CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006086
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 2 
Protein Synonyms/Alias
 EF-2; Eukaryotic elongation factor 2; eEF2; Ribosomal translocase; Translation elongation factor 2 
Gene Name
 EFT1; EFT2 
Gene Synonyms/Alias
 YOR133W; O3317; YOR3317W; YDR385W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
15QMRSLMDKVTNVRNMacetylation[1]
15QMRSLMDKVTNVRNMubiquitination[2]
50AGIISAAKAGEARFTubiquitination[2]
87EMSDEDVKEIKQKTDacetylation[1]
87EMSDEDVKEIKQKTDubiquitination[2]
152QALGERIKPVVVINKacetylation[1]
152QALGERIKPVVVINKubiquitination[2]
159KPVVVINKVDRALLEacetylation[1]
159KPVVVINKVDRALLEubiquitination[2]
171LLELQVSKEDLYQTFubiquitination[2]
253GDSFFNPKTKKWTNKacetylation[1]
260KTKKWTNKDTDAEGKacetylation[1]
260KTKKWTNKDTDAEGKubiquitination[2]
267KDTDAEGKPLERAFNacetylation[1]
267KDTDAEGKPLERAFNubiquitination[2]
292FTAIMNFKKDEIPVLacetylation[1]
293TAIMNFKKDEIPVLLacetylation[1]
308EKLEIVLKGDEKDLEacetylation[1]
312IVLKGDEKDLEGKALacetylation[1]
317DEKDLEGKALLKVVMacetylation[1]
317DEKDLEGKALLKVVMubiquitination[2]
321LEGKALLKVVMRKFLacetylation[1]
326LLKVVMRKFLPAADAubiquitination[2]
370DANCIAIKNCDPKADubiquitination[2]
391KMVPTSDKGRFYAFGubiquitination[2]
406RVFAGTVKSGQKVRIubiquitination[2]
423PNYVPGKKDDLFIKAubiquitination[2]
429KKDDLFIKAIQRVVLacetylation[1]
479SETAHNMKVMKFSVSacetylation[1]
479SETAHNMKVMKFSVSubiquitination[2]
496VQVAVEVKNANDLPKacetylation[1]
496VQVAVEVKNANDLPKubiquitination[2]
509PKLVEGLKRLSKSDPacetylation[3]
509PKLVEGLKRLSKSDPubiquitination[2]
578SSQTALSKSPNKHNRubiquitination[2]
589KHNRIYLKAEPIDEEacetylation[1]
632WDVTDARKIWCFGPDacetylation[1]
632WDVTDARKIWCFGPDubiquitination[2]
769GTPLFTVKAYLPVNEubiquitination[2]
814DPLDPTSKAGEIVLAubiquitination[2]
829ARKRHGMKEEVPGWQubiquitination[2]
841GWQEYYDKL******acetylation[1]
841GWQEYYDKL******ubiquitination[2, 4]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A.
 Zhang Y, Liu S, Lajoie G, Merrill AR.
 Biochem J. 2008 Jul 1;413(1):163-74. [PMID: 18373493]
 [4] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. 
Sequence Annotation
 NP_BIND 26 33 GTP (By similarity).
 NP_BIND 104 108 GTP (By similarity).
 NP_BIND 158 161 GTP (By similarity).
 MOD_RES 579 579 Phosphoserine.
 MOD_RES 699 699 Diphthamide.
 MOD_RES 713 713 Phosphothreonine.
 MOD_RES 763 763 Phosphothreonine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding; rRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 842 AA 
Protein Sequence
MVAFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR 60
KDEQERGITI KSTAISLYSE MSDEDVKEIK QKTDGNSFLI NLIDSPGHVD FSSEVTAALR 120
VTDGALVVVD TIEGVCVQTE TVLRQALGER IKPVVVINKV DRALLELQVS KEDLYQTFAR 180
TVESVNVIVS TYADEVLGDV QVYPARGTVA FGSGLHGWAF TIRQFATRYA KKFGVDKAKM 240
MDRLWGDSFF NPKTKKWTNK DTDAEGKPLE RAFNMFILDP IFRLFTAIMN FKKDEIPVLL 300
EKLEIVLKGD EKDLEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA YRAEQLYEGP 360
ADDANCIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV FAGTVKSGQK VRIQGPNYVP 420
GKKDDLFIKA IQRVVLMMGR FVEPIDDCPA GNIIGLVGID QFLLKTGTLT TSETAHNMKV 480
MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI 540
CLQDLEHDHA GVPLKISPPV VAYRETVESE SSQTALSKSP NKHNRIYLKA EPIDEEVSLA 600
IENGIINPRD DFKARARIMA DDYGWDVTDA RKIWCFGPDG NGPNLVIDQT KAVQYLHEIK 660
DSVVAAFQWA TKEGPIFGEE MRSVRVNILD VTLHADAIHR GGGQIIPTMR RATYAGFLLA 720
DPKIQEPVFL VEIQCPEQAV GGIYSVLNKK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF 780
TGELRQATGG QAFPQMVFDH WSTLGSDPLD PTSKAGEIVL AARKRHGMKE EVPGWQEYYD 840
KL 842 
Gene Ontology
 GO:0005840; C:ribosome; TAS:SGD.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
 GO:0003746; F:translation elongation factor activity; TAS:SGD.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0045901; P:positive regulation of translational elongation; IMP:SGD. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR009022; EFG_III-V.
 IPR000640; EFG_V.
 IPR027417; P-loop_NTPase.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR005225; Small_GTP-bd_dom.
 IPR005517; Transl_elong_EFG/EF2_IV.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00679; EFG_C
 PF03764; EFG_IV
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
 SM00838; EFG_C
 SM00889; EFG_IV 
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.