P02994 (EF1A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor 1-alpha
Short name=EF-1-alpha

Alternative name(s):
Eukaryotic elongation factor 1A
Short name=eEF1A
Translation elongation factor 1A

Gene names

Name:	TEF1
Ordered Locus Names:	YPR080W
ORF Names:	P9513.7
AND
Name:	TEF2
Ordered Locus Names:	YBR118W
ORF Names:	YBR0913

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.17 Ref.22 Ref.28
Pathway	Protein biosynthesis; polypeptide chain elongation.
Subunit structure	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. Ref.12 Ref.15 Ref.18 Ref.20 Ref.24 Ref.28 Ref.30 Ref.32
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton Ref.26.
Post-translational modification	S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis. Monomethylated at Lys-30 and Lys-390. EFM1 is required for such methylation but it is unclear whether it mediates monomethylation at Lys-30 and/or Lys-390. Ref.11 Ref.23 Ref.34
Miscellaneous	Present with 827 molecules/cell in log phase SD medium. Ref.27 There are two genes for eEF1A in yeast.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.14 mM for GTP Ref.19

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	tRNA export from nucleus Inferred from mutant phenotype Ref.22Ref.30. Source: SGD
Cellular component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell ribosome Traceable author statement. Source: SGD
Molecular function	GDP binding Inferred from direct assay. Source: SGD GTP binding Inferred from direct assay. Source: SGD GTPase activity Inferred from electronic annotation. Source: InterPro actin binding Inferred from electronic annotation. Source: UniProtKB-KW translation elongation factor activity Inferred from mutant phenotype Ref.21. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUD27	P43573	2	EBI-6314,EBI-22787
FAR8	Q05040	2	EBI-6314,EBI-28053
SRV2	P17555	3	EBI-6314,EBI-4024

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 458

458

Elongation factor 1-alpha

PRO_0000090973

Regions

Nucleotide binding

14 – 21

8

GTP

Nucleotide binding

91 – 95

5

GTP

Nucleotide binding

153 – 156

4

GTP

Sites

Site

298

1

Not modified

Site

372

1

Not modified

Amino acid modifications

Modified residue

1

1

Blocked amino end (Met)

Modified residue

6

1

Phosphoserine Ref.31

Modified residue

18

1

Phosphoserine Ref.31

Modified residue

30

1

N6-methyllysine; by EFM1 Probable

Modified residue

53

1

Phosphoserine Ref.33

Modified residue

72

1

Phosphothreonine Ref.31

Modified residue

79

1

N6,N6,N6-trimethyllysine Ref.11

Modified residue

163

1

Phosphoserine Ref.31

Modified residue

259

1

Phosphothreonine Ref.33

Modified residue

316

1

N6,N6-dimethyllysine; by SEE1 Probable

Modified residue

355

1

Phosphotyrosine Ref.33

Modified residue

356

1

Phosphoserine Ref.33

Modified residue

390

1

N6-methyllysine; by EFM1 Probable

Modified residue

394

1

Phosphoserine Ref.29 Ref.33

Modified residue

414

1

Phosphoserine Ref.31 Ref.33

Modified residue

430

1

Phosphothreonine Ref.31

Modified residue

458

1

Lysine methyl ester Ref.23

Experimental info

Mutagenesis

122

1

E → K: Reduces interaction with YEF3. Ref.18

Mutagenesis

153

1

N → D: Increases KM for GTP to 2.7 mM. Ref.19 Ref.21

Mutagenesis

153

1

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. Ref.19 Ref.21

Mutagenesis

156

1

D → E: Increases KM for GTP to 10.3 mM and reduces translation fidelity; when associated with T-152. Ref.19 Ref.21 Ref.28

Mutagenesis

156

1

D → N: Increases KM for GTP to 13.1 mM and reduces translation fidelity. Confers hyperresistance to canavanine. Ref.19 Ref.21 Ref.28

Mutagenesis

156

1

D → W: Increases KM for GTP to 4.2 mM. Preferres XTP over GTP as substrate. Ref.19 Ref.21 Ref.28

Mutagenesis

286

1

E → K in TEF2-1; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. Ref.17

Mutagenesis

317

1

E → K in TEF2-2; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. Ref.17

Sequence conflict

86

1

Q → E AA sequence Ref.14

Secondary structure

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458

Helix Strand Turn

Details...

Beta strand

6 – 14

9

Helix

20 – 31

12

Helix

36 – 45

10

Helix

46 – 49

4

Beta strand

50 – 52

3

Helix

56 – 68

13

Beta strand

78 – 81

4

Beta strand

83 – 91

9

Helix

98 – 104

7

Beta strand

105 – 107

3

Beta strand

110 – 117

8

Helix

120 – 126

7

Helix

132 – 142

11

Beta strand

147 – 153

7

Helix

155 – 158

4

Helix

162 – 179

18

Helix

183 – 185

3

Beta strand

188 – 190

3

Turn

193 – 195

3

Turn

197 – 199

3

Beta strand

212 – 215

4

Beta strand

217 – 225

9

Helix

226 – 231

6

Beta strand

245 – 254

10

Turn

255 – 257

3

Beta strand

258 – 264

7

Beta strand

275 – 279

5

Turn

280 – 282

3

Beta strand

283 – 292

10

Beta strand

305 – 312

8

Turn

315 – 317

3

Beta strand

323 – 326

4

Beta strand

336 – 344

9

Beta strand

358 – 361

4

Beta strand

364 – 377

14

Turn

379 – 381

3

Beta strand

384 – 388

5

Beta strand

397 – 406

10

Turn

413 – 415

3

Helix

417 – 419

3

Beta strand

420 – 426

7

Beta strand

429 – 440

12

Sequences

	Sequence		Length	Mass (Da)
	P02994 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 411C66D830716576	FASTA	458	50,033
	10 20 30 40 50 60 MGKEKSHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL 70 80 90 100 110 120 DKLKAERERG ITIDIALWKF ETPKYQVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGV 130 140 150 160 170 180 GEFEAGISKD GQTREHALLA FTLGVRQLIV AVNKMDSVKW DESRFQEIVK ETSNFIKKVG 190 200 210 220 230 240 YNPKTVPFVP ISGWNGDNMI EATTNAPWYK GWEKETKAGV VKGKTLLEAI DAIEQPSRPT 250 260 270 280 290 300 DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KPGMVVTFAP AGVTTEVKSV EMHHEQLEQG 310 320 330 340 350 360 VPGDNVGFNV KNVSVKEIRR GNVCGDAKND PPKGCASFNA TVIVLNHPGQ ISAGYSPVLD 370 380 390 400 410 420 CHTAHIACRF DELLEKNDRR SGKKLEDHPK FLKSGDAALV KFVPSKPMCV EAFSEYPPLG 430 440 450 RFAVRDMRQT VAVGVIKSVD KTEKAAKVTK AAQKAAKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Nagata S., Nagashima K., Tsunetsugu-Yokota Y., Fujimura K., Miyazaki M., Kaziro Y. EMBO J. 3:1825-1830(1984) [PubMed: 6383821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).
[2]	"Identification of two genes coding for the translation elongation factor EF-1 alpha of S. cerevisiae." Schirmaier F., Philippsen P. EMBO J. 3:3311-3315(1984) [PubMed: 6396088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF2).
[3]	"Cloning, nucleotide sequence, and expression of one of two genes coding for yeast elongation factor 1 alpha." Cottrelle P., Thiele D., Price V.L., Memet S., Micouin J.-Y., Marck C., Buhler J.-M., Sentenac A., Fromageot P. J. Biol. Chem. 260:3090-3096(1985) [PubMed: 2982849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1).
[4]	"Structure of the two genes coding for polypeptide chain elongation factor 1 alpha (EF-1 alpha) from Saccharomyces cerevisiae." Nagashima K., Kasai M., Nagata S., Kaziro Y. Gene 45:265-273(1986) [PubMed: 3026912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1 AND TEF2).
[5]	"Analysis of a 70 kb region on the right arm of yeast chromosome II." Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H. Yeast 10:1363-1381(1994) [PubMed: 7900426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF2). Strain: ATCC 204508 / S288c.
[6]	"Complete DNA sequence of yeast chromosome II." 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. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF2). Strain: ATCC 204508 / S288c.
[7]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." 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. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF1). Strain: ATCC 204511 / S288c / AB972.
[8]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION (TEF1 AND TEF2). Strain: ATCC 204508 / S288c.
[9]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEF1). Strain: ATCC 204508 / S288c.
[10]	"TKL2, a second transketolase gene of Saccharomyces cerevisiae. Cloning, sequence and deletion analysis of the gene." Schaaff-Gerstenschlaeger I., Mannhaupt G., Vetter I., Zimmermann F.K., Feldmann H. Eur. J. Biochem. 217:487-492(1993) [PubMed: 7916691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-237 (TEF1). Strain: ATCC 204508 / S288c.
[11]	"Characterization of yeast EF-1 alpha: non-conservation of post-translational modifications." Cavallius J., Zoll W., Chakraburtty K., Merrick W.C. Biochim. Biophys. Acta 1163:75-80(1993) [PubMed: 8476932] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, METHYLATION AT LYS-30; LYS-79; LYS-316 AND LYS-390.
[12]	"Association of elongation factor 1 alpha and ribosomal protein L3 with the proline-rich region of yeast adenylyl cyclase-associated protein CAP." Yanagihara C., Shinkai M., Kariya K., Yamawaki-Kataoka Y., Hu C.-D., Masuda T., Kataoka T. Biochem. Biophys. Res. Commun. 232:503-507(1997) [PubMed: 9125210] [Abstract] Cited for: PROTEIN SEQUENCE OF 6-20, INTERACTION WITH SRV2.
[13]	"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." Norbeck J., Blomberg A. Yeast 13:1519-1534(1997) [PubMed: 9509572] [Abstract] Cited for: PROTEIN SEQUENCE OF 56-61 AND 265-280. Strain: ATCC 44827 / SKQ2N.
[14]	"Elongation factor 1 alpha from Saccharomyces cerevisiae. Rapid large-scale purification and molecular characterization." Thiele D., Cottrelle P., Iborra F., Buhler J.-M., Sentenac A., Fromageot P. J. Biol. Chem. 260:3084-3089(1985) [PubMed: 3882705] [Abstract] Cited for: PROTEIN SEQUENCE OF 70-77 AND 80-87.
[15]	"Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae." Umikawa M., Tanaka K., Kamei T., Shimizu K., Imamura H., Sasaki T., Takai Y. Oncogene 16:2011-2016(1998) [PubMed: 9591785] [Abstract] Cited for: PROTEIN SEQUENCE OF 211-214 AND 289-308, INTERACTION WITH BNI1, IDENTIFICATION IN A COMPLEX WITH BNI1 AND PROFILIN.
[16]	"Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses." Kurtzman C.P., Robnett C.J. FEMS Yeast Res. 3:417-432(2003) [PubMed: 12748053] [Abstract] Cited for: 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.
[17]	"Mutations in elongation factor EF-1 alpha affect the frequency of frameshifting and amino acid misincorporation in Saccharomyces cerevisiae." Sandbaken M.G., Culbertson M.R. Genetics 120:923-934(1988) [PubMed: 3066688] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-286 AND GLU-317.
[18]	"Competition and cooperation amongst yeast elongation factors." Kovalchuke O., Kambampati R., Pladies E., Chakraburtty K. Eur. J. Biochem. 258:986-993(1998) [PubMed: 9990316] [Abstract] Cited for: INTERACTION WITH YEF3, MUTAGENESIS OF GLU-122.
[19]	"Site-directed mutagenesis of yeast eEF1A. Viable mutants with altered nucleotide specificity." Cavallius J., Merrick W.C. J. Biol. Chem. 273:28752-28758(1998) [PubMed: 9786872] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-153 AND ASP-156.
[20]	"Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells." Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J. J. Cell Biol. 143:1471-1484(1998) [PubMed: 9852145] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ZPR1.
[21]	"Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange." Carr-Schmid A., Durko N., Cavallius J., Merrick W.C., Kinzy T.G. J. Biol. Chem. 274:30297-30302(1999) [PubMed: 10514524] [Abstract] Cited for: MUTAGENESIS OF ASN-153 AND ASP-156.
[22]	"An aminoacylation-dependent nuclear tRNA export pathway in yeast." Grosshans H., Hurt E.C., Simos G. Genes Dev. 14:830-840(2000) [PubMed: 10766739] [Abstract] Cited for: FUNCTION IN NUCLEAR EXPORT OF AMINOACYL-TRNAS.
[23]	"A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C-terminus." Zobel-Thropp P., Yang M.C., Machado L., Clarke S. J. Biol. Chem. 275:37150-37158(2000) [PubMed: 10973948] [Abstract] Cited for: METHYLATION AT LYS-458.
[24]	"Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast." Munshi R., Kandl K.A., Carr-Schmid A., Whitacre J.L., Adams A.E.M., Kinzy T.G. Genetics 157:1425-1436(2001) [PubMed: 11290701] [Abstract] Cited for: INTERACTION WITH ACTIN.
[25]	"Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae." Shenton D., Grant C.M. Biochem. J. 374:513-519(2003) [PubMed: 12755685] [Abstract] Cited for: S-THIOLATION.
[26]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[27]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[28]	"Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A." Chuang S.-M., Chen L., Lambertson D., Anand M., Kinzy T.G., Madura K. Mol. Cell. Biol. 25:403-413(2005) [PubMed: 15601860] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-156, INTERACTION WITH RPT1.
[29]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY. Strain: YAL6B.
[30]	"Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery." McGuire A.T., Mangroo D. EMBO J. 26:288-300(2007) [PubMed: 17203074] [Abstract] Cited for: INTERACTION WITH CEX1.
[31]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." 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. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-18; THR-72; SER-163; SER-414 AND THR-430, MASS SPECTROMETRY.
[32]	"Phosphorylation by casein kinase 2 regulates Nap1 localization and function." Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F. Mol. Cell. Biol. 28:1313-1325(2008) [PubMed: 18086883] [Abstract] Cited for: INTERACTION WITH NAP1, MASS SPECTROMETRY.
[33]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; THR-259; TYR-355; SER-356; SER-394 AND SER-414, MASS SPECTROMETRY.
[34]	"Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae." Lipson R.S., Webb K.J., Clarke S.G. Arch. Biochem. Biophys. 500:137-143(2010) [PubMed: 20510667] [Abstract] Cited for: METHYLATION AT LYS-30; LYS-316 AND LYS-390.
[35]	"Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha." Andersen G.R., Pedersen L., Valente L., Chatterjee I., Kinzy T.G., Kjeldgaard M., Nyborg J. Mol. Cell 6:1261-1266(2000) [PubMed: 11106763] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH EFB1.
[36]	"Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex." Andersen G.R., Valente L., Pedersen L., Kinzy T.G., Nyborg J. Nat. Struct. Biol. 8:531-534(2001) [PubMed: 11373622] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH EFB1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00779 Genomic DNA. Translation: CAA25356.1.
X01638 Genomic DNA. Translation: CAA25798.1.
M10992 Genomic DNA. Translation: AAA34585.1.
M15666 Genomic DNA. Translation: AAA34584.1.
M15667 Genomic DNA. Translation: AAA34586.1.
X78993 Genomic DNA. Translation: CAA55620.1.
Z35987 Genomic DNA. Translation: CAA85075.1.
U51033 Genomic DNA. Translation: AAB68129.1.
AY692927 Genomic DNA. Translation: AAT92946.1.
X73532 Genomic DNA. Translation: CAA51936.1.
AF402004 Genomic DNA. Translation: AAP86465.1.
AY130810 Genomic DNA. Translation: AAM83111.1.
AY130811 Genomic DNA. Translation: AAM83112.1.
AY130812 Genomic DNA. Translation: AAM83113.1.
AY130813 Genomic DNA. Translation: AAM83114.1.
BK006936 Genomic DNA. Translation: DAA07236.1.
BK006949 Genomic DNA. Translation: DAA11498.1.

PIR

EFBY1A. A03522.

RefSeq

NP_009676.1. NM_001178466.1.
NP_015405.1. NM_001184177.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F60	X-ray	1.67	A	1-458	[»]
1G7C	X-ray	2.05	A	1-458	[»]
1IJE	X-ray	2.40	A	1-458	[»]
1IJF	X-ray	3.00	A	1-458	[»]
2B7B	X-ray	2.60	A	1-458	[»]
2B7C	X-ray	1.80	A	1-458	[»]

ProteinModelPortal

P02994.

SMR

P02994. Positions 2-441.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2250N.

IntAct

P02994. 713 interactions.

MINT

MINT-441761.

STRING

P02994.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBR118W; YBR118W; YBR118W.
YPR080W; YPR080W; YPR080W.

GeneID

852415.
856195.

KEGG

sce:YBR118W.
sce:YPR080W.

Organism-specific databases

CYGD

YBR118w.
YPR080w.

SGD

S000006284. TEF1.
S000000322. TEF2.

Phylogenomic databases

eggNOG

fuNOG07405.

GeneTree

EFGT00050000001540.

HOGENOM

HBG307581.

OMA

FLKAGDA.

OrthoDB

EOG4BS0V0.

Gene expression databases

Genevestigator

P02994.

GermOnline

YBR118W. Saccharomyces cerevisiae.
YPR080W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000795. ProtSyn_GTP-bd.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

KO

K03231.

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

SUPFAM

SSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.

TIGRFAMs

TIGR00483. EF-1_alpha. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

971270.

Entry information

Entry name

EF1A_YEAST

Accession

Primary (citable) accession number: P02994
Secondary accession number(s): D6VQB6 , Q7Z7U8, Q7Z8Q8, Q7Z8Q9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	December 14, 2011
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program