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Elongation factor 1-alpha (EF-1-alpha) (Eukaryotic elongation factor 1A) (eEF1A) (Translation elongation factor 1A)

 EF1A_YEAST              Reviewed;         458 AA.
P02994; D6VQB6; Q7Z7U8; Q7Z8Q8; Q7Z8Q9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 202.
RecName: Full=Elongation factor 1-alpha;
Short=EF-1-alpha;
AltName: Full=Eukaryotic elongation factor 1A;
Short=eEF1A;
AltName: Full=Translation elongation factor 1A;
Name=TEF1; OrderedLocusNames=YPR080W; ORFNames=P9513.7;
and
Name=TEF2; OrderedLocusNames=YBR118W; ORFNames=YBR0913;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).
PubMed=6383821;
Nagata S., Nagashima K., Tsunetsugu-Yokota Y., Fujimura K.,
Miyazaki M., Kaziro Y.;
"Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast:
nucleotide sequence of one of the two genes for EF-1 alpha from
Saccharomyces cerevisiae.";
EMBO J. 3:1825-1830(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF2).
PubMed=6396088;
Schirmaier F., Philippsen P.;
"Identification of two genes coding for the translation elongation
factor EF-1 alpha of S. cerevisiae.";
EMBO J. 3:3311-3315(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).
PubMed=2982849;
Cottrelle P., Thiele D., Price V.L., Memet S., Micouin J.-Y.,
Marck C., Buhler J.-M., Sentenac A., Fromageot P.;
"Cloning, nucleotide sequence, and expression of one of two genes
coding for yeast elongation factor 1 alpha.";
J. Biol. Chem. 260:3090-3096(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1 AND TEF2).
PubMed=3026912; DOI=10.1016/0378-1119(86)90024-7;
Nagashima K., Kasai M., Nagata S., Kaziro Y.;
"Structure of the two genes coding for polypeptide chain elongation
factor 1 alpha (EF-1 alpha) from Saccharomyces cerevisiae.";
Gene 45:265-273(1986).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF2).
STRAIN=ATCC 204508 / S288c;
PubMed=7900426; DOI=10.1002/yea.320101014;
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
"Analysis of a 70 kb region on the right arm of yeast chromosome II.";
Yeast 10:1363-1381(1994).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF2).
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF1).
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[8]
GENOME REANNOTATION (TEF1 AND TEF2).
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-237 (TEF1).
STRAIN=ATCC 204508 / S288c;
PubMed=7916691; DOI=10.1111/j.1432-1033.1993.tb18268.x;
Schaaff-Gerstenschlaeger I., Mannhaupt G., Vetter I., Zimmermann F.K.,
Feldmann H.;
"TKL2, a second transketolase gene of Saccharomyces cerevisiae.
Cloning, sequence and deletion analysis of the gene.";
Eur. J. Biochem. 217:487-492(1993).
[11]
PARTIAL PROTEIN SEQUENCE, AND METHYLATION AT LYS-30; LYS-79; LYS-316
AND LYS-390.
PubMed=8476932; DOI=10.1016/0167-4838(93)90281-U;
Cavallius J., Zoll W., Chakraburtty K., Merrick W.C.;
"Characterization of yeast EF-1 alpha: non-conservation of post-
translational modifications.";
Biochim. Biophys. Acta 1163:75-80(1993).
[12]
PROTEIN SEQUENCE OF 6-20, AND INTERACTION WITH SRV2.
PubMed=9125210; DOI=10.1006/bbrc.1997.6326;
Yanagihara C., Shinkai M., Kariya K., Yamawaki-Kataoka Y., Hu C.-D.,
Masuda T., Kataoka T.;
"Association of elongation factor 1 alpha and ribosomal protein L3
with the proline-rich region of yeast adenylyl cyclase-associated
protein CAP.";
Biochem. Biophys. Res. Commun. 232:503-507(1997).
[13]
PROTEIN SEQUENCE OF 56-61 AND 265-280.
STRAIN=ATCC 44827 / SKQ2N;
PubMed=9509572;
DOI=10.1002/(SICI)1097-0061(199712)13:16<1519::AID-YEA211>3.0.CO;2-U;
Norbeck J., Blomberg A.;
"Two-dimensional electrophoretic separation of yeast proteins using a
non-linear wide range (pH 3-10) immobilized pH gradient in the first
dimension; reproducibility and evidence for isoelectric focusing of
alkaline (pI > 7) proteins.";
Yeast 13:1519-1534(1997).
[14]
PROTEIN SEQUENCE OF 70-77 AND 80-87.
PubMed=3882705;
Thiele D., Cottrelle P., Iborra F., Buhler J.-M., Sentenac A.,
Fromageot P.;
"Elongation factor 1 alpha from Saccharomyces cerevisiae. Rapid large-
scale purification and molecular characterization.";
J. Biol. Chem. 260:3084-3089(1985).
[15]
PROTEIN SEQUENCE OF 211-214 AND 289-308, INTERACTION WITH BNI1, AND
IDENTIFICATION IN A COMPLEX WITH BNI1 AND PROFILIN.
PubMed=9591785; DOI=10.1038/sj.onc.1201724;
Umikawa M., Tanaka K., Kamei T., Shimizu K., Imamura H., Sasaki T.,
Takai Y.;
"Interaction of Rho1p target Bni1p with F-actin-binding elongation
factor 1alpha: implication in Rho1p-regulated reorganization of the
actin cytoskeleton in Saccharomyces cerevisiae.";
Oncogene 16:2011-2016(1998).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-397.
STRAIN=ATCC 13507 / CBS 459 / NRRL Y-12649,
ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632,
ATCC 24702 / NRRL Y-2034,
Diastaticus / ATCC 13007 / CBS 1782 / IFO 1046 / NRRL Y-2416, and
NRRL YB-210;
PubMed=12748053; DOI=10.1016/S1567-1356(03)00012-6;
Kurtzman C.P., Robnett C.J.;
"Phylogenetic relationships among yeasts of the 'Saccharomyces
complex' determined from multigene sequence analyses.";
FEMS Yeast Res. 3:417-432(2003).
[17]
FUNCTION, AND MUTAGENESIS OF GLU-286 AND GLU-317.
PubMed=3066688;
Sandbaken M.G., Culbertson M.R.;
"Mutations in elongation factor EF-1 alpha affect the frequency of
frameshifting and amino acid misincorporation in Saccharomyces
cerevisiae.";
Genetics 120:923-934(1988).
[18]
INTERACTION WITH YEF3, AND MUTAGENESIS OF GLU-122.
PubMed=9990316; DOI=10.1046/j.1432-1327.1998.2580986.x;
Kovalchuke O., Kambampati R., Pladies E., Chakraburtty K.;
"Competition and cooperation amongst yeast elongation factors.";
Eur. J. Biochem. 258:986-993(1998).
[19]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASN-153 AND ASP-156.
PubMed=9786872; DOI=10.1074/jbc.273.44.28752;
Cavallius J., Merrick W.C.;
"Site-directed mutagenesis of yeast eEF1A. Viable mutants with altered
nucleotide specificity.";
J. Biol. Chem. 273:28752-28758(1998).
[20]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH ZPR1.
PubMed=9852145; DOI=10.1083/jcb.143.6.1471;
Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.;
"Interaction of ZPR1 with translation elongation factor-1alpha in
proliferating cells.";
J. Cell Biol. 143:1471-1484(1998).
[21]
MUTAGENESIS OF ASN-153 AND ASP-156.
PubMed=10514524; DOI=10.1074/jbc.274.42.30297;
Carr-Schmid A., Durko N., Cavallius J., Merrick W.C., Kinzy T.G.;
"Mutations in a GTP-binding motif of eukaryotic elongation factor 1A
reduce both translational fidelity and the requirement for nucleotide
exchange.";
J. Biol. Chem. 274:30297-30302(1999).
[22]
FUNCTION IN NUCLEAR EXPORT OF AMINOACYL-TRNAS.
PubMed=10766739;
Grosshans H., Hurt E.C., Simos G.;
"An aminoacylation-dependent nuclear tRNA export pathway in yeast.";
Genes Dev. 14:830-840(2000).
[23]
METHYLATION AT LYS-458.
PubMed=10973948; DOI=10.1074/jbc.M001005200;
Zobel-Thropp P., Yang M.C., Machado L., Clarke S.;
"A novel post-translational modification of yeast elongation factor
1A. Methylesterification at the C-terminus.";
J. Biol. Chem. 275:37150-37158(2000).
[24]
INTERACTION WITH ACTIN.
PubMed=11290701;
Munshi R., Kandl K.A., Carr-Schmid A., Whitacre J.L., Adams A.E.M.,
Kinzy T.G.;
"Overexpression of translation elongation factor 1A affects the
organization and function of the actin cytoskeleton in yeast.";
Genetics 157:1425-1436(2001).
[25]
S-THIOLATION.
PubMed=12755685; DOI=10.1042/BJ20030414;
Shenton D., Grant C.M.;
"Protein S-thiolation targets glycolysis and protein synthesis in
response to oxidative stress in the yeast Saccharomyces cerevisiae.";
Biochem. J. 374:513-519(2003).
[26]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
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).
[27]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
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).
[28]
FUNCTION, MUTAGENESIS OF ASP-156, AND INTERACTION WITH RPT1.
PubMed=15601860; DOI=10.1128/MCB.25.1.403-413.2005;
Chuang S.-M., Chen L., Lambertson D., Anand M., Kinzy T.G., Madura K.;
"Proteasome-mediated degradation of cotranslationally damaged proteins
involves translation elongation factor 1A.";
Mol. Cell. Biol. 25:403-413(2005).
[29]
INTERACTION WITH CEX1.
PubMed=17203074; DOI=10.1038/sj.emboj.7601493;
McGuire A.T., Mangroo D.;
"Cex1p is a novel cytoplasmic component of the Saccharomyces
cerevisiae nuclear tRNA export machinery.";
EMBO J. 26:288-300(2007).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-72; THR-82;
SER-163 AND THR-430, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[31]
INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18086883; DOI=10.1128/MCB.01035-07;
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
Pemberton L.F.;
"Phosphorylation by casein kinase 2 regulates Nap1 localization and
function.";
Mol. Cell. Biol. 28:1313-1325(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-259 AND SER-414, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[34]
METHYLATION.
PubMed=20510667; DOI=10.1016/j.abb.2010.05.023;
Lipson R.S., Webb K.J., Clarke S.G.;
"Two novel methyltransferases acting upon eukaryotic elongation factor
1A in Saccharomyces cerevisiae.";
Arch. Biochem. Biophys. 500:137-143(2010).
[35]
FUNCTION, INTERACTION WITH GCN2, AND ASSOCIATION WITH RIBOSOMES.
PubMed=21849502; DOI=10.1074/jbc.M111.248898;
Visweswaraiah J., Lageix S., Castilho B.A., Izotova L., Kinzy T.G.,
Hinnebusch A.G., Sattlegger E.;
"Evidence that eukaryotic translation elongation factor 1A (eEF1A)
binds the Gcn2 protein C terminus and inhibits Gcn2 activity.";
J. Biol. Chem. 286:36568-36579(2011).
[36]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-224; LYS-242; LYS-253;
LYS-271; LYS-393 AND LYS-437, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[37]
METHYLATION AT LYS-30 BY EFM1, METHYLATION AT LYS-316 BY SEE1, AND
METHYLATION AT LYS-79 AND LYS-390.
PubMed=22522802; DOI=10.1002/pmic.201100570;
Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
"Methylation of translation-associated proteins in Saccharomyces
cerevisiae: Identification of methylated lysines and their
methyltransferases.";
Proteomics 12:960-972(2012).
[38]
METHYLATION AT LYS-79 BY EFM5.
PubMed=25446118; DOI=10.1016/j.bbrc.2014.11.022;
Dzialo M.C., Travaglini K.J., Shen S., Loo J.A., Clarke S.G.;
"A new type of protein lysine methyltransferase trimethylates Lys-79
of elongation factor 1A.";
Biochem. Biophys. Res. Commun. 455:382-389(2014).
[39]
METHYLATION AT LYS-30; LYS-79 AND LYS-390, AND METHYLATION AT LYS-316
BY SEE1.
PubMed=24517342; DOI=10.1021/pr401251k;
Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P.,
Wilkins M.R.;
"Stoichiometry of Saccharomyces cerevisiae lysine methylation:
insights into non-histone protein lysine methyltransferase activity.";
J. Proteome Res. 13:1744-1756(2014).
[40]
METHYLATION AT LYS-390 BY EFM6.
PubMed=26115316; DOI=10.1371/journal.pone.0131426;
Jakobsson M.E., Davydova E., Malecki J., Moen A., Falnes P.O.;
"Saccharomyces cerevisiae eukaryotic elongation factor 1A (eEF1A) is
methylated at Lys-390 by a METTL21-like methyltransferase.";
PLoS ONE 10:E0131426-E0131426(2015).
[41]
METHYLATION AT GLY-2 AND LYS-3 BY NNT1.
PubMed=26545399; DOI=10.1074/mcp.M115.052449;
Hamey J.J., Winter D.L., Yagoub D., Overall C.M., Hart-Smith G.,
Wilkins M.R.;
"Novel N-terminal and lysine methyltransferases that target
translation elongation factor 1A in yeast and human.";
Mol. Cell. Proteomics 15:164-176(2016).
[42]
X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH EFB1.
PubMed=11106763; DOI=10.1016/S1097-2765(00)00122-2;
Andersen G.R., Pedersen L., Valente L., Chatterjee I., Kinzy T.G.,
Kjeldgaard M., Nyborg J.;
"Structural basis for nucleotide exchange and competition with tRNA in
the yeast elongation factor complex eEF1A:eEF1Balpha.";
Mol. Cell 6:1261-1266(2000).
[43]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH EFB1.
PubMed=11373622; DOI=10.1038/88598;
Andersen G.R., Valente L., Pedersen L., Kinzy T.G., Nyborg J.;
"Crystal structures of nucleotide exchange intermediates in the eEF1A-
eEF1Balpha complex.";
Nat. Struct. Biol. 8:531-534(2001).
-!- FUNCTION: GTP-binding component of the eukaryotic elongation
factor 1 complex (eEF1). In its active GTP-bound form, binds to
and delivers aminoacyl-tRNA to the A-site of ribosomes during
protein biosynthesis. In the presence of a correct codon-anticodon
match between the aminoacyl-tRNA and the A-site codon of the
ribosome-bound mRNA, the ribosome acts as a GTPase activator and
the GTP is hydrolyzed. The inactive GDP-bound form leaves the
ribosome and must be recycled by its guanine nucleotide exchange
factor (GEF) (eEF1B subcomplex) before binding another molecule of
aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs.
May also be involved in translational quality control by targeting
cotranslationally damaged proteins to the proteasome. Also
exhibits actin filament-binding and -bundling activities and is
involved in cytoskeleton organization. Plays a role as a negative
regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-
2-alpha phosphorylation in amino acid-repleted cells
(PubMed:21849502). {ECO:0000269|PubMed:10766739,
ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:21849502,
ECO:0000269|PubMed:3066688}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.14 mM for GTP {ECO:0000269|PubMed:9786872};
-!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
-!- SUBUNIT: The eukaryotic elongation factor 1 complex (eEF1) is
probably a heterohexamer. Two trimeric complexes, each composed of
eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or
TEF4), are probably dimerized via the eF1Bgamma subunits. eEF1A
interacts directly with eEF1Balpha. Interacts with elongation
factor 3 (YEF3 or HEF3), BNI1, SRV2 and ZPR1. Binds to actin and
forms a ternary complex with BNI1 and profilin. Interacts with the
proteasome, probably via RPT1. Interacts with CEX1 and NAP1.
Interacts with GCN2 (via C-terminus); this interaction is direct,
occurs in amino acid-repleted cells, may be stabilzed in a
ribosome-dependent manner, reduces GCN2-mediated eIF-2-alpha
phosphorylation and is lost in amino acid-starved cells and by
uncharged tRNAs (PubMed:21849502). Associates with ribosomes
(PubMed:21849502). {ECO:0000269|PubMed:11106763,
ECO:0000269|PubMed:11290701, ECO:0000269|PubMed:11373622,
ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:17203074,
ECO:0000269|PubMed:18086883, ECO:0000269|PubMed:21849502,
ECO:0000269|PubMed:9125210, ECO:0000269|PubMed:9591785,
ECO:0000269|PubMed:9852145, ECO:0000269|PubMed:9990316}.
-!- INTERACTION:
P43573:BUD27; NbExp=2; IntAct=EBI-6314, EBI-22787;
P32471:EFB1; NbExp=2; IntAct=EBI-6314, EBI-6319;
Q05040:FAR8; NbExp=2; IntAct=EBI-6314, EBI-28053;
P17555:SRV2; NbExp=3; IntAct=EBI-6314, EBI-4024;
Q62384:Zpr1 (xeno); NbExp=2; IntAct=EBI-6314, EBI-11566629;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.
-!- PTM: S-thiolated in response to oxidative stress, probably
inhibiting the protein and causing a reduction in protein
synthesis.
-!- MISCELLANEOUS: Present with 827 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: There are two genes for eEF1A in yeast.
-!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X00779; CAA25356.1; -; Genomic_DNA.
EMBL; X01638; CAA25798.1; -; Genomic_DNA.
EMBL; M10992; AAA34585.1; -; Genomic_DNA.
EMBL; M15666; AAA34584.1; -; Genomic_DNA.
EMBL; M15667; AAA34586.1; -; Genomic_DNA.
EMBL; X78993; CAA55620.1; -; Genomic_DNA.
EMBL; Z35987; CAA85075.1; -; Genomic_DNA.
EMBL; U51033; AAB68129.1; -; Genomic_DNA.
EMBL; AY692927; AAT92946.1; -; Genomic_DNA.
EMBL; X73532; CAA51936.1; -; Genomic_DNA.
EMBL; AF402004; AAP86465.1; -; Genomic_DNA.
EMBL; AY130810; AAM83111.1; -; Genomic_DNA.
EMBL; AY130811; AAM83112.1; -; Genomic_DNA.
EMBL; AY130812; AAM83113.1; -; Genomic_DNA.
EMBL; AY130813; AAM83114.1; -; Genomic_DNA.
EMBL; BK006936; DAA07236.1; -; Genomic_DNA.
EMBL; BK006949; DAA11498.1; -; Genomic_DNA.
PIR; A03522; EFBY1A.
RefSeq; NP_009676.1; NM_001178466.1.
RefSeq; NP_015405.1; NM_001184177.1.
PDB; 1F60; X-ray; 1.67 A; A=1-458.
PDB; 1G7C; X-ray; 2.05 A; A=1-458.
PDB; 1IJE; X-ray; 2.40 A; A=1-458.
PDB; 1IJF; X-ray; 3.00 A; A=1-458.
PDB; 2B7B; X-ray; 2.60 A; A=1-458.
PDB; 2B7C; X-ray; 1.80 A; A=1-458.
PDB; 5O8W; X-ray; 1.67 A; A=1-458.
PDBsum; 1F60; -.
PDBsum; 1G7C; -.
PDBsum; 1IJE; -.
PDBsum; 1IJF; -.
PDBsum; 2B7B; -.
PDBsum; 2B7C; -.
PDBsum; 5O8W; -.
ProteinModelPortal; P02994; -.
SMR; P02994; -.
BioGrid; 32820; 324.
BioGrid; 36251; 212.
DIP; DIP-2250N; -.
IntAct; P02994; 805.
MINT; MINT-441761; -.
STRING; 4932.YPR080W; -.
iPTMnet; P02994; -.
MaxQB; P02994; -.
PRIDE; P02994; -.
TopDownProteomics; P02994; -.
EnsemblFungi; YBR118W; YBR118W; YBR118W.
EnsemblFungi; YPR080W; YPR080W; YPR080W.
GeneID; 852415; -.
GeneID; 856195; -.
KEGG; sce:YBR118W; -.
KEGG; sce:YPR080W; -.
SGD; S000006284; TEF1.
SGD; S000000322; TEF2.
GeneTree; ENSGT00670000097815; -.
GeneTree; ENSGT00900000141045; -.
HOGENOM; HOG000229291; -.
InParanoid; P02994; -.
KO; K03231; -.
OMA; WYKGWTK; -.
OrthoDB; EOG092C2HV8; -.
BioCyc; YEAST:G3O-29075-MONOMER; -.
BioCyc; YEAST:G3O-34224-MONOMER; -.
Reactome; R-SCE-156842; Eukaryotic Translation Elongation.
Reactome; R-SCE-3371511; HSF1 activation.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-8876725; Protein methylation.
UniPathway; UPA00345; -.
EvolutionaryTrace; P02994; -.
PRO; PR:P02994; -.
Proteomes; UP000002311; Chromosome II.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; ISS:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0005739; C:mitochondrion; IPI:SGD.
GO; GO:0005840; C:ribosome; TAS:SGD.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0019003; F:GDP binding; IDA:SGD.
GO; GO:0005525; F:GTP binding; IDA:SGD.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0003746; F:translation elongation factor activity; IMP:SGD.
GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0006414; P:translational elongation; IMP:SGD.
GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
HAMAP; MF_00118_A; EF_Tu_A; 1.
InterPro; IPR004161; EFTu-like_2.
InterPro; IPR031157; G_TR_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000795; TF_GTP-bd_dom.
InterPro; IPR009000; Transl_B-barrel.
InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
Pfam; PF00009; GTP_EFTU; 1.
Pfam; PF03144; GTP_EFTU_D2; 1.
Pfam; PF03143; GTP_EFTU_D3; 1.
PRINTS; PR00315; ELONGATNFCT.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF50465; SSF50465; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00483; EF-1_alpha; 1.
PROSITE; PS00301; G_TR_1; 1.
PROSITE; PS51722; G_TR_2; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Elongation factor;
GTP-binding; Isopeptide bond; Methylation; Nucleotide-binding;
Phosphoprotein; Protein biosynthesis; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:26545399}.
CHAIN 2 458 Elongation factor 1-alpha.
/FTId=PRO_0000090973.
DOMAIN 5 240 tr-type G.
NP_BIND 14 21 GTP.
NP_BIND 91 95 GTP.
NP_BIND 153 156 GTP.
REGION 14 21 G1. {ECO:0000250}.
REGION 70 74 G2. {ECO:0000250}.
REGION 91 94 G3. {ECO:0000250}.
REGION 153 156 G4. {ECO:0000250}.
REGION 192 194 G5. {ECO:0000250}.
SITE 298 298 Not modified.
SITE 372 372 Not modified.
MOD_RES 2 2 N,N,N-trimethylglycine; by EFM7.
{ECO:0000269|PubMed:26545399}.
MOD_RES 3 3 N6,N6-dimethyllysine; by EFM7; alternate.
{ECO:0000269|PubMed:26545399}.
MOD_RES 3 3 N6-methyllysine; by EFM7; alternate.
{ECO:0000269|PubMed:26545399}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 30 30 N6-methyllysine; by EFM1.
{ECO:0000269|PubMed:22522802,
ECO:0000269|PubMed:24517342,
ECO:0000269|PubMed:8476932}.
MOD_RES 72 72 Phosphothreonine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 79 79 N6,N6,N6-trimethyllysine; by EFM5.
{ECO:0000269|PubMed:22522802,
ECO:0000269|PubMed:24517342,
ECO:0000269|PubMed:25446118,
ECO:0000269|PubMed:8476932}.
MOD_RES 82 82 Phosphothreonine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 259 259 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 316 316 N6,N6-dimethyllysine; by EFM4; alternate.
{ECO:0000269|PubMed:22522802,
ECO:0000269|PubMed:24517342,
ECO:0000269|PubMed:8476932}.
MOD_RES 316 316 N6-methyllysine; by EFM4; alternate.
{ECO:0000269|PubMed:24517342}.
MOD_RES 390 390 N6-methyllysine; by EFM6.
{ECO:0000269|PubMed:22522802,
ECO:0000269|PubMed:24517342,
ECO:0000269|PubMed:26115316,
ECO:0000269|PubMed:8476932}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 430 430 Phosphothreonine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 458 458 Lysine methyl ester.
{ECO:0000269|PubMed:10973948}.
CROSSLNK 224 224 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 242 242 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 253 253 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 271 271 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 393 393 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 437 437 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 122 122 E->K: Reduces interaction with YEF3.
{ECO:0000269|PubMed:9990316}.
MUTAGEN 153 153 N->D: Increases KM for GTP to 2.7 mM.
{ECO:0000269|PubMed:10514524,
ECO:0000269|PubMed:9786872}.
MUTAGEN 153 153 N->T: Increases KM for GTP to 6.0 mM and
reduces translation fidelity. Increases
Km for GTP to 10.3 mM and reduces
translation fidelity; when associated
with E-156. {ECO:0000269|PubMed:10514524,
ECO:0000269|PubMed:9786872}.
MUTAGEN 156 156 D->E: Increases KM for GTP to 10.3 mM and
reduces translation fidelity; when
associated with T-152.
{ECO:0000269|PubMed:10514524,
ECO:0000269|PubMed:15601860,
ECO:0000269|PubMed:9786872}.
MUTAGEN 156 156 D->N: Increases KM for GTP to 13.1 mM and
reduces translation fidelity. Confers
hyperresistance to canavanine.
{ECO:0000269|PubMed:10514524,
ECO:0000269|PubMed:15601860,
ECO:0000269|PubMed:9786872}.
MUTAGEN 156 156 D->W: Increases KM for GTP to 4.2 mM.
Preferres XTP over GTP as substrate.
{ECO:0000269|PubMed:10514524,
ECO:0000269|PubMed:15601860,
ECO:0000269|PubMed:9786872}.
MUTAGEN 286 286 E->K: In TEF2-1; strongly reduces
translation fidelity by increasing the
frequency of frameshifting and amino acid
misincorporation.
{ECO:0000269|PubMed:3066688}.
MUTAGEN 317 317 E->K: In TEF2-2; strongly reduces
translation fidelity by increasing the
frequency of frameshifting and amino acid
misincorporation.
{ECO:0000269|PubMed:3066688}.
CONFLICT 86 86 Q -> E (in Ref. 14; AA sequence).
{ECO:0000305}.
STRAND 6 14 {ECO:0000244|PDB:1F60}.
HELIX 20 31 {ECO:0000244|PDB:1F60}.
HELIX 36 45 {ECO:0000244|PDB:1F60}.
HELIX 46 49 {ECO:0000244|PDB:1F60}.
STRAND 50 52 {ECO:0000244|PDB:1F60}.
HELIX 56 68 {ECO:0000244|PDB:1F60}.
STRAND 78 81 {ECO:0000244|PDB:1F60}.
STRAND 83 91 {ECO:0000244|PDB:1F60}.
HELIX 98 104 {ECO:0000244|PDB:1F60}.
STRAND 105 107 {ECO:0000244|PDB:1F60}.
STRAND 110 117 {ECO:0000244|PDB:1F60}.
HELIX 120 126 {ECO:0000244|PDB:1F60}.
HELIX 132 142 {ECO:0000244|PDB:1F60}.
STRAND 147 153 {ECO:0000244|PDB:1F60}.
HELIX 155 158 {ECO:0000244|PDB:1F60}.
HELIX 162 179 {ECO:0000244|PDB:1F60}.
HELIX 183 185 {ECO:0000244|PDB:1F60}.
STRAND 188 190 {ECO:0000244|PDB:1F60}.
TURN 193 195 {ECO:0000244|PDB:1F60}.
TURN 197 199 {ECO:0000244|PDB:1F60}.
STRAND 212 215 {ECO:0000244|PDB:1F60}.
STRAND 217 225 {ECO:0000244|PDB:1F60}.
HELIX 226 231 {ECO:0000244|PDB:1F60}.
STRAND 239 242 {ECO:0000244|PDB:2B7C}.
STRAND 245 254 {ECO:0000244|PDB:1F60}.
TURN 255 257 {ECO:0000244|PDB:1F60}.
STRAND 258 264 {ECO:0000244|PDB:1F60}.
STRAND 275 279 {ECO:0000244|PDB:1F60}.
TURN 280 282 {ECO:0000244|PDB:1F60}.
STRAND 283 292 {ECO:0000244|PDB:1F60}.
STRAND 295 298 {ECO:0000244|PDB:2B7C}.
STRAND 305 312 {ECO:0000244|PDB:1F60}.
TURN 315 317 {ECO:0000244|PDB:1F60}.
STRAND 323 326 {ECO:0000244|PDB:1F60}.
STRAND 336 344 {ECO:0000244|PDB:1F60}.
STRAND 358 361 {ECO:0000244|PDB:1F60}.
STRAND 364 377 {ECO:0000244|PDB:1F60}.
TURN 379 381 {ECO:0000244|PDB:1F60}.
STRAND 384 388 {ECO:0000244|PDB:1F60}.
STRAND 397 406 {ECO:0000244|PDB:1F60}.
TURN 413 415 {ECO:0000244|PDB:1F60}.
HELIX 417 419 {ECO:0000244|PDB:1F60}.
STRAND 420 426 {ECO:0000244|PDB:1F60}.
STRAND 429 440 {ECO:0000244|PDB:1F60}.
SEQUENCE 458 AA; 50033 MW; 411C66D830716576 CRC64;
MGKEKSHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPKYQVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGV
GEFEAGISKD GQTREHALLA FTLGVRQLIV AVNKMDSVKW DESRFQEIVK ETSNFIKKVG
YNPKTVPFVP ISGWNGDNMI EATTNAPWYK GWEKETKAGV VKGKTLLEAI DAIEQPSRPT
DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KPGMVVTFAP AGVTTEVKSV EMHHEQLEQG
VPGDNVGFNV KNVSVKEIRR GNVCGDAKND PPKGCASFNA TVIVLNHPGQ ISAGYSPVLD
CHTAHIACRF DELLEKNDRR SGKKLEDHPK FLKSGDAALV KFVPSKPMCV EAFSEYPPLG
RFAVRDMRQT VAVGVIKSVD KTEKAAKVTK AAQKAAKK


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