ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P32324


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name EF2_YEAST
Primary accession number P32324
Secondary accession number Q6JEF7
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 93)
Name and origin of the protein
Protein name Elongation factor 2
Synonyms EF-2
Translation elongation factor 2
Eukaryotic elongation factor 2
eEF2
Ribosomal translocase
Gene names
Name: EFT1
OrderedLocusNames: YOR133W
ORFNames: O3317, YOR3317W
and
Name: EFT2
OrderedLocusNames: YDR385W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1 AND EFT2).
PubMed=1730643 [NCBI, ExPASy, EBI, Israel, Japan]
Perentesis J.P., Phan L.D., Laporte D.C., Livingston D.M., Bodley J.W.;
"Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling.";
J. Biol. Chem. 267:1190-1197(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1).
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(19960315)12:3<281::AID-YEA904>3.3.CO;2-F; PubMed=8904341 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
"Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames.";
Yeast 12:281-288(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1).
DOI=10.1002/(SICI)1097-0061(19970615)13:7<655::AID-YEA120>3.0.CO;2-I; PubMed=9200815 [NCBI, ExPASy, EBI, Israel, Japan]
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W.;
"DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
Yeast 13:655-672(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT2).
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1).
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[6]
PROTEIN SEQUENCE OF 411-422 AND 505-513.
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/elps.11501501210; PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-785.
DOI=10.1128/JCM.42.12.5624-5635.2004; PubMed=15583292 [NCBI, ExPASy, EBI, Israel, Japan]
Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.;
"Phylogeny and evolution of medical species of Candida and related taxa: a multigenic analysis.";
J. Clin. Microbiol. 42:5624-5635(2004).
[8]
PROTEIN SEQUENCE OF 686-700, AND DIPHTHAMIDE AT HIS-699.
PubMed=721806 [NCBI, ExPASy, EBI, Israel, Japan]
Van Ness B.G., Howard J.B., Bodley J.W.;
"Isolation and properties of the trypsin-derived ADP-ribosyl peptide from diphtheria toxin-modified yeast elongation factor 2.";
J. Biol. Chem. 253:8687-8690(1978).
[9]
PHOSPHORYLATION.
DOI=10.1016/0014-5793(91)81307-T; PubMed=1936278 [NCBI, ExPASy, EBI, Israel, Japan]
Donovan M.G., Bodley J.W.;
"Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endogenous kinase.";
FEBS Lett. 291:303-306(1991).
[10]
MUTAGENESIS OF GLY-701.
DOI=10.1006/bbrc.1993.1336; PubMed=8466491 [NCBI, ExPASy, EBI, Israel, Japan]
Kimata Y., Harashima S., Kohno K.;
"Expression of non-ADP-ribosylatable, diphtheria toxin-resistant elongation factor 2 in Saccharomyces cerevisiae.";
Biochem. Biophys. Res. Commun. 191:1145-1151(1993).
[11]
MUTAGENESIS OF HIS-699.
PubMed=8473309 [NCBI, ExPASy, EBI, Israel, Japan]
Phan L.D., Perentesis J.P., Bodley J.W.;
"Saccharomyces cerevisiae elongation factor 2. Mutagenesis of the histidine precursor of diphthamide yields a functional protein that is resistant to diphtheria toxin.";
J. Biol. Chem. 268:8665-8668(1993).
[12]
MUTAGENESIS OF ARG-180; VAL-187; GLN-490; TYR-521; SER-523; ILE-529; PRO-559; ALA-562; PRO-727; VAL-774 AND GLY-790.
DOI=10.1074/jbc.273.6.3148; PubMed=9452424 [NCBI, ExPASy, EBI, Israel, Japan]
Justice M.C., Hsu M.-J., Tse B., Ku T., Balkovec J., Schmatz D., Nielsen J.;
"Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis.";
J. Biol. Chem. 273:3148-3151(1998).
[13]
INTERACTION WITH RPL0.
PubMed=12410829 [NCBI, ExPASy, EBI, Israel, Japan]
Lalioti V.S., Perez-Fernandez J., Remacha M.A., Ballesta J.P.G.;
"Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components.";
Mol. Microbiol. 46:719-729(2002).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[15]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-82; SER-514; SER-569; SER-572 AND THR-763, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[17]
X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SORDARIN.
DOI=10.1038/nsb923; PubMed=12692531 [NCBI, ExPASy, EBI, Israel, Japan]
Joergensen R., Ortiz P.A., Carr-Schmid A., Nissen P., Kinzy T.G., Andersen G.R.;
"Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase.";
Nat. Struct. Biol. 10:379-385(2003).
[18]
STRUCTURE BY ELECTRON MICROSCOPY (11.7 ANGSTROMS) IN COMPLEX WITH 80S RIBOSOME AND SORDARIN, FUNCTION, AND INTERACTION WITH RPL9A; RPL12A; RPS23A; 18S RRNA AND 25S RRNA.
DOI=10.1038/sj.emboj.7600102; PubMed=14976550 [NCBI, ExPASy, EBI, Israel, Japan]
Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
"Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation.";
EMBO J. 23:1008-1019(2004).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF ADP-RIBOSYLATED FORM IN COMPLEX WITH GDP AND SORDARIN.
DOI=10.1074/jbc.M406218200; PubMed=15316019 [NCBI, ExPASy, EBI, Israel, Japan]
Joergensen R., Yates S.P., Teal D.J., Nilsson J., Prentice G.A., Merrill A.R., Andersen G.R.;
"Crystal structure of ADP-ribosylated ribosomal translocase from Saccharomyces cerevisiae.";
J. Biol. Chem. 279:45919-45925(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M59369; AAA21646.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M59370; AAA51398.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75041; CAA99332.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U32274; AAB64827.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28373; AAB64821.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X90518; CAA62116.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94335; CAA64052.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY497635; AAT12549.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41778; A41778.
RefSeq NP_010673.1; -.
NP_014776.1; -.
3D structure databases
PDB
1N0U; X-ray; 2.12 A; A=1-842.[ExPASy / RCSB / EBI]
1N0V; X-ray; 2.85 A; C/D=1-842.[ExPASy / RCSB / EBI]
1S1H; EM; 11.70 A; T=1-842.[ExPASy / RCSB / EBI]
1U2R; X-ray; 2.60 A; A=1-842.[ExPASy / RCSB / EBI]
1ZM2; X-ray; 3.07 A; A/C/E=1-842.[ExPASy / RCSB / EBI]
1ZM3; X-ray; 3.07 A; A/C/E=1-842.[ExPASy / RCSB / EBI]
1ZM4; X-ray; 2.90 A; A/C/E=1-842.[ExPASy / RCSB / EBI]
1ZM9; X-ray; 2.80 A; A/C/E=1-842.[ExPASy / RCSB / EBI]
2E1R; X-ray; 3.15 A; A=1-842.[ExPASy / RCSB / EBI]
2NPF; X-ray; 2.90 A; A/B=1-842.[ExPASy / RCSB / EBI]
2P8W; EM; 11.30 A; T=1-842.[ExPASy / RCSB / EBI]
2P8X; EM; 9.70 A; T=1-842.[ExPASy / RCSB / EBI]
2P8Y; EM; 11.70 A; T=1-842.[ExPASy / RCSB / EBI]
2P8Z; EM; 8.90 A; T=1-842.[ExPASy / RCSB / EBI]
2ZIT; X-ray; 3.00 A; A/C/E=1-842.[ExPASy / RCSB / EBI]
3B78; X-ray; 2.50 A; A/C/E=1-842.[ExPASy / RCSB / EBI]
3B82; X-ray; 2.35 A; A/C/E=1-842.[ExPASy / RCSB / EBI]
3B8H; X-ray; 2.50 A; A/C/E=1-842.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1N0U; -.
1N0V; -.
1S1H; -.
1U2R; -.
1ZM2; -.
1ZM3; -.
1ZM4; -.
1ZM9; -.
2E1R; -.
2NPF; -.
2P8W; -.
2P8X; -.
2P8Y; -.
2P8Z; -.
2ZIT; -.
3B78; -.
3B82; -.
3B8H; -.
ModBase P32324.
Protein-protein interaction databases
DIP DIP:4911N; -.
IntAct P32324; -.
2D gel databases
SWISS-2DPAGE P32324; -.
Organism-specific databases
CYGD YDR385w; -.
YOR133w; -.
SGD S000005659; EFT1.
S000002793; EFT2.
Yeast-GFP YOR133W.
Gene expression databases
GermOnline YDR385W; Saccharomyces cerevisiae.
YOR133W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005840; Cellular component: ribosome (traceable author statement from SGD).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from InterPro).
GO:0003924; Molecular function: GTPase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0043021; Molecular function: ribonucleoprotein binding (inferred from physical interaction from UniProtKB).
GO:0019843; Molecular function: rRNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003746; Molecular function: translation elongation factor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006414; Biological process: translational elongation (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000795; ProtSyn_GTP_bd.
IPR014721; Ribosomal_S5_D2-type_fold.
IPR005225; Small_GTP_bd.
IPR000640; Transl_elong_EFG/EF2_C.
IPR005517; Transl_elong_EFG/EF2_IV.
IPR004161; Transl_elong_EFTu/EF1A_2.
Graphical view of domain structure.
Gene3D G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 2.
Pfam PF00679; EFG_C; 1.
PF03764; EFG_IV; 1.
PF00009; GTP_EFTU; 1.
PF03144; GTP_EFTU_D2; 1.
Pfam graphical view of domain structure.
PRINTS PR00315; ELONGATNFCT.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS00301; EFACTOR_GTP; 1.
BLOCKS P32324.
ProtoNet P32324.
Genome annotation databases
Ensembl YDR385W; Saccharomyces cerevisiae. [Contig view]
YOR133W; Saccharomyces cerevisiae. [Contig view]
GeneID 851993; -.
854301; -.
KEGG sce:YDR385W; -.
sce:YOR133W; -.
Phylogenomic databases
HOGENOM P32324; -.
Other
LinkHub P32324; -.
NextBio 970163; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; RNA-binding; rRNA-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   842  842     Elongation factor 2. PRO_0000091024
NP_BIND   26    33  8     GTP (By similarity). 
NP_BIND   104   108  5     GTP (By similarity). 
NP_BIND   158   161  4     GTP (By similarity). 
MOD_RES   79    79        Phosphoserine. 
MOD_RES   82    82        Phosphoserine. 
MOD_RES   514   514        Phosphoserine. 
MOD_RES   569   569        Phosphoserine. 
MOD_RES   572   572        Phosphoserine. 
MOD_RES   699   699        Diphthamide. 
MOD_RES   763   763        Phosphothreonine. 
MUTAGEN   180   180        R->G: Causes resistance to fusidic acid and reduces sensitivity to sordarin. 
MUTAGEN   187   187        V->F: Causes resistance to fusidic acid and reduces sensitivity to sordarin. 
MUTAGEN   490   490        Q->E: Reduces sensitivity to sordarin. 
MUTAGEN   521   521        Y->D,N,S: Reduces sensitivity to fusidic acid and sordarin. 
MUTAGEN   523   523        S->F,P: Causes resistance to fusidic acid and sordarin. 
MUTAGEN   529   529        I->T: Reduces sensitivity to sordarin. 
MUTAGEN   559   559        P->L,R: Causes resistance to fusidic acid and sordarin. 
MUTAGEN   562   562        A->P: Reduces sensitivity to fusidic acid and causes resistance to sordarin. 
MUTAGEN   699   699        H->D,E,L,M: Prevents post-translational modification of this residue to diphthamide. Results in a functional protein that is resistant to diphtheria toxin. 
MUTAGEN   701   701        G->R: Prevents ADP-ribosylation of the diphthamide by diphtheria toxin. 
MUTAGEN   727   727        P->S: Causes resistance to sordarin. 
MUTAGEN   774   774        V->F: Causes resistance to sordarin. 
MUTAGEN   790   790        Missing: Causes resistance to fusidic acid and sordarin. 
HELIX   6    14  9      
HELIX   16    18  3      
STRAND   19    25  7      
HELIX   28    30  3      
HELIX   32    43  12      
STRAND   74    80  7      
HELIX   83    88  6      
STRAND   95   103  9      
HELIX   113   120  8      
STRAND   123   130  8      
TURN   131   133  3      
HELIX   137   148  12      
STRAND   152   158  7      
HELIX   160   165  6      
HELIX   171   192  22      
HELIX   195   197  3      
HELIX   204   206  3      
STRAND   209   213  5      
TURN   214   217  4      
STRAND   218   221  4      
HELIX   222   230  9      
TURN   231   234  4      
HELIX   237   243  7      
STRAND   245   247  3      
STRAND   249   251  3      
TURN   252   255  4      
STRAND   256   259  4      
HELIX   272   276  5      
HELIX   278   289  12      
HELIX   295   302  8      
HELIX   309   313  5      
HELIX   316   327  12      
HELIX   330   341  12      
HELIX   345   356  12      
STRAND   357   359  3      
HELIX   364   370  7