CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031238
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 1-gamma 
Protein Synonyms/Alias
 cDNA FLJ56389, highly similar to Elongation factor 1-gamma 
Gene Name
 EEF1G 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67PENWRAFKALIAAQYubiquitination[1, 2, 3]
107LRKFPAGKVPAFEGDubiquitination[4]
182KQATENAKEEVRRILacetylation[3, 5]
182KQATENAKEEVRRILubiquitination[1]
197GLLDAYLKTRTFLVGacetylation[3, 5, 6]
197GLLDAYLKTRTFLVGubiquitination[1, 2, 3, 4, 7, 8, 9, 10]
258RAVLGEVKLCEKMAQacetylation[3]
258RAVLGEVKLCEKMAQubiquitination[1, 3, 4, 9, 10]
262GEVKLCEKMAQFDAKacetylation[3, 6]
262GEVKLCEKMAQFDAKubiquitination[1, 3, 4, 8, 9, 11]
269KMAQFDAKKFAETQPacetylation[6]
269KMAQFDAKKFAETQPubiquitination[4, 9]
270MAQFDAKKFAETQPKubiquitination[1, 3, 10]
303AERKEEKKAAAPAPEubiquitination[1]
327LAAEPKAKDPFAHLPubiquitination[3, 4]
335DPFAHLPKSTFVLDEacetylation[6]
335DPFAHLPKSTFVLDEubiquitination[8]
344TFVLDEFKRKYSNEDacetylation[3]
344TFVLDEFKRKYSNEDubiquitination[1, 2, 3, 4, 8, 9]
346VLDEFKRKYSNEDTLacetylation[6]
451YESYTWRKLDPGSEEacetylation[12]
451YESYTWRKLDPGSEEubiquitination[1, 9]
478GAFQHVGKAFNQGKIubiquitination[8]
484GKAFNQGKIFK****acetylation[3, 5, 6]
484GKAFNQGKIFK****malonylation[13]
484GKAFNQGKIFK****ubiquitination[1, 2, 3, 9]
487FNQGKIFK*******ubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [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] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [11] 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]
 [12] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [13] The first identification of lysine malonylation substrates and its regulatory enzyme.
 Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
 Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Elongation factor; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 487 AA 
Protein Sequence
MAERWVAPAV LRRARFASTF FLSPQIYAHK DGDLRSAFFI LSFKRGEFIP FLNWTLYTYP 60
ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA FEGDDGFCVF 120
ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI MHHNKQATEN 180
AKEEVRRILG LLDAYLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF RQAFPNTNRW 240
FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAETQPKKDT PRKEKGSREE KQKPQAERKE 300
EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE DTLSVALPYF 360
WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV ILFGTNNSSS 420
ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE GAFQHVGKAF 480
NQGKIFK 487 
Gene Ontology
 GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. 
Interpro
 IPR010987; Glutathione-S-Trfase_C-like.
 IPR004045; Glutathione_S-Trfase_N.
 IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
 IPR004046; GST_C.
 IPR012336; Thioredoxin-like_fold.
 IPR001662; Transl_elong_EF1_G_con. 
Pfam
 PF00647; EF1G
 PF00043; GST_C
 PF02798; GST_N 
SMART
  
PROSITE
 PS50040; EF1G_C
 PS50405; GST_CTER
 PS50404; GST_NTER 
PRINTS