Elongation factor 2

Details

Name
Elongation factor 2
Synonyms
  • EF-2
  • EF2
Gene Name
EEF2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0020757|Elongation factor 2
MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTR
KDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALR
VTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQR
IVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKG
EGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKV
FDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPS
PVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGL
VSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLV
KTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEE
SGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHN
RLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPN
ILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQ
IIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTP
MFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRK
RKGLKEGIPALDNFLDKL
Number of residues
858
Molecular Weight
95337.385
Theoretical pI
6.82
GO Classification
Functions
GTP binding / GTPase activity / poly(A) RNA binding / protein kinase binding / translation elongation factor activity
Processes
cellular protein metabolic process / gene expression / hematopoietic progenitor cell differentiation / peptidyl-diphthamide biosynthetic process from peptidyl-histidine / positive regulation of translation / post-translational protein modification / translation / translational elongation
Components
aggresome / cytoplasm / cytosol / extracellular exosome / membrane / nucleus / plasma membrane / polysome / ribonucleoprotein complex
General Function
Translation elongation factor activity
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0020758|Elongation factor 2 (EEF2)
ATGGTGAACTTCACGGTAGACCAGATCCGCGCCATCATGGACAAGAAGGCCAACATCCGC
AACATGTCTGTCATCGCCCACGTGGACCATGGCAAGTCCACGCTGACAGACTCCCTGGTG
TGCAAGGCGGGCATCATCGCCTCGGCCCGGGCCGGGGAGACACGCTTCACTGATACCCGG
AAGGACGAGCAGGAGCGTTGCATCACCATCAAGTCAACTGCCATCTCCCTCTTCTACGAG
CTCTCGGAGAATGACTTGAACTTCATCAAGCAGAGCAAGGACGGTGCCGGCTTCCTCATC
AACCTCATTGACTCCCCCGGGCATGTCGACTTCTCCTCGGAGGTGACTGCTGCCCTCCGA
GTCACCGATGGCGCATTGGTGGTGGTGGACTGCGTGTCAGGCGTGTGCGTGCAGACGGAG
ACAGTGCTGCGGCAGGCCATTGCCGAGCGCATCAAGCCTGTGCTGATGATGAACAAGATG
GACCGCGCCCTGCTGGAGCTGCAGCTGGAGCCCGAGGAGCTCTACCAGACTTTCCAGCGC
ATCGTGGAGAACGTGAACGTCATCATCTCCACCTACGGCGAGGGCGAGAGCGGCCCCATG
GGCAACATCATGATCGATCCTGTCCTCGGTACCGTGGGCTTTGGGTCTGGCCTCCACGGG
TGGGCCTTCACCCTGAAGCAGTTTGCCGAGATGTATGTGGCCAAGTTCGCCGCCAAGGGG
GAGGGCCAGTTGGGGCCTGCCGAGCGGGCCAAGAAAGTAGAGGACATGATGAAGAAGCTG
TGGGGTGACAGGTACTTTGACCCAGCCAACGGCAAGTTCAGCAAGTCAGCCACCAGCCCC
GAAGGGAAGAAGCTGCCACGCACCTTCTGCCAGCTGATCCTGGACCCCATCTTCAAGGTG
TTTGATGCGATCATGAATTTCAAGAAAGAGGAGACAGCAAAACTGATAGAGAAACTGGAC
ATCAAACTGGACAGCGAGGACAAGGACAAAGAAGGCAAACCCCTGCTGAAGGCTGTGATG
CGCCGCTGGCTGCCTGCCGGAGACGCCTTGTTGCAGATGATCACCATCCACCTGCCCTCC
CCTGTGACGGCCCAGAAGTACCGCTGCGAGCTCCTGTACGAGGGGCCCCCGGACGACGAG
GCTGCCATGGGCATTAAAAGCTGTGACCCCAAAGGCCCTCTTATGATGTATATTTCCAAA
ATGGTGCCAACCTCCGACAAAGGTCGGTTCTACGCCTTTGGACGAGTCTTCTCGGGGCTG
GTCTCCACTGGCCTGAAGGTCAGGATCATGGGGCCCAACTATACCCCTGGGAAGAAGGAG
GACCTCTACCTGAAGCCAATCCAGAGAACAATCTTGATGATGGGCCGCTACGTGGAGCCC
ATCGAGGATGTGCCTTGTGGGAACATTGTGGGCCTCGTGGGCGTGGACCAGTTCCTGGTG
AAGACGGGCACCATCACCACCTTCGAGCACGCGCACAACATGCGGGTGATGAAGTTCAGC
GTCAGCCCTGTTGTCAGAGTGGCCGTGGAGGCCAAGAACCCGGCTGACCTGCCCAAGCTG
GTGGAGGGGCTGAAGCGGCTGGCCAAGTCCGACCCCATGGTGCAGTGCATCATCGAGGAG
TCGGGAGAGCATATCATCGCGGGCGCCGGCGAGCTGCACCTGGAGATCTGCCTGAAGGAC
CTGGAGGAGGACCACGCCTGCATCCCCATCAAGAAATCTGACCCGGTCGTCTCGTACCGC
GAGACGGTCAGTGAAGAGTCGAACGTGCTCTGCCTCTCCAAGTCCCCCAACAAGCACAAC
CGGCTGTACATGAAGGCGCGGCCCTTCCCCGACGGCCTGGCCGAGGACATCGATAAAGGC
GAGGTGTCCGCCCGTCAGGAGCTCAAGCAGCGGGCGCGCTACCTGGCCGAGAAGTACGAG
TGGGACGTGGCTGAGGCCCGCAAGATCTGGTGCTTTGGGCCCGACGGCACCGGCCCCAAC
ATCCTCACCGACATCACCAAGGGTGTGCAGTACCTCAACGAGATCAAGGACAGTGTGGTG
GCCGGCTTCCAGTGGGCCACCAAGGAGGGCGCACTGTGTGAGGAGAACATGCGGGGTGTG
CGCTTCGACGTCCACGACGTCACCCTGCACGCCGACGCCATCCACCGCGGAGGGGGCCAG
ATCATCCCCACAGCACGGCGCTGCCTCTATGCCAGTGTGCTGACCGCCCAGCCACGCCTC
ATGGAGCCCATCTACCTTGTGGAGATCCAGTGTCCAGAGCAGGTGGTCGGTGGCATCTAC
GGGGTTTTGAACAGGAAGCGGGGCCACGTGTTCGAGGAGTCCCAGGTGGCCGGCACCCCC
ATGTTTGTGGTCAAGGCCTATCTGCCCGTCAACGAGTCCTTTGGCTTCACCGCTGACCTG
AGGTCCAACACGGGCGGCCAGGCGTTCCCCCAGTGTGTGTTTGACCACTGGCAGATCCTG
CCCGGAGACCCCTTCGACAACAGCAGCCGCCCCAGCCAGGTGGTGGCGGAGACCCGCAAG
CGCAAGGGCCTGAAAGAAGGCATCCCTGCCCTGGACAACTTCCTGGACAAATTGTAG
Chromosome Location
19
Locus
19pter-q12
External Identifiers
ResourceLink
UniProtKB IDP13639
UniProtKB Entry NameEF2_HUMAN
GenBank Protein ID31106
GenBank Gene IDX51466
HGNC IDHGNC:3214
General References
  1. Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH: Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells. Biol Chem Hoppe Seyler. 1989 Oct;370(10):1071-5. [Article]
  2. Hanes J, Freudenstein J, Rapp G, Scheit KH: Construction of a plasmid containing the complete coding region of human elongation factor 2. Biol Chem Hoppe Seyler. 1992 Apr;373(4):201-4. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Rapp G, Mucha J, Einspanier R, Luck M, Scheit KH: Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2. Biol Chem Hoppe Seyler. 1988 Apr;369(4):247-50. [Article]
  5. Giannakopoulos NV, Luo JK, Papov V, Zou W, Lenschow DJ, Jacobs BS, Borden EC, Li J, Virgin HW, Zhang DE: Proteomic identification of proteins conjugated to ISG15 in mouse and human cells. Biochem Biophys Res Commun. 2005 Oct 21;336(2):496-506. [Article]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [Article]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  9. Yamashita A, Izumi N, Kashima I, Ohnishi T, Saari B, Katsuhata Y, Muramatsu R, Morita T, Iwamatsu A, Hachiya T, Kurata R, Hirano H, Anderson P, Ohno S: SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay. Genes Dev. 2009 May 1;23(9):1091-105. doi: 10.1101/gad.1767209. [Article]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
  11. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  12. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  13. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
  14. Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C: Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131. Epub 2012 Jan 5. [Article]
  15. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
  16. Hizli AA, Chi Y, Swanger J, Carter JH, Liao Y, Welcker M, Ryazanov AG, Clurman BE: Phosphorylation of eukaryotic elongation factor 2 (eEF2) by cyclin A-cyclin-dependent kinase 2 regulates its inhibition by eEF2 kinase. Mol Cell Biol. 2013 Feb;33(3):596-604. doi: 10.1128/MCB.01270-12. Epub 2012 Nov 26. [Article]
  17. Yao Q, Liu BQ, Li H, McGarrigle D, Xing BW, Zhou MT, Wang Z, Zhang JJ, Huang XY, Guo L: C-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2. J Biol Chem. 2014 May 2;289(18):12666-78. doi: 10.1074/jbc.M113.546481. Epub 2014 Mar 19. [Article]
  18. Davydova E, Ho AY, Malecki J, Moen A, Enserink JM, Jakobsson ME, Loenarz C, Falnes PO: Identification and characterization of a novel evolutionarily conserved lysine-specific methyltransferase targeting eukaryotic translation elongation factor 2 (eEF2). J Biol Chem. 2014 Oct 31;289(44):30499-510. doi: 10.1074/jbc.M114.601658. Epub 2014 Sep 17. [Article]
  19. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  20. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  21. Anger AM, Armache JP, Berninghausen O, Habeck M, Subklewe M, Wilson DN, Beckmann R: Structures of the human and Drosophila 80S ribosome. Nature. 2013 May 2;497(7447):80-5. doi: 10.1038/nature12104. [Article]
  22. Hekman KE, Yu GY, Brown CD, Zhu H, Du X, Gervin K, Undlien DE, Peterson A, Stevanin G, Clark HB, Pulst SM, Bird TD, White KP, Gomez CM: A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult. Hum Mol Genet. 2012 Dec 15;21(26):5472-83. doi: 10.1093/hmg/dds392. Epub 2012 Sep 21. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02059Adenosine-5-DiphosphoriboseexperimentalunknownDetails
DB03223DiphthamideexperimentalunknownDetails
DB04315Guanosine-5'-DiphosphateexperimentalunknownDetails
DB08348N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDEexperimentalunknownDetails
DB12688Moxetumomab pasudotoxapproved, investigationalyesinactivatorDetails
DB11823Esketamineapproved, investigationalunknowninhibitorDetails