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Protein

Elongation factor 1-alpha

Gene

TEF1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).4 Publications

Kineticsi

  1. KM=0.14 mM for GTP1 Publication

    Pathwayi: polypeptide chain elongation

    This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein biosynthesis.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 218GTP
    Nucleotide bindingi91 – 955GTP
    Nucleotide bindingi153 – 1564GTP

    GO - Molecular functioni

    • GDP binding Source: SGD
    • GTPase activity Source: InterPro
    • GTP binding Source: SGD
    • protein kinase binding Source: UniProtKB
    • ribosome binding Source: UniProtKB
    • translation elongation factor activity Source: SGD

    GO - Biological processi

    • cellular response to amino acid starvation Source: UniProtKB
    • negative regulation of protein kinase activity Source: UniProtKB
    • negative regulation of protein phosphorylation Source: UniProtKB
    • translational elongation Source: SGD
    • tRNA export from nucleus Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    Actin-binding, GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29075-MONOMER.
    YEAST:G3O-34224-MONOMER.
    ReactomeiR-SCE-156842. Eukaryotic Translation Elongation.
    R-SCE-3371511. HSF1 activation.
    UniPathwayiUPA00345.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:TEF1
    Ordered Locus Names:YPR080W
    ORF Names:P9513.7
    AND
    Name:TEF2
    Ordered Locus Names:YBR118W
    ORF Names:YBR0913
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componentsi: Chromosome II, Chromosome XVI

    Organism-specific databases

    SGDiS000006284. TEF1.
    S000000322. TEF2.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: SGD
    • cytoskeleton Source: UniProtKB-SubCell
    • eukaryotic translation elongation factor 1 complex Source: SGD
    • fungal-type vacuole membrane Source: SGD
    • mitochondrion Source: SGD
    • ribosome Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi122 – 1221E → K: Reduces interaction with YEF3. 1 Publication
    Mutagenesisi153 – 1531N → D: Increases KM for GTP to 2.7 mM. 2 Publications
    Mutagenesisi153 – 1531N → 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. 2 Publications
    Mutagenesisi156 – 1561D → E: Increases KM for GTP to 10.3 mM and reduces translation fidelity; when associated with T-152. 3 Publications
    Mutagenesisi156 – 1561D → N: Increases KM for GTP to 13.1 mM and reduces translation fidelity. Confers hyperresistance to canavanine. 3 Publications
    Mutagenesisi156 – 1561D → W: Increases KM for GTP to 4.2 mM. Preferres XTP over GTP as substrate. 3 Publications
    Mutagenesisi286 – 2861E → K in TEF2-1; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. 1 Publication
    Mutagenesisi317 – 3171E → K in TEF2-2; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Elongation factor 1-alphaPRO_0000090973Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11Blocked amino end (Met)
    Modified residuei18 – 181PhosphoserineCombined sources
    Modified residuei30 – 301N6-methyllysine; by EFM13 Publications
    Modified residuei72 – 721PhosphothreonineCombined sources
    Modified residuei79 – 791N6,N6,N6-trimethyllysine; by EFM54 Publications
    Modified residuei82 – 821PhosphothreonineCombined sources
    Modified residuei163 – 1631PhosphoserineCombined sources
    Modified residuei259 – 2591PhosphothreonineCombined sources
    Modified residuei289 – 2891PhosphoserineCombined sources
    Modified residuei316 – 3161N6,N6-dimethyllysine; by EFM4; alternate3 Publications
    Modified residuei316 – 3161N6-methyllysine; by EFM4; alternate1 Publication
    Modified residuei390 – 3901N6-methyllysine; by EFM64 Publications
    Modified residuei414 – 4141PhosphoserineCombined sources
    Modified residuei430 – 4301PhosphothreonineCombined sources
    Modified residuei458 – 4581Lysine methyl ester1 Publication

    Post-translational modificationi

    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-390.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei298 – 2981Not modified
    Sitei372 – 3721Not modified

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP02994.
    PRIDEiP02994.
    TopDownProteomicsiP02994.

    PTM databases

    iPTMnetiP02994.

    Interactioni

    Subunit structurei

    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).11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BUD27P435732EBI-6314,EBI-22787
    FAR8Q050402EBI-6314,EBI-28053
    SRV2P175553EBI-6314,EBI-4024

    GO - Molecular functioni

    • protein kinase binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi32820. 183 interactions.
    36251. 164 interactions.
    DIPiDIP-2250N.
    IntActiP02994. 723 interactions.
    MINTiMINT-441761.

    Structurei

    Secondary structure

    1
    458
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 149Combined sources
    Helixi20 – 3112Combined sources
    Helixi36 – 4510Combined sources
    Helixi46 – 494Combined sources
    Beta strandi50 – 523Combined sources
    Helixi56 – 6813Combined sources
    Beta strandi78 – 814Combined sources
    Beta strandi83 – 919Combined sources
    Helixi98 – 1047Combined sources
    Beta strandi105 – 1073Combined sources
    Beta strandi110 – 1178Combined sources
    Helixi120 – 1267Combined sources
    Helixi132 – 14211Combined sources
    Beta strandi147 – 1537Combined sources
    Helixi155 – 1584Combined sources
    Helixi162 – 17918Combined sources
    Helixi183 – 1853Combined sources
    Beta strandi188 – 1903Combined sources
    Turni193 – 1953Combined sources
    Turni197 – 1993Combined sources
    Beta strandi212 – 2154Combined sources
    Beta strandi217 – 2259Combined sources
    Helixi226 – 2316Combined sources
    Beta strandi239 – 2424Combined sources
    Beta strandi245 – 25410Combined sources
    Turni255 – 2573Combined sources
    Beta strandi258 – 2647Combined sources
    Beta strandi275 – 2795Combined sources
    Turni280 – 2823Combined sources
    Beta strandi283 – 29210Combined sources
    Beta strandi295 – 2984Combined sources
    Beta strandi305 – 3128Combined sources
    Turni315 – 3173Combined sources
    Beta strandi323 – 3264Combined sources
    Beta strandi336 – 3449Combined sources
    Beta strandi358 – 3614Combined sources
    Beta strandi364 – 37714Combined sources
    Turni379 – 3813Combined sources
    Beta strandi384 – 3885Combined sources
    Beta strandi397 – 40610Combined sources
    Turni413 – 4153Combined sources
    Helixi417 – 4193Combined sources
    Beta strandi420 – 4267Combined sources
    Beta strandi429 – 44012Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F60X-ray1.67A1-458[»]
    1G7CX-ray2.05A1-458[»]
    1IJEX-ray2.40A1-458[»]
    1IJFX-ray3.00A1-458[»]
    2B7BX-ray2.60A1-458[»]
    2B7CX-ray1.80A1-458[»]
    ProteinModelPortaliP02994.
    SMRiP02994. Positions 2-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02994.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 240236tr-type GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 218G1By similarity
    Regioni70 – 745G2By similarity
    Regioni91 – 944G3By similarity
    Regioni153 – 1564G4By similarity
    Regioni192 – 1943G5By similarity

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00670000097815.
    ENSGT00840000130086.
    HOGENOMiHOG000229291.
    InParanoidiP02994.
    KOiK03231.
    OMAiPASTIFH.
    OrthoDBiEOG715QCW.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00118_A. EF_Tu_A.
    InterProiIPR031157. G_TR_CS.
    IPR027417. P-loop_NTPase.
    IPR000795. TF_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    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.
    [Graphical view]
    PfamiPF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF50465. SSF50465. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P02994-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGKEKSHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG
    60 70 80 90 100
    KGSFKYAWVL DKLKAERERG ITIDIALWKF ETPKYQVTVI DAPGHRDFIK
    110 120 130 140 150
    NMITGTSQAD CAILIIAGGV GEFEAGISKD GQTREHALLA FTLGVRQLIV
    160 170 180 190 200
    AVNKMDSVKW DESRFQEIVK ETSNFIKKVG YNPKTVPFVP ISGWNGDNMI
    210 220 230 240 250
    EATTNAPWYK GWEKETKAGV VKGKTLLEAI DAIEQPSRPT DKPLRLPLQD
    260 270 280 290 300
    VYKIGGIGTV PVGRVETGVI KPGMVVTFAP AGVTTEVKSV EMHHEQLEQG
    310 320 330 340 350
    VPGDNVGFNV KNVSVKEIRR GNVCGDAKND PPKGCASFNA TVIVLNHPGQ
    360 370 380 390 400
    ISAGYSPVLD CHTAHIACRF DELLEKNDRR SGKKLEDHPK FLKSGDAALV
    410 420 430 440 450
    KFVPSKPMCV EAFSEYPPLG RFAVRDMRQT VAVGVIKSVD KTEKAAKVTK

    AAQKAAKK
    Length:458
    Mass (Da):50,033
    Last modified:July 21, 1986 - v1
    Checksum:i411C66D830716576
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861Q → E AA sequence (PubMed:3882705).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    PIRiA03522. EFBY1A.
    RefSeqiNP_009676.1. NM_001178466.1.
    NP_015405.1. NM_001184177.1.

    Genome annotation databases

    EnsemblFungiiYBR118W; YBR118W; YBR118W.
    YPR080W; YPR080W; YPR080W.
    GeneIDi852415.
    856195.
    KEGGisce:YBR118W.
    sce:YPR080W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    PIRiA03522. EFBY1A.
    RefSeqiNP_009676.1. NM_001178466.1.
    NP_015405.1. NM_001184177.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F60X-ray1.67A1-458[»]
    1G7CX-ray2.05A1-458[»]
    1IJEX-ray2.40A1-458[»]
    1IJFX-ray3.00A1-458[»]
    2B7BX-ray2.60A1-458[»]
    2B7CX-ray1.80A1-458[»]
    ProteinModelPortaliP02994.
    SMRiP02994. Positions 2-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32820. 183 interactions.
    36251. 164 interactions.
    DIPiDIP-2250N.
    IntActiP02994. 723 interactions.
    MINTiMINT-441761.

    PTM databases

    iPTMnetiP02994.

    Proteomic databases

    MaxQBiP02994.
    PRIDEiP02994.
    TopDownProteomicsiP02994.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYBR118W; YBR118W; YBR118W.
    YPR080W; YPR080W; YPR080W.
    GeneIDi852415.
    856195.
    KEGGisce:YBR118W.
    sce:YPR080W.

    Organism-specific databases

    SGDiS000006284. TEF1.
    S000000322. TEF2.

    Phylogenomic databases

    GeneTreeiENSGT00670000097815.
    ENSGT00840000130086.
    HOGENOMiHOG000229291.
    InParanoidiP02994.
    KOiK03231.
    OMAiPASTIFH.
    OrthoDBiEOG715QCW.

    Enzyme and pathway databases

    UniPathwayiUPA00345.
    BioCyciYEAST:G3O-29075-MONOMER.
    YEAST:G3O-34224-MONOMER.
    ReactomeiR-SCE-156842. Eukaryotic Translation Elongation.
    R-SCE-3371511. HSF1 activation.

    Miscellaneous databases

    EvolutionaryTraceiP02994.
    PROiP02994.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00118_A. EF_Tu_A.
    InterProiIPR031157. G_TR_CS.
    IPR027417. P-loop_NTPase.
    IPR000795. TF_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    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.
    [Graphical view]
    PfamiPF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF50465. SSF50465. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF1).
      Strain: ATCC 204508 / S288c.
    8. Cited for: GENOME REANNOTATION (TEF1 AND TEF2).
      Strain: ATCC 204508 / S288c.
    9. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: S-THIOLATION.
    26. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    27. 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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-156, INTERACTION WITH RPT1.
    29. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEX1.
    30. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-72; THR-82; SER-163 AND THR-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
    32. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-259 AND SER-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
      Cited for: METHYLATION.
    35. "Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activity."
      Visweswaraiah J., Lageix S., Castilho B.A., Izotova L., Kinzy T.G., Hinnebusch A.G., Sattlegger E.
      J. Biol. Chem. 286:36568-36579(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GCN2, ASSOCIATION WITH RIBOSOMES.
    36. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases."
      Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.
      Proteomics 12:960-972(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-30 BY EFM1, METHYLATION AT LYS-316 BY SEE1, METHYLATION AT LYS-79 AND LYS-390.
    38. "A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A."
      Dzialo M.C., Travaglini K.J., Shen S., Loo J.A., Clarke S.G.
      Biochem. Biophys. Res. Commun. 455:382-389(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-79 BY EFM5.
    39. "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights into non-histone protein lysine methyltransferase activity."
      Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.
      J. Proteome Res. 13:1744-1756(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-30; LYS-79 AND LYS-390, METHYLATION AT LYS-316 BY SEE1.
    40. "Saccharomyces cerevisiae eukaryotic elongation factor 1A (eEF1A) is methylated at Lys-390 by a METTL21-like methyltransferase."
      Jakobsson M.E., Davydova E., Malecki J., Moen A., Falnes P.O.
      PLoS ONE 10:E0131426-E0131426(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-390 BY EFM6.
    41. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH EFB1.
    42. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH EFB1.

    Entry informationi

    Entry nameiEF1A_YEAST
    AccessioniPrimary (citable) accession number: P02994
    Secondary accession number(s): D6VQB6
    , Q7Z7U8, Q7Z8Q8, Q7Z8Q9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: June 8, 2016
    This is version 188 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 827 molecules/cell in log phase SD medium.1 Publication
    There are two genes for eEF1A in yeast.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
    6. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.