CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004090
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 2 
Protein Synonyms/Alias
 EF-2 
Gene Name
 Ef2b 
Gene Synonyms/Alias
 CG2238 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
238FSEMYSEKFKIDVVKacetylation[1]
245KFKIDVVKLMNRLWGacetylation[1]
259GENFFNAKTKKWQKQacetylation[1]
310EKIGVTLKHEDKDKDacetylation[1]
323KDGKALLKTVMRTWLacetylation[1]
431KKEDLYEKAIQRTILacetylation[1]
475TGTITTFKDAHNMKVacetylation[1]
498VRVAVEPKNPADLPKacetylation[1]
624RARYLSEKYDYDVTEacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702] 
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 108 112 GTP (By similarity).
 NP_BIND 162 165 GTP (By similarity).
 MOD_RES 57 57 Phosphothreonine (By similarity).
 MOD_RES 59 59 Phosphothreonine (By similarity).
 MOD_RES 701 701 Diphthamide (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 844 AA 
Protein Sequence
MVNFTVDEIR GLMDKKRNIR NMSVIAHVDH GKSTLTDSLV SKAGIIAGAK AGETRFTDTR 60
KDEQERCITI KSTAISMYFE VEEKDLVFIT HPDQREKECK GFLINLIDSP GHVDFSSEVT 120
AALRVTDGAL VVVDCVSGVC VQTETVLRQA IAERIKPILF MNKMDRALLE LQLDAEELYQ 180
TFQRIVENVN VIIATYNDDG GPMGEVRVDP SKGSVGFGSG LHGWAFTLKQ FSEMYSEKFK 240
IDVVKLMNRL WGENFFNAKT KKWQKQKEAD NKRSFCMYIL DPIYKVFDAI MNYKKEEIGT 300
LLEKIGVTLK HEDKDKDGKA LLKTVMRTWL PAGEALLQMI AIHLPSPVVA QKYRMEMLYE 360
GPHDDEAAIA VKSCDPDGPL MMYISKMVPT SDKGRFYAFG RVFAGKVATG QKCRIMGPNY 420
TPGKKEDLYE KAIQRTILMM GRYVEAIEDV PSGNICGLVG VDQFLVKTGT ITTFKDAHNM 480
KVMKFSVSPV VRVAVEPKNP ADLPKLVEGL KRLAKSDPMV QCIIEESGEH IIAGAGELHL 540
EICLKDLEED HACIPLKKSD PVVSYRETVS EESDQMCLSK SPNKHNRLLM KALPMPDGLP 600
EDIDNGDVSA KDEFKARARY LSEKYDYDVT EARKIWCFGP DGTGPNFILD CTKSVQYLNE 660
IKDSVVAGFQ WASKEGILAD ENLRGVRFNI YDVTLHADAI HRGGGQIIPT TRRCLYAAAI 720
TAKPRLMEPV YLCEIQCPEV AVGGIYGVLN RRRGHVFEEN QVVGTPMFVV KAYLPVNESF 780
GFTADLRSNT GGQAFPQCVF DHWQVLPGDP SEPSSKPYAI VQDTRKRKGL KEGLPDLSQY 840
LDKL 844 
Gene Ontology
 GO:0005829; C:cytosol; ISS:FlyBase.
 GO:0005811; C:lipid particle; IDA:FlyBase.
 GO:0005875; C:microtubule associated complex; IDA:FlyBase.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; ISS:FlyBase.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0000022; P:mitotic spindle elongation; IMP:FlyBase. 
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.