CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001267
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 3 subunit G 
Protein Synonyms/Alias
 eIF3g; Eukaryotic translation initiation factor 3 RNA-binding subunit; eIF-3 RNA-binding subunit; Eukaryotic translation initiation factor 3 subunit 4; eIF-3-delta; eIF3 p42; eIF3 p44 
Gene Name
 EIF3G 
Gene Synonyms/Alias
 EIF3S4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
65EVINGNIKTVTEYKIubiquitination[1, 2]
71IKTVTEYKIDEDGKKubiquitination[3]
78KIDEDGKKFKIVRTFubiquitination[3]
148EEEDPMNKLKGQKIVubiquitination[3]
150EDPMNKLKGQKIVSCubiquitination[3]
161IVSCRICKGDHWTTRacetylation[4]
161IVSCRICKGDHWTTRubiquitination[3]
172WTTRCPYKDTLGPMQacetylation[4]
180DTLGPMQKELAEQLGubiquitination[1, 2, 5]
193LGLSTGEKEKLPGELacetylation[4]
193LGLSTGEKEKLPGELubiquitination[3]
195LSTGEKEKLPGELEPubiquitination[3, 5]
209PVQATQNKTGKYVPPubiquitination[1, 2, 5]
212ATQNKTGKYVPPSLRacetylation[6]
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] 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]
 [3] 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]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [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] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330
Functional Description
 Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. This subunit can bind 18S rRNA. 
Sequence Annotation
 DOMAIN 239 317 RRM.
 MOD_RES 38 38 Phosphothreonine.
 MOD_RES 41 41 Phosphothreonine.
 MOD_RES 42 42 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 320 AA 
Protein Sequence
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSPEPELLPG APLPPPKEVI 60
NGNIKTVTEY KIDEDGKKFK IVRTFRIETR KASKAVARRK NWKKFGNSEF DPPGPNVATT 120
TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK 180
ELAEQLGLST GEKEKLPGEL EPVQATQNKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT 240
IRVTNLSEDT RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV 300
SGFGYDHLIL NVEWAKPSTN 320 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:HAMAP.
 GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:HAMAP.
 GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003743; F:translation initiation factor activity; IEA:HAMAP.
 GO:0001731; P:formation of translation preinitiation complex; IEA:HAMAP.
 GO:0006446; P:regulation of translational initiation; IEA:HAMAP.
 GO:0006413; P:translational initiation; IDA:UniProtKB. 
Interpro
 IPR017334; eIF3_g.
 IPR024675; eIF3g_N.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF12353; eIF3g
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS