CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-033782
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 4 gamma 2 
Protein Synonyms/Alias
 Eukaryotic translation initiation factor 4 gamma, 2, isoform CRA_b 
Gene Name
 EIF4G2 
Gene Synonyms/Alias
 hCG_1991788 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41GNSEFLGKTPGQNAQubiquitination[1, 2]
49TPGQNAQKWIPARSTubiquitination[2]
71ANNSANEKERHDAIFubiquitination[3]
158AEGQPGQKQSTTFRRubiquitination[2, 3, 4, 5]
170FRRLLISKLQDEFENubiquitination[1, 2, 3, 4, 5, 6]
187RNVDVYDKRENPLLPubiquitination[1, 2, 5]
206QRAIAKIKMLGNIKFubiquitination[2]
212IKMLGNIKFIGELGKubiquitination[2]
219KFIGELGKLDLIHESubiquitination[2]
230IHESILHKCIKTLLEacetylation[6]
233SILHKCIKTLLEKKKacetylation[6]
245KKKRVQLKDMGEDLEubiquitination[2]
271RLDHERAKSLMDQYFubiquitination[2]
288MCSLMLSKELPARIRubiquitination[2]
313EHHWVPRKAFLDNGPubiquitination[2]
332QIRQDAVKDLGVFIPubiquitination[2]
362PFMPPRMKMDRDPLGubiquitination[2]
428QFGEMGGKFMKSQGLubiquitination[7]
431EMGGKFMKSQGLSQLubiquitination[2, 7]
464MPPRFSKKGQLNADEubiquitination[2]
520QTPQLGLKTNPPLIQubiquitination[2]
529NPPLIQEKPAKTSKKacetylation[6]
529NPPLIQEKPAKTSKKubiquitination[2, 6]
541SKKPPPSKEELLKLTacetylation[8]
575VREMRAPKHFLPEMLubiquitination[7]
739KLEKELLKQIKLDPSubiquitination[7]
813KQLLLSFKPVMQKFLubiquitination[2]
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] 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]
 [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]
 [6] 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]
 [7] 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]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Initiation factor; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 907 AA 
Protein Sequence
VESAIAEGGA SRFSASSGGG GSRGAPQHYP KTAGNSEFLG KTPGQNAQKW IPARSTRRDD 60
NSAANNSANE KERHDAIFRK VRGILNKLTP EKFDKLCLEL LNVGVESKLI LKGVILLIVD 120
KALEEPKYSS LYAQLCLRLA EDAPNFDGPA AEGQPGQKQS TTFRRLLISK LQDEFENRTR 180
NVDVYDKREN PLLPEEEEQR AIAKIKMLGN IKFIGELGKL DLIHESILHK CIKTLLEKKK 240
RVQLKDMGED LECLCQIMRT VGPRLDHERA KSLMDQYFAR MCSLMLSKEL PARIRFLLQD 300
TVELREHHWV PRKAFLDNGP KTINQIRQDA VKDLGVFIPA PMAQGMRSDF FLEGPFMPPR 360
MKMDRDPLGG LADMFGQMPG SGIGTGPGVI QDRFSPTMGR HRSNQLFNGH GGHIMPPTQS 420
QFGEMGGKFM KSQGLSQLYH NQSQGLLSQL QGQSKDMPPR FSKKGQLNAD EISLRPAQSF 480
LMNKNQVPKL QPQITMIPPS AQPPRTQTPP LGQTPQLGLK TNPPLIQEKP AKTSKKPPPS 540
KEELLKLTET VVTEYLNSGN ANEAVNGVRE MRAPKHFLPE MLSKVIILSL DRSDEDKEKA 600
SSLISLLKQE GIATSDNFMQ AFLNVLDQCP KLEVDIPLVK SYLAQFAARA IISELVSISE 660
LAQPLESGTH FPLFLLCLQQ LAKLQDREWL TELFQQSKVN MQKMLPEIDQ NKDRMLEILE 720
GKGLSFLFPL LKLEKELLKQ IKLDPSPQTI YKWIKDNISP KLHVDKGFVN ILMTSFLQYI 780
SSEVNPPSDE TDSSSAPSKE QLEQEKQLLL SFKPVMQKFL HDHVDLQVSA LYALQVHCYN 840
SNFPKGMLLR FFVHFYDMEI IEEEAFLAWK EDITQEFPGK GKALFQVNQW LTWLETAEEE 900
ESEEEAD 907 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
 GO:0016070; P:RNA metabolic process; IEA:InterPro. 
Interpro
 IPR016024; ARM-type_fold.
 IPR003891; Initiation_fac_eIF4g_MI.
 IPR016021; MIF4-like_typ_1/2/3.
 IPR003890; MIF4G-like_typ-3.
 IPR003307; W2_domain. 
Pfam
 PF02847; MA3
 PF02854; MIF4G
 PF02020; W2 
SMART
 SM00515; eIF5C
 SM00544; MA3
 SM00543; MIF4G 
PROSITE
 PS51366; MI
 PS51363; W2 
PRINTS