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Protein

Elongation factor 2

Gene

EFT1

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

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.1 Publication

Enzyme regulationi

Inhibited by fusidic acid and sordarin, which prevent the release of eEF2 from the ribosome after the translocation step. While fusidic acid acts on all eukaryotic eEF2, sordarin specifically binds and inhibits only selected fungal eEF2. Inhibited by diphtheria toxin and Pseudomonas aeruginosa exotoxin A (ETA), which ADP-ribosylate the diphthamide residue.

Kineticsi

  1. KM=0.010 mM for GTP

    Pathway: 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 bindingi26 – 338GTPBy similarity
    Nucleotide bindingi104 – 1085GTPBy similarity
    Nucleotide bindingi158 – 1614GTPBy similarity

    GO - Molecular functioni

    • GTPase activity Source: SGD
    • GTP binding Source: UniProtKB-KW
    • rRNA binding Source: UniProtKB-KW
    • translation elongation factor activity Source: SGD

    GO - Biological processi

    • maintenance of translational fidelity Source: SGD
    • positive regulation of translational elongation Source: SGD
    • translational elongation Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding, RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29933-MONOMER.
    YEAST:G3O-33657-MONOMER.
    ReactomeiREACT_343353. Peptide chain elongation.
    REACT_345803. Synthesis of diphthamide-EEF2.
    UniPathwayiUPA00345.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 2
    Short name:
    EF-2
    Alternative name(s):
    Eukaryotic elongation factor 2
    Short name:
    eEF2
    Ribosomal translocase
    Translation elongation factor 2
    Gene namesi
    Name:EFT1
    Ordered Locus Names:YOR133W
    ORF Names:O3317, YOR3317W
    AND
    Name:EFT2
    Ordered Locus Names:YDR385W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componentsi: Chromosome IV, Chromosome XV

    Organism-specific databases

    CYGDiYDR385w.
    YOR133w.
    SGDiS000005659. EFT1.
    S000002793. EFT2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801R → G: Causes resistance to fusidic acid and reduces sensitivity to sordarin. 1 Publication
    Mutagenesisi187 – 1871V → F: Causes resistance to fusidic acid and reduces sensitivity to sordarin. 1 Publication
    Mutagenesisi490 – 4901Q → E: Reduces sensitivity to sordarin. 1 Publication
    Mutagenesisi521 – 5211Y → D, N or S: Reduces sensitivity to fusidic acid and sordarin. 1 Publication
    Mutagenesisi523 – 5231S → F or P: Causes resistance to fusidic acid and sordarin. 1 Publication
    Mutagenesisi529 – 5291I → T: Reduces sensitivity to sordarin. 1 Publication
    Mutagenesisi559 – 5591P → L or R: Causes resistance to fusidic acid and sordarin. 1 Publication
    Mutagenesisi562 – 5621A → P: Reduces sensitivity to fusidic acid and causes resistance to sordarin. 1 Publication
    Mutagenesisi580 – 5801P → H: Causes impaired ribosomal translocation with an increased rate of -1 programmed ribosomal frameshift read-through during translation. 1 Publication
    Mutagenesisi699 – 6991H → D, E, L or M: Prevents post-translational modification of this residue to diphthamide. Results in a functional protein that is resistant to diphtheria toxin. 1 Publication
    Mutagenesisi701 – 7011G → R: Prevents ADP-ribosylation of the diphthamide by diphtheria toxin. 1 Publication
    Mutagenesisi727 – 7271P → S: Causes resistance to sordarin. 1 Publication
    Mutagenesisi774 – 7741V → F: Causes resistance to sordarin. 1 Publication
    Mutagenesisi790 – 7901Missing : Causes resistance to fusidic acid and sordarin. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 842842Elongation factor 2PRO_0000091024Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei509 – 5091N6,N6,N6-trimethyllysine; by EFM3; alternate2 Publications
    Modified residuei509 – 5091N6,N6-dimethyllysine; by EFM3; alternate3 Publications
    Modified residuei509 – 5091N6-methyllysine; by EFM3; alternate2 Publications
    Modified residuei579 – 5791Phosphoserine1 Publication
    Modified residuei613 – 6131N6,N6-dimethyllysine; by EFM2; alternate2 Publications
    Modified residuei613 – 6131N6-methyllysine; by EFM2; alternate2 Publications
    Modified residuei699 – 6991Diphthamide1 Publication
    Modified residuei713 – 7131Phosphothreonine1 Publication
    Modified residuei763 – 7631Phosphothreonine1 Publication

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP32324.
    PaxDbiP32324.
    PRIDEiP32324.

    2D gel databases

    SWISS-2DPAGEP32324.

    Interactioni

    Subunit structurei

    Binds to 80S ribosomes. Interacts directly with the 40S ribosomal subunit protein RPL9A, the 60S ribosomal subunit proteins RPL12A and RPS23A, as well as the 18S rRNA and the 25S rRNA. Interacts with RPL0.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RPP0P053172EBI-6333,EBI-15447
    SKP1P522862EBI-6333,EBI-4090

    Protein-protein interaction databases

    BioGridi32446. 137 interactions.
    34529. 90 interactions.
    DIPiDIP-4911N.
    IntActiP32324. 138 interactions.
    MINTiMINT-8285544.
    STRINGi4932.YOR133W.

    Structurei

    Secondary structure

    1
    842
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43Combined sources
    Helixi6 – 149Combined sources
    Helixi16 – 183Combined sources
    Beta strandi19 – 257Combined sources
    Helixi28 – 303Combined sources
    Helixi32 – 4312Combined sources
    Beta strandi44 – 485Combined sources
    Beta strandi74 – 807Combined sources
    Helixi83 – 886Combined sources
    Beta strandi95 – 1039Combined sources
    Helixi109 – 1113Combined sources
    Helixi113 – 1208Combined sources
    Beta strandi123 – 1308Combined sources
    Turni131 – 1333Combined sources
    Helixi137 – 14812Combined sources
    Beta strandi152 – 1587Combined sources
    Helixi160 – 1656Combined sources
    Helixi171 – 19222Combined sources
    Helixi195 – 1973Combined sources
    Helixi204 – 2063Combined sources
    Beta strandi209 – 2135Combined sources
    Turni214 – 2174Combined sources
    Beta strandi218 – 2214Combined sources
    Helixi222 – 2309Combined sources
    Turni231 – 2344Combined sources
    Helixi237 – 2437Combined sources
    Beta strandi245 – 2473Combined sources
    Beta strandi249 – 2513Combined sources
    Turni252 – 2554Combined sources
    Beta strandi256 – 2594Combined sources
    Beta strandi261 – 2633Combined sources
    Turni264 – 2663Combined sources
    Helixi272 – 2765Combined sources
    Helixi278 – 28912Combined sources
    Helixi295 – 3028Combined sources
    Helixi309 – 3135Combined sources
    Helixi316 – 32712Combined sources
    Helixi330 – 34112Combined sources
    Helixi345 – 35612Combined sources
    Beta strandi357 – 3593Combined sources
    Helixi364 – 3707Combined sources
    Beta strandi374 – 3774Combined sources
    Beta strandi379 – 39012Combined sources
    Beta strandi394 – 40613Combined sources
    Beta strandi410 – 4145Combined sources
    Beta strandi420 – 4223Combined sources
    Beta strandi426 – 4305Combined sources
    Beta strandi433 – 4386Combined sources
    Beta strandi441 – 4499Combined sources
    Beta strandi453 – 4586Combined sources
    Turni460 – 4623Combined sources
    Beta strandi465 – 4717Combined sources
    Beta strandi489 – 4979Combined sources
    Helixi498 – 5003Combined sources
    Helixi501 – 51414Combined sources
    Beta strandi519 – 5224Combined sources
    Beta strandi528 – 5347Combined sources
    Helixi535 – 54713Combined sources
    Beta strandi554 – 5574Combined sources
    Beta strandi564 – 5696Combined sources
    Beta strandi575 – 5784Combined sources
    Beta strandi580 – 5823Combined sources
    Beta strandi585 – 5928Combined sources
    Helixi595 – 6028Combined sources
    Beta strandi604 – 6063Combined sources
    Beta strandi608 – 6103Combined sources
    Helixi612 – 62110Combined sources
    Helixi627 – 6315Combined sources
    Beta strandi633 – 6386Combined sources
    Turni639 – 6413Combined sources
    Beta strandi642 – 6487Combined sources
    Helixi656 – 67217Combined sources
    Turni675 – 6773Combined sources
    Beta strandi683 – 69210Combined sources
    Helixi697 – 6993Combined sources
    Helixi702 – 71918Combined sources
    Beta strandi722 – 73514Combined sources
    Helixi737 – 7393Combined sources
    Helixi740 – 7489Combined sources
    Turni749 – 7513Combined sources
    Beta strandi753 – 7586Combined sources
    Beta strandi766 – 7738Combined sources
    Helixi774 – 7763Combined sources
    Helixi780 – 7878Combined sources
    Turni788 – 7903Combined sources
    Beta strandi793 – 80311Combined sources
    Beta strandi811 – 8133Combined sources
    Helixi814 – 82512Combined sources
    Helixi835 – 8384Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N0UX-ray2.12A1-842[»]
    1N0VX-ray2.85C/D1-842[»]
    1U2RX-ray2.60A1-842[»]
    1ZM2X-ray3.07A/C/E1-842[»]
    1ZM3X-ray3.07A/C/E1-842[»]
    1ZM4X-ray2.90A/C/E1-842[»]
    1ZM9X-ray2.80A/C/E1-842[»]
    2E1RX-ray3.15A1-842[»]
    2NPFX-ray2.90A/B1-842[»]
    2P8Welectron microscopy11.30T1-842[»]
    2P8Xelectron microscopy9.70T1-842[»]
    2P8Yelectron microscopy11.70T1-842[»]
    2P8Zelectron microscopy8.90T1-842[»]
    2ZITX-ray3.00A/C/E1-842[»]
    3B78X-ray2.50A/C/E1-842[»]
    3B82X-ray2.35A/C/E1-842[»]
    3B8HX-ray2.50A/C/E1-842[»]
    3DNYelectron microscopy12.60T1-842[»]
    4V4Belectron microscopy11.70AT1-842[»]
    ProteinModelPortaliP32324.
    SMRiP32324. Positions 2-842.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32324.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 346330tr-type GPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation
    Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0480.
    GeneTreeiENSGT00770000120583.
    ENSGT00790000123721.
    HOGENOMiHOG000231589.
    InParanoidiP32324.
    KOiK03234.
    OMAiKMAPEEF.
    OrthoDBiEOG7966SQ.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR031157. G_TR_CS.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR000795. TF_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view]
    PfamiPF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SMARTiSM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32324-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVAFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK
    60 70 80 90 100
    AGEARFTDTR KDEQERGITI KSTAISLYSE MSDEDVKEIK QKTDGNSFLI
    110 120 130 140 150
    NLIDSPGHVD FSSEVTAALR VTDGALVVVD TIEGVCVQTE TVLRQALGER
    160 170 180 190 200
    IKPVVVINKV DRALLELQVS KEDLYQTFAR TVESVNVIVS TYADEVLGDV
    210 220 230 240 250
    QVYPARGTVA FGSGLHGWAF TIRQFATRYA KKFGVDKAKM MDRLWGDSFF
    260 270 280 290 300
    NPKTKKWTNK DTDAEGKPLE RAFNMFILDP IFRLFTAIMN FKKDEIPVLL
    310 320 330 340 350
    EKLEIVLKGD EKDLEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA
    360 370 380 390 400
    YRAEQLYEGP ADDANCIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV
    410 420 430 440 450
    FAGTVKSGQK VRIQGPNYVP GKKDDLFIKA IQRVVLMMGR FVEPIDDCPA
    460 470 480 490 500
    GNIIGLVGID QFLLKTGTLT TSETAHNMKV MKFSVSPVVQ VAVEVKNAND
    510 520 530 540 550
    LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI CLQDLEHDHA
    560 570 580 590 600
    GVPLKISPPV VAYRETVESE SSQTALSKSP NKHNRIYLKA EPIDEEVSLA
    610 620 630 640 650
    IENGIINPRD DFKARARIMA DDYGWDVTDA RKIWCFGPDG NGPNLVIDQT
    660 670 680 690 700
    KAVQYLHEIK DSVVAAFQWA TKEGPIFGEE MRSVRVNILD VTLHADAIHR
    710 720 730 740 750
    GGGQIIPTMR RATYAGFLLA DPKIQEPVFL VEIQCPEQAV GGIYSVLNKK
    760 770 780 790 800
    RGQVVSEEQR PGTPLFTVKA YLPVNESFGF TGELRQATGG QAFPQMVFDH
    810 820 830 840
    WSTLGSDPLD PTSKAGEIVL AARKRHGMKE EVPGWQEYYD KL
    Length:842
    Mass (Da):93,289
    Last modified:October 1, 1993 - v1
    Checksum:iFD2F8073CB9B66AA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M59369 Genomic DNA. Translation: AAA21646.1.
    M59370 Genomic DNA. Translation: AAA51398.1.
    X90518 Genomic DNA. Translation: CAA62116.1.
    X94335 Genomic DNA. Translation: CAA64052.1.
    U32274 Genomic DNA. Translation: AAB64827.1.
    U28373 Genomic DNA. Translation: AAB64821.1.
    Z75041 Genomic DNA. Translation: CAA99332.1.
    AY497635 Genomic DNA. Translation: AAT12549.1.
    BK006948 Genomic DNA. Translation: DAA10907.1.
    BK006938 Genomic DNA. Translation: DAA12229.1.
    PIRiA41778.
    RefSeqiNP_010673.1. NM_001180693.1.
    NP_014776.1. NM_001183552.1.

    Genome annotation databases

    EnsemblFungiiYDR385W; YDR385W; YDR385W.
    YOR133W; YOR133W; YOR133W.
    GeneIDi851993.
    854301.
    KEGGisce:YDR385W.
    sce:YOR133W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M59369 Genomic DNA. Translation: AAA21646.1.
    M59370 Genomic DNA. Translation: AAA51398.1.
    X90518 Genomic DNA. Translation: CAA62116.1.
    X94335 Genomic DNA. Translation: CAA64052.1.
    U32274 Genomic DNA. Translation: AAB64827.1.
    U28373 Genomic DNA. Translation: AAB64821.1.
    Z75041 Genomic DNA. Translation: CAA99332.1.
    AY497635 Genomic DNA. Translation: AAT12549.1.
    BK006948 Genomic DNA. Translation: DAA10907.1.
    BK006938 Genomic DNA. Translation: DAA12229.1.
    PIRiA41778.
    RefSeqiNP_010673.1. NM_001180693.1.
    NP_014776.1. NM_001183552.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N0UX-ray2.12A1-842[»]
    1N0VX-ray2.85C/D1-842[»]
    1U2RX-ray2.60A1-842[»]
    1ZM2X-ray3.07A/C/E1-842[»]
    1ZM3X-ray3.07A/C/E1-842[»]
    1ZM4X-ray2.90A/C/E1-842[»]
    1ZM9X-ray2.80A/C/E1-842[»]
    2E1RX-ray3.15A1-842[»]
    2NPFX-ray2.90A/B1-842[»]
    2P8Welectron microscopy11.30T1-842[»]
    2P8Xelectron microscopy9.70T1-842[»]
    2P8Yelectron microscopy11.70T1-842[»]
    2P8Zelectron microscopy8.90T1-842[»]
    2ZITX-ray3.00A/C/E1-842[»]
    3B78X-ray2.50A/C/E1-842[»]
    3B82X-ray2.35A/C/E1-842[»]
    3B8HX-ray2.50A/C/E1-842[»]
    3DNYelectron microscopy12.60T1-842[»]
    4V4Belectron microscopy11.70AT1-842[»]
    ProteinModelPortaliP32324.
    SMRiP32324. Positions 2-842.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32446. 137 interactions.
    34529. 90 interactions.
    DIPiDIP-4911N.
    IntActiP32324. 138 interactions.
    MINTiMINT-8285544.
    STRINGi4932.YOR133W.

    2D gel databases

    SWISS-2DPAGEP32324.

    Proteomic databases

    MaxQBiP32324.
    PaxDbiP32324.
    PRIDEiP32324.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDR385W; YDR385W; YDR385W.
    YOR133W; YOR133W; YOR133W.
    GeneIDi851993.
    854301.
    KEGGisce:YDR385W.
    sce:YOR133W.

    Organism-specific databases

    CYGDiYDR385w.
    YOR133w.
    SGDiS000005659. EFT1.
    S000002793. EFT2.

    Phylogenomic databases

    eggNOGiCOG0480.
    GeneTreeiENSGT00770000120583.
    ENSGT00790000123721.
    HOGENOMiHOG000231589.
    InParanoidiP32324.
    KOiK03234.
    OMAiKMAPEEF.
    OrthoDBiEOG7966SQ.

    Enzyme and pathway databases

    UniPathwayiUPA00345.
    BioCyciYEAST:G3O-29933-MONOMER.
    YEAST:G3O-33657-MONOMER.
    ReactomeiREACT_343353. Peptide chain elongation.
    REACT_345803. Synthesis of diphthamide-EEF2.

    Miscellaneous databases

    EvolutionaryTraceiP32324.
    NextBioi970163.
    PROiP32324.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR031157. G_TR_CS.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR000795. TF_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view]
    PfamiPF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SMARTiSM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling."
      Perentesis J.P., Phan L.D., Laporte D.C., Livingston D.M., Bodley J.W.
      J. Biol. Chem. 267:1190-1197(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1 AND EFT2).
    2. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
      Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
      Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1).
      Strain: ATCC 96604 / S288c / FY1679.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1).
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT2).
      Strain: ATCC 204508 / S288c.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1).
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION (EFT1 AND EFT2).
      Strain: ATCC 204508 / S288c.
    7. Cited for: PROTEIN SEQUENCE OF 411-422 AND 505-513.
      Strain: ATCC 204508 / S288c.
    8. "Phylogeny and evolution of medical species of Candida and related taxa: a multigenic analysis."
      Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.
      J. Clin. Microbiol. 42:5624-5635(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-785.
    9. "Isolation and properties of the trypsin-derived ADP-ribosyl peptide from diphtheria toxin-modified yeast elongation factor 2."
      Van Ness B.G., Howard J.B., Bodley J.W.
      J. Biol. Chem. 253:8687-8690(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 686-700, DIPHTHAMIDE AT HIS-699.
    10. "Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endogenous kinase."
      Donovan M.G., Bodley J.W.
      FEBS Lett. 291:303-306(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    11. "Expression of non-ADP-ribosylatable, diphtheria toxin-resistant elongation factor 2 in Saccharomyces cerevisiae."
      Kimata Y., Harashima S., Kohno K.
      Biochem. Biophys. Res. Commun. 191:1145-1151(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-701.
    12. "Saccharomyces cerevisiae elongation factor 2. Mutagenesis of the histidine precursor of diphthamide yields a functional protein that is resistant to diphtheria toxin."
      Phan L.D., Perentesis J.P., Bodley J.W.
      J. Biol. Chem. 268:8665-8668(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-699.
    13. "Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis."
      Justice M.C., Hsu M.-J., Tse B., Ku T., Balkovec J., Schmatz D., Nielsen J.
      J. Biol. Chem. 273:3148-3151(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-180; VAL-187; GLN-490; TYR-521; SER-523; ILE-529; PRO-559; ALA-562; PRO-727; VAL-774 AND GLY-790.
    14. "Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components."
      Lalioti V.S., Perez-Fernandez J., Remacha M.A., Ballesta J.P.G.
      Mol. Microbiol. 46:719-729(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPL0.
    15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-579; THR-713 AND THR-763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult."
      Hekman K.E., Yu G.Y., Brown C.D., Zhu H., Du X., Gervin K., Undlien D.E., Peterson A., Stevanin G., Clark H.B., Pulst S.M., Bird T.D., White K.P., Gomez C.M.
      Hum. Mol. Genet. 21:5472-5483(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-580.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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].
    22. "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-509.
    23. "Elongation factor methyltransferase 3 - A novel eukaryotic lysine methyltransferase."
      Zhang L., Hamey J.J., Hart-Smith G., Erce M.A., Wilkins M.R.
      Biochem. Biophys. Res. Commun. 451:229-234(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-509 BY EFM3, METHYLATION AT LYS-613 BY EFM2.
    24. "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-509, METHYLATION AT LYS-613 BY EFM2.
    25. "Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase."
      Joergensen R., Ortiz P.A., Carr-Schmid A., Nissen P., Kinzy T.G., Andersen G.R.
      Nat. Struct. Biol. 10:379-385(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SORDARIN.
    26. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
      Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
      EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.7 ANGSTROMS) IN COMPLEX WITH 80S RIBOSOME AND SORDARIN, FUNCTION, INTERACTION WITH RPL9A; RPL12A; RPS23A; 18S RRNA AND 25S RRNA.
    27. "Crystal structure of ADP-ribosylated ribosomal translocase from Saccharomyces cerevisiae."
      Joergensen R., Yates S.P., Teal D.J., Nilsson J., Prentice G.A., Merrill A.R., Andersen G.R.
      J. Biol. Chem. 279:45919-45925(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF ADP-RIBOSYLATED FORM IN COMPLEX WITH GDP AND SORDARIN.

    Entry informationi

    Entry nameiEF2_YEAST
    AccessioniPrimary (citable) accession number: P32324
    Secondary accession number(s): D6VT19, Q6JEF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: June 24, 2015
    This is version 162 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 160782 molecules/cell in log phase SD medium.1 Publication
    There are 2 genes for eEF2 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
    6. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3

    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 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.