UniProt Accession

 EF2_HUMAN; P13639; B2RMP5; D6W618; Q58J86 

Genbank Protein ID

 X51466; Z11692; AY942181; CH471139; CH471139; BC126259; BC136313; M19997 

Genbank Nucleotide ID

 CAA35829.1; CAA77750.1; AAX34409.1; EAW69274.1; EAW69275.1; AAI26260.1; AAI36314.1; AAA50388.1 

Protein Name

 Elongation factor 2 

Protein Synonyms/Alias

 EF-2 

Gene Name

 EEF2 

Gene Synonyms/Alias

 EF2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
32	IAHVDHGKSTLTDSL	ubiquitination	[1, 2, 3, 4]
42	LTDSLVCKAGIIASA	acetylation	[4]
42	LTDSLVCKAGIIASA	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
90	ENDLNFIKQSKDGAG	ubiquitination	[3, 7, 12]
152	QAIAERIKPVLMMNK	ubiquitination	[1, 3, 7]
159	KPVLMMNKMDRALLE	ubiquitination	[1, 3, 6, 7, 11, 12]
235	FAEMYVAKFAAKGEG	acetylation	[13, 14, 15]
235	FAEMYVAKFAAKGEG	ubiquitination	[1, 3, 6, 7, 11]
239	YVAKFAAKGEGQLGP	acetylation	[4, 13]
239	YVAKFAAKGEGQLGP	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 16]
251	LGPAERAKKVEDMMK	ubiquitination	[3]
252	GPAERAKKVEDMMKK	acetylation	[4]
252	GPAERAKKVEDMMKK	ubiquitination	[3]
258	KKVEDMMKKLWGDRY	acetylation	[4]
258	KKVEDMMKKLWGDRY	ubiquitination	[3]
259	KVEDMMKKLWGDRYF	ubiquitination	[3]
272	YFDPANGKFSKSATS	acetylation	[4, 13, 14, 15]
272	YFDPANGKFSKSATS	ubiquitination	[1, 2, 3, 4, 6, 7, 9, 10, 11, 12]
275	PANGKFSKSATSPEG	acetylation	[4, 13, 14]
275	PANGKFSKSATSPEG	ubiquitination	[1, 2, 3, 4, 6, 7, 9, 11, 12, 16]
283	SATSPEGKKLPRTFC	ubiquitination	[3, 7]
284	ATSPEGKKLPRTFCQ	ubiquitination	[3]
308	FDAIMNFKKEETAKL	acetylation	[4, 15]
308	FDAIMNFKKEETAKL	ubiquitination	[1, 3, 6, 7, 10, 11, 12]
309	DAIMNFKKEETAKLI	ubiquitination	[3]
314	FKKEETAKLIEKLDI	acetylation	[4, 14, 15]
314	FKKEETAKLIEKLDI	ubiquitination	[3, 4, 7]
318	ETAKLIEKLDIKLDS	acetylation	[4, 13, 14, 15]
318	ETAKLIEKLDIKLDS	ubiquitination	[3, 4, 6, 10, 11, 12]
322	LIEKLDIKLDSEDKD	acetylation	[14]
322	LIEKLDIKLDSEDKD	ubiquitination	[1, 7, 12]
328	IKLDSEDKDKEGKPL	acetylation	[15]
328	IKLDSEDKDKEGKPL	ubiquitination	[12]
333	EDKDKEGKPLLKAVM	ubiquitination	[1, 11, 17]
337	KEGKPLLKAVMRRWL	acetylation	[15]
337	KEGKPLLKAVMRRWL	ubiquitination	[1, 6, 11]
386	DEAAMGIKSCDPKGP	ubiquitination	[1, 2, 3, 4, 7, 8]
391	GIKSCDPKGPLMMYI	ubiquitination	[2, 3, 4]
400	PLMMYISKMVPTSDK	ubiquitination	[1, 2, 3, 7, 12]
407	KMVPTSDKGRFYAFG	acetylation	[4]
407	KMVPTSDKGRFYAFG	methylation	[18]
407	KMVPTSDKGRFYAFG	ubiquitination	[3, 4, 10]
426	GLVSTGLKVRIMGPN	ubiquitination	[1, 3, 4, 6, 7, 8, 10, 11, 12]
438	GPNYTPGKKEDLYLK	ubiquitination	[3, 7, 12]
439	PNYTPGKKEDLYLKP	ubiquitination	[1, 3, 4, 7, 12]
445	KKEDLYLKPIQRTIL	acetylation	[4, 13, 14, 15, 19]
445	KKEDLYLKPIQRTIL	ubiquitination	[1, 3, 4, 6, 7, 10, 11, 12]
481	GVDQFLVKTGTITTF	ubiquitination	[3, 7]
498	AHNMRVMKFSVSPVV	ubiquitination	[1, 2, 3, 4, 6, 7, 10, 11, 12]
512	VRVAVEAKNPADLPK	acetylation	[15]
512	VRVAVEAKNPADLPK	ubiquitination	[1, 2, 3, 4, 7, 12, 16]
525	PKLVEGLKRLAKSDP	ubiquitination	[3, 4, 7]
571	DHACIPIKKSDPVVS	ubiquitination	[1, 2, 3, 4, 7, 9]
572	HACIPIKKSDPVVSY	ubiquitination	[1, 3, 4, 7, 9]
594	SNVLCLSKSPNKHNR	methylation	[20]
594	SNVLCLSKSPNKHNR	ubiquitination	[3, 4, 6, 11]
605	KHNRLYMKARPFPDG	ubiquitination	[2, 3, 12]
619	GLAEDIDKGEVSARQ	ubiquitination	[3]
638	RARYLAEKYEWDVAE	acetylation	[15]
638	RARYLAEKYEWDVAE	ubiquitination	[1, 2, 3, 4, 6, 7, 9, 10, 11, 12]
648	WDVAEARKIWCFGPD	ubiquitination	[1, 2, 3, 4, 6, 11]
676	VQYLNEIKDSVVAGF	ubiquitination	[3, 7, 12]
688	AGFQWATKEGALCEE	ubiquitination	[1, 7]
766	IYGVLNRKRGHVFEE	ubiquitination	[3, 12]
785	GTPMFVVKAYLPVNE	ubiquitination	[1]
845	TRKRKGLKEGIPALD	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 11, 12, 17]
857	ALDNFLDKL******	acetylation	[13]
857	ALDNFLDKL******	ubiquitination	[3, 7, 12]

Reference

 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [11] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [12] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [13] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [14] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [15] 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]
 [16] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [17] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [18] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [19] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [20] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077] 

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.
 MOD_RES 57 57 Phosphothreonine.
 MOD_RES 59 59 Phosphothreonine.
 MOD_RES 235 235 N6-acetyllysine.
 MOD_RES 239 239 N6-acetyllysine.
 MOD_RES 272 272 N6-acetyllysine.
 MOD_RES 275 275 N6-acetyllysine.
 MOD_RES 435 435 Phosphothreonine.
 MOD_RES 445 445 N6-acetyllysine.
 MOD_RES 502 502 Phosphoserine.
 MOD_RES 715 715 Diphthamide.  

Keyword

 3D-structure; 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

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005844; C:polysome; IEA:Compara.
 GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:Compara.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
 GO:0006414; P:translational elongation; TAS:Reactome. 

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.