Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Nucleotide bindingi14 – 21GTP8
    Nucleotide bindingi91 – 95GTP5
    Nucleotide bindingi153 – 156GTP4

    GO - Molecular functioni

    • GDP binding Source: SGD
    • GTPase activity Source: GO_Central
    • 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.
    R-SCE-6798695. Neutrophil degranulation.
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi122E → K: Reduces interaction with YEF3. 1 Publication1
    Mutagenesisi153N → D: Increases KM for GTP to 2.7 mM. 2 Publications1
    Mutagenesisi153N → 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 Publications1
    Mutagenesisi156D → E: Increases KM for GTP to 10.3 mM and reduces translation fidelity; when associated with T-152. 3 Publications1
    Mutagenesisi156D → N: Increases KM for GTP to 13.1 mM and reduces translation fidelity. Confers hyperresistance to canavanine. 3 Publications1
    Mutagenesisi156D → W: Increases KM for GTP to 4.2 mM. Preferres XTP over GTP as substrate. 3 Publications1
    Mutagenesisi286E → K in TEF2-1; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. 1 Publication1
    Mutagenesisi317E → K in TEF2-2; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000909731 – 458Elongation factor 1-alphaAdd BLAST458

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1Blocked amino end (Met)1
    Modified residuei18PhosphoserineCombined sources1
    Modified residuei30N6-methyllysine; by EFM13 Publications1
    Modified residuei72PhosphothreonineCombined sources1
    Modified residuei79N6,N6,N6-trimethyllysine; by EFM54 Publications1
    Modified residuei82PhosphothreonineCombined sources1
    Modified residuei163PhosphoserineCombined sources1
    Cross-linki224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Cross-linki242Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Cross-linki253Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei259PhosphothreonineCombined sources1
    Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei289PhosphoserineCombined sources1
    Modified residuei316N6,N6-dimethyllysine; by EFM4; alternate3 Publications1
    Modified residuei316N6-methyllysine; by EFM4; alternate1 Publication1
    Modified residuei390N6-methyllysine; by EFM64 Publications1
    Cross-linki393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei414PhosphoserineCombined sources1
    Modified residuei430PhosphothreonineCombined sources1
    Cross-linki437Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei458Lysine methyl ester1 Publication1

    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)DescriptionActionsGraphical viewLength
    Sitei298Not modified1
    Sitei372Not modified1

    Keywords - PTMi

    Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    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 interactors.
    36251. 167 interactors.
    DIPiDIP-2250N.
    IntActiP02994. 723 interactors.
    MINTiMINT-441761.

    Structurei

    Secondary structure

    1458
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 14Combined sources9
    Helixi20 – 31Combined sources12
    Helixi36 – 45Combined sources10
    Helixi46 – 49Combined sources4
    Beta strandi50 – 52Combined sources3
    Helixi56 – 68Combined sources13
    Beta strandi78 – 81Combined sources4
    Beta strandi83 – 91Combined sources9
    Helixi98 – 104Combined sources7
    Beta strandi105 – 107Combined sources3
    Beta strandi110 – 117Combined sources8
    Helixi120 – 126Combined sources7
    Helixi132 – 142Combined sources11
    Beta strandi147 – 153Combined sources7
    Helixi155 – 158Combined sources4
    Helixi162 – 179Combined sources18
    Helixi183 – 185Combined sources3
    Beta strandi188 – 190Combined sources3
    Turni193 – 195Combined sources3
    Turni197 – 199Combined sources3
    Beta strandi212 – 215Combined sources4
    Beta strandi217 – 225Combined sources9
    Helixi226 – 231Combined sources6
    Beta strandi239 – 242Combined sources4
    Beta strandi245 – 254Combined sources10
    Turni255 – 257Combined sources3
    Beta strandi258 – 264Combined sources7
    Beta strandi275 – 279Combined sources5
    Turni280 – 282Combined sources3
    Beta strandi283 – 292Combined sources10
    Beta strandi295 – 298Combined sources4
    Beta strandi305 – 312Combined sources8
    Turni315 – 317Combined sources3
    Beta strandi323 – 326Combined sources4
    Beta strandi336 – 344Combined sources9
    Beta strandi358 – 361Combined sources4
    Beta strandi364 – 377Combined sources14
    Turni379 – 381Combined sources3
    Beta strandi384 – 388Combined sources5
    Beta strandi397 – 406Combined sources10
    Turni413 – 415Combined sources3
    Helixi417 – 419Combined sources3
    Beta strandi420 – 426Combined sources7
    Beta strandi429 – 440Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02994.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini5 – 240tr-type GAdd BLAST236

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni14 – 21G1By similarity8
    Regioni70 – 74G2By similarity5
    Regioni91 – 94G3By similarity4
    Regioni153 – 156G4By similarity4
    Regioni192 – 194G5By similarity3

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00670000097815.
    ENSGT00860000134053.
    HOGENOMiHOG000229291.
    InParanoidiP02994.
    KOiK03231.
    OMAiVNYDQKR.
    OrthoDBiEOG092C2HV8.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00118_A. EF_Tu_A. 1 hit.
    InterProiIPR004161. EFTu-like_2.
    IPR031157. 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.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti86Q → E AA sequence (PubMed:3882705).Curated1

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32820. 183 interactors.
    36251. 167 interactors.
    DIPiDIP-2250N.
    IntActiP02994. 723 interactors.
    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.
    ENSGT00860000134053.
    HOGENOMiHOG000229291.
    InParanoidiP02994.
    KOiK03231.
    OMAiVNYDQKR.
    OrthoDBiEOG092C2HV8.

    Enzyme and pathway databases

    UniPathwayiUPA00345.
    BioCyciYEAST:G3O-29075-MONOMER.
    YEAST:G3O-34224-MONOMER.
    ReactomeiR-SCE-156842. Eukaryotic Translation Elongation.
    R-SCE-3371511. HSF1 activation.
    R-SCE-6798695. Neutrophil degranulation.

    Miscellaneous databases

    EvolutionaryTraceiP02994.
    PROiP02994.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00118_A. EF_Tu_A. 1 hit.
    InterProiIPR004161. EFTu-like_2.
    IPR031157. 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.
    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...

    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: November 30, 2016
    This is version 193 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.