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P32324

- EF2_YEAST

UniProt

P32324 - EF2_YEAST

Protein

Elongation factor 2

Gene

EFT1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 338GTPBy similarity
    Nucleotide bindingi104 – 1085GTPBy similarity
    Nucleotide bindingi158 – 1614GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: SGD
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. rRNA binding Source: UniProtKB-KW
    5. translation elongation factor activity Source: SGD

    GO - Biological processi

    1. GTP catabolic process Source: GOC
    2. maintenance of translational fidelity Source: SGD
    3. positive regulation of translational elongation Source: SGD
    4. translational elongation Source: SGD

    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.
    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: Chromosome IV, UP000002311: Chromosome XV

    Organism-specific databases

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

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 residuei579 – 5791Phosphoserine2 Publications
    Modified residuei699 – 6991Diphthamide1 Publication
    Modified residuei713 – 7131Phosphothreonine2 Publications
    Modified residuei763 – 7631Phosphothreonine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32324.
    PaxDbiP32324.
    PRIDEiP32324.

    2D gel databases

    SWISS-2DPAGEP32324.

    Expressioni

    Gene expression databases

    GenevestigatoriP32324.

    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. 131 interactions.
    34529. 83 interactions.
    DIPiDIP-4911N.
    IntActiP32324. 138 interactions.
    MINTiMINT-8285544.
    STRINGi4932.YDR385W.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N0UX-ray2.12A1-842[»]
    1N0VX-ray2.85C/D1-842[»]
    1S1Helectron microscopy11.70T1-842[»]
    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[»]
    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.
    GeneTreeiENSGT00750000117652.
    ENSGT00750000118348.
    HOGENOMiHOG000231589.
    KOiK03234.
    OMAiRWAPVPE.
    OrthoDBiEOG7966SQ.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_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.
    PF00009. GTP_EFTU. 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

    MVAFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK    50
    AGEARFTDTR KDEQERGITI KSTAISLYSE MSDEDVKEIK QKTDGNSFLI 100
    NLIDSPGHVD FSSEVTAALR VTDGALVVVD TIEGVCVQTE TVLRQALGER 150
    IKPVVVINKV DRALLELQVS KEDLYQTFAR TVESVNVIVS TYADEVLGDV 200
    QVYPARGTVA FGSGLHGWAF TIRQFATRYA KKFGVDKAKM MDRLWGDSFF 250
    NPKTKKWTNK DTDAEGKPLE RAFNMFILDP IFRLFTAIMN FKKDEIPVLL 300
    EKLEIVLKGD EKDLEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA 350
    YRAEQLYEGP ADDANCIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV 400
    FAGTVKSGQK VRIQGPNYVP GKKDDLFIKA IQRVVLMMGR FVEPIDDCPA 450
    GNIIGLVGID QFLLKTGTLT TSETAHNMKV MKFSVSPVVQ VAVEVKNAND 500
    LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI CLQDLEHDHA 550
    GVPLKISPPV VAYRETVESE SSQTALSKSP NKHNRIYLKA EPIDEEVSLA 600
    IENGIINPRD DFKARARIMA DDYGWDVTDA RKIWCFGPDG NGPNLVIDQT 650
    KAVQYLHEIK DSVVAAFQWA TKEGPIFGEE MRSVRVNILD VTLHADAIHR 700
    GGGQIIPTMR RATYAGFLLA DPKIQEPVFL VEIQCPEQAV GGIYSVLNKK 750
    RGQVVSEEQR PGTPLFTVKA YLPVNESFGF TGELRQATGG QAFPQMVFDH 800
    WSTLGSDPLD PTSKAGEIVL AARKRHGMKE EVPGWQEYYD KL 842
    Length:842
    Mass (Da):93,289
    Last modified:October 1, 1993 - v1
    Checksum:iFD2F8073CB9B66AA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A41778.
    RefSeqi NP_010673.1. NM_001180693.1.
    NP_014776.1. NM_001183552.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N0U X-ray 2.12 A 1-842 [» ]
    1N0V X-ray 2.85 C/D 1-842 [» ]
    1S1H electron microscopy 11.70 T 1-842 [» ]
    1U2R X-ray 2.60 A 1-842 [» ]
    1ZM2 X-ray 3.07 A/C/E 1-842 [» ]
    1ZM3 X-ray 3.07 A/C/E 1-842 [» ]
    1ZM4 X-ray 2.90 A/C/E 1-842 [» ]
    1ZM9 X-ray 2.80 A/C/E 1-842 [» ]
    2E1R X-ray 3.15 A 1-842 [» ]
    2NPF X-ray 2.90 A/B 1-842 [» ]
    2P8W electron microscopy 11.30 T 1-842 [» ]
    2P8X electron microscopy 9.70 T 1-842 [» ]
    2P8Y electron microscopy 11.70 T 1-842 [» ]
    2P8Z electron microscopy 8.90 T 1-842 [» ]
    2ZIT X-ray 3.00 A/C/E 1-842 [» ]
    3B78 X-ray 2.50 A/C/E 1-842 [» ]
    3B82 X-ray 2.35 A/C/E 1-842 [» ]
    3B8H X-ray 2.50 A/C/E 1-842 [» ]
    3DNY electron microscopy 12.60 T 1-842 [» ]
    ProteinModelPortali P32324.
    SMRi P32324. Positions 2-842.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32446. 131 interactions.
    34529. 83 interactions.
    DIPi DIP-4911N.
    IntActi P32324. 138 interactions.
    MINTi MINT-8285544.
    STRINGi 4932.YDR385W.

    2D gel databases

    SWISS-2DPAGE P32324.

    Proteomic databases

    MaxQBi P32324.
    PaxDbi P32324.
    PRIDEi P32324.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR385W ; YDR385W ; YDR385W .
    YOR133W ; YOR133W ; YOR133W .
    GeneIDi 851993.
    854301.
    KEGGi sce:YDR385W.
    sce:YOR133W.

    Organism-specific databases

    CYGDi YDR385w.
    YOR133w.
    SGDi S000005659. EFT1.
    S000002793. EFT2.

    Phylogenomic databases

    eggNOGi COG0480.
    GeneTreei ENSGT00750000117652.
    ENSGT00750000118348.
    HOGENOMi HOG000231589.
    KOi K03234.
    OMAi RWAPVPE.
    OrthoDBi EOG7966SQ.

    Enzyme and pathway databases

    UniPathwayi UPA00345 .
    BioCyci YEAST:G3O-29933-MONOMER.
    YEAST:G3O-33657-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32324.
    NextBioi 970163.
    PROi P32324.

    Gene expression databases

    Genevestigatori P32324.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view ]
    Pfami PF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SMARTi SM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    23. "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.
    24. "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: October 1, 2014
    This is version 154 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