CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002234
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 2 
Protein Synonyms/Alias
 EF-2 
Gene Name
 Eef2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
15QIRAIMDKKANIRNMacetylation[1]
42LTDSLVCKAGIIASAacetylation[1]
152QAIAERIKPVLMMNKacetylation[1]
159KPVLMMNKMDRALLEacetylation[1]
239YVAKFAAKGEGQLGAubiquitination[2]
251LGAAERAKKVEDMMKacetylation[1]
252GAAERAKKVEDMMKKacetylation[1]
258KKVEDMMKKLWGDRYacetylation[1]
259KVEDMMKKLWGDRYFacetylation[1]
272YFDPANGKFSKSANSacetylation[1]
272YFDPANGKFSKSANSubiquitination[2]
275PANGKFSKSANSPDGacetylation[1]
314FRKEETAKLIEKLDIacetylation[1]
318ETAKLIEKLDIKLDSacetylation[1]
322LIEKLDIKLDSEDKDacetylation[1]
328IKLDSEDKDKEGKPLacetylation[1]
337KEGKPLLKAVMRRWLacetylation[1]
426GVVSTGLKVRIMGPNacetylation[1]
445KKEDLYLKPIQRTILacetylation[1]
498AHNMRVMKFSVSPVVacetylation[1]
512VRVAVEAKNPADLPKacetylation[1]
512VRVAVEAKNPADLPKubiquitination[2]
845TRKRKGLKEGIPALDacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
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 54 54 Phosphothreonine (By similarity).
 MOD_RES 57 57 Phosphothreonine.
 MOD_RES 59 59 Phosphothreonine.
 MOD_RES 235 235 N6-acetyllysine (By similarity).
 MOD_RES 239 239 N6-acetyllysine (By similarity).
 MOD_RES 272 272 N6-acetyllysine (By similarity).
 MOD_RES 275 275 N6-acetyllysine (By similarity).
 MOD_RES 435 435 Phosphothreonine (By similarity).
 MOD_RES 445 445 N6-acetyllysine (By similarity).
 MOD_RES 502 502 Phosphoserine (By similarity).
 MOD_RES 715 715 Diphthamide.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 858 AA 
Protein Sequence
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR 60
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI NLIDSPGHVD FSSEVTAALR 120
VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLE PEELYQTFQR 180
IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG 240
EGQLGAAERA KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV 300
FDAIMNFRKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS 360
PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK MVPTSDKGRF YAFGRVFSGV 420
VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV 480
KTGTITTFEH AHNMRVMKFS VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE 540
SGEHIIAGAG ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN 600
RLYMKARPFP DGLAEDIDKG EVSARQELKA RARYLAEKYE WDVAEARKIW CFGPDGTGPN 660
ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ 720
IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP 780
MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK 840
RKGLKEGIPA LDNFLDKL 858 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005844; C:polysome; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:Compara.
 GO:0003746; F:translation elongation factor activity; TAS:RGD. 
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.