CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005527
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 1-gamma 
Protein Synonyms/Alias
 EF-1-gamma; eEF-1B gamma 
Gene Name
 EEF1G 
Gene Synonyms/Alias
 EF1G; PRO1608 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17PENWRAFKALIAAQYubiquitination[1, 2]
132KQATENAKEEVRRILacetylation[3]
132KQATENAKEEVRRILubiquitination[1]
147GLLDAYLKTRTFLVGacetylation[3, 4]
147GLLDAYLKTRTFLVGubiquitination[1, 2, 5, 6, 7, 8, 9, 10]
208RAVLGEVKLCEKMAQubiquitination[1, 8]
212GEVKLCEKMAQFDAKubiquitination[1, 7, 8, 9, 10]
219KMAQFDAKKFAETQPubiquitination[11]
220MAQFDAKKFAETQPKubiquitination[1]
253AERKEEKKAAAPAPEubiquitination[1]
285DPFAHLPKSTFVLDEubiquitination[7, 10]
294TFVLDEFKRKYSNEDubiquitination[1, 2, 7, 10]
401YESYTWRKLDPGSEEubiquitination[1]
428GAFQHVGKAFNQGKIubiquitination[7, 10]
434GKAFNQGKIFK****acetylation[3]
434GKAFNQGKIFK****ubiquitination[1, 2, 9]
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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [6] 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]
 [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] 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]
 [9] 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]
 [10] 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]
 [11] 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
Functional Description
 Probably plays a role in anchoring the complex to other cellular components. 
Sequence Annotation
 DOMAIN 2 87 GST N-terminal.
 DOMAIN 88 216 GST C-terminal.
 DOMAIN 276 437 EF-1-gamma C-terminal.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 147 147 N6-acetyllysine.
 MOD_RES 434 434 N6-acetyllysine; alternate.
 MOD_RES 434 434 N6-malonyllysine; alternate.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Elongation factor; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 437 AA 
Protein Sequence
MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA 60
FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI 120
MHHNKQATEN AKEEVRRILG LLDAYLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF 180
RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAETQPKKDT PRKEKGSREE 240
KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE 300
DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV 360
ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE 420
GAFQHVGKAF NQGKIFK 437 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
 GO:0009615; P:response to virus; IEP:UniProtKB. 
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