By similarity).
 NP_BIND 176 182 GTP (By similarity).
 NP_BIND 201 205 GTP (By similarity).
 NP_BIND 270 273 GTP (By similarity).
 METAL 47 47 Magnesium (By similarity).
 METAL 182 182 Magnesium (By similarity).
 BINDING 327 327 GTP; via amide nitrogen (By similarity).
 MOD_RES 179 179 ADP-ribosylarginine; by cholera toxin (By
 MOD_RES 352 352 ADP-ribosylcysteine; by pertussis toxin
 LIPID 2 2 N-myristoyl glycine (Probable).
 LIPID 3 3 S-palmitoyl cysteine (By similarity).  
Keyword
 ADP-ribosylation; Alternative splicing; Cell cycle; Cell division; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate; Reference proteome; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 355 AA 
Protein Sequence
MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG 60
YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPSR ADDARQLFAL SCTAEEQGVL 120
PDDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV 180
KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE 240
MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT HSPLTICFPE YTGANKYDEA 300
ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF 355 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome.
 GO:0045121; C:membrane raft; IEA:Compara.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0005634; C:nucleus; IEA:Compara.
 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; IBA:RefGenome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004871; F:signal transducer activity; IBA:RefGenome.
 GO:0000186; P:activation of MAPKK activity; IEA:Compara.
 GO:0001973; P:adenosine receptor signaling pathway; IBA:RefGenome.
 GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:Reactome.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IMP:UniProtKB.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0007213; P:G-protein coupled acetylcholine receptor signaling pathway; IEA:Compara.
 GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:RefGenome.
 GO:0007243; P:intracellular protein kinase cascade; IEA:Compara.
 GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
 GO:0050805; P:negative regulation of synaptic transmission; IEA:Compara.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0051924; P:regulation of calcium ion transport; IEA:Compara.
 GO:0007584; P:response to nutrient; TAS:ProtInc.
 GO:0007268; P:synaptic transmission; TAS:Reactome. 
Interpro
 IPR001408; Gprotein_alpha_I.
 IPR001019; Gprotein_alpha_su.
 IPR011025; GproteinA_insert.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00503; G-alpha 
SMART
 SM00275; G_alpha 
PROSITE
  
PRINTS
 PR00318; GPROTEINA.
 PR00441; GPROTEINAI.