CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-033967
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor Tu 
Protein Synonyms/Alias
  
Gene Name
 Gm9755 
Gene Synonyms/Alias
 mCG_1048875 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
55KKTYVRDKPHVNVGTacetylation[1]
79TLTAAITKILAEGGGacetylation[2, 3]
88LAEGGGAKFKKYEEIacetylation[3, 4]
88LAEGGGAKFKKYEEIsuccinylation[4]
88LAEGGGAKFKKYEEIubiquitination[5]
90EGGGAKFKKYEEIDNacetylation[3]
91GGGAKFKKYEEIDNAacetylation[3]
234RDPELGVKSVQKLLDacetylation[4]
234RDPELGVKSVQKLLDsuccinylation[4]
238LGVKSVQKLLDAVDTacetylation[3]
256VPTRDLDKPFLLPVEacetylation[1, 2, 3, 4, 6, 7, 8]
286LERGILKKGDECELLacetylation[4]
286LERGILKKGDECELLsuccinylation[4]
297CELLGHNKNIRTVVTacetylation[1]
342RRGLVMVKPGSIQPHacetylation[3]
361AQVYILSKEEGGRHKacetylation[1, 3]
447PAMTEEDKNIKWS**acetylation[3, 4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [7] 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]
 [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
 This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity). 
Sequence Annotation
  
Keyword
 Complete proteome; Elongation factor; GTP-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 452 AA 
Protein Sequence
MAAATLLRAT PRFSGLCASP TPFLQGRLRP LKAPASPFLC RGLAVEAKKT YVRDKPHVNV 60
GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR 120
HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDSPMPQ TREHLLLAKQ IGVEHVVVYV 180
NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPVIVGSA LCALEQRDPE LGVKSVQKLL 240
DAVDTYIPVP TRDLDKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC ELLGHNKNIR 300
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIQPHQ KVEAQVYILS 360
KEEGGRHKPF VSHFMPVMFS LTWDMACRVI LPPGKELAMP GEDLKLSLIL RQPMILEKGQ 420
RFTLRDGNKT IGTGLVTDVP AMTEEDKNIK WS 452 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR004541; Transl_elong_EFTu/EF1A_bac/org.
 IPR004160; Transl_elong_EFTu/EF1A_C.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF03143; GTP_EFTU_D3 
SMART
  
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.