CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020872
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
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
17PENWRAFKALIAAQYacetylation[1]
132KQATENAKEEVKRILacetylation[2, 3]
136ENAKEEVKRILGLLDacetylation[2]
147GLLDTHLKTRTFLVGacetylation[1, 2, 4, 5, 6]
147GLLDTHLKTRTFLVGubiquitination[7]
208RAILGEVKLCEKMAQubiquitination[7]
212GEVKLCEKMAQFDAKacetylation[1, 5, 6]
212GEVKLCEKMAQFDAKubiquitination[7]
220MAQFDAKKFAESQPKacetylation[6]
277LAAEPKAKDPFAHLPubiquitination[7]
285DPFAHLPKSTFVLDEacetylation[5]
294TFVLDEFKRKYSNEDacetylation[6]
294TFVLDEFKRKYSNEDsuccinylation[6]
294TFVLDEFKRKYSNEDubiquitination[7]
401YESYTWRKLDPGSEEacetylation[6]
428GTFQHVGKAVNQGKIacetylation[1]
434GKAVNQGKIFK****acetylation[1, 2, 3, 4, 5, 6, 8, 9]
434GKAVNQGKIFK****ubiquitination[7]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [5] 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]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [7] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [8] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [9] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753] 
Functional Description
 Probably plays a role in anchoring the complex to other cellular components (By similarity). 
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 (By similarity).
 MOD_RES 147 147 N6-acetyllysine (By similarity).
 MOD_RES 434 434 N6-acetyllysine; alternate (By
 MOD_RES 434 434 N6-malonyllysine; alternate (By  
Keyword
 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 AKEEVKRILG LLDTHLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF 180
RQAFPNTNRW FLTCINQPQF RAILGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE 240
KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE 300
DTLSVALPYF WEHFDKDGWS LWYAEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV 360
ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE 420
GTFQHVGKAV NQGKIFK 437 
Gene Ontology
 GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
 GO:0009615; P:response to virus; IEA:Compara. 
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