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P32471

- EF1B_YEAST

UniProt

P32471 - EF1B_YEAST

Protein

Elongation factor 1-beta

Gene

EFB1

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 138 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation of eEF1A-GTP, which rapidly forms a ternary complex with aminoacyl-tRNA that in turn displaces eEF1B from the complex.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: SGD
    2. translation elongation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. maintenance of translational fidelity Source: SGD
    2. negative regulation of actin filament bundle assembly Source: SGD
    3. positive regulation of GTPase activity Source: GOC
    4. regulation of translational termination Source: SGD
    5. translational elongation Source: SGD

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28818-MONOMER.
    UniPathwayiUPA00345.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 1-beta
    Short name:
    EF-1-beta
    Alternative name(s):
    Eukaryotic elongation factor 1Balpha
    Short name:
    eEF1Balpha
    Translation elongation factor 1B alpha
    Gene namesi
    Name:EFB1
    Synonyms:TEF5
    Ordered Locus Names:YAL003W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome I

    Organism-specific databases

    SGDiS000000003. EFB1.

    Subcellular locationi

    GO - Cellular componenti

    1. eukaryotic translation elongation factor 1 complex Source: SGD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi120 – 1223KSI → R in TEF5-7; reduces translation efficiency and enhances translation fidelity.
    Mutagenesisi121 – 1211S → I, L or N: Reduces translation efficiency and enhances translation fidelity. 1 Publication
    Mutagenesisi163 – 1631F → A: Temperature-sensitive. 1 Publication
    Mutagenesisi205 – 2051K → A: Loss of catalytic activity, but still binds to eEF1A. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 206205Elongation factor 1-betaPRO_0000155042Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei31 – 311Phosphoserine2 Publications
    Modified residuei86 – 861Phosphoserine4 Publications

    Post-translational modificationi

    S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP32471.
    PaxDbiP32471.
    PeptideAtlasiP32471.

    2D gel databases

    SWISS-2DPAGEP32471.

    Expressioni

    Gene expression databases

    GenevestigatoriP32471.

    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. eEF1Balpha interacts directly with eEF1A. eEF1Balpha and eEF1Bgamma form the eEF1B subcomplex with the GEF activity.2 Publications

    Protein-protein interaction databases

    BioGridi31787. 56 interactions.
    DIPiDIP-6445N.
    IntActiP32471. 6 interactions.
    MINTiMINT-441798.
    STRINGi4932.YAL003W.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi120 – 13112
    Helixi136 – 1449
    Beta strandi151 – 16212
    Beta strandi165 – 17511
    Turni176 – 1783
    Helixi181 – 1899
    Turni192 – 1943
    Beta strandi195 – 20511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F60X-ray1.67B113-206[»]
    1G7CX-ray2.05B113-206[»]
    1IJEX-ray2.40B117-206[»]
    1IJFX-ray3.00B117-206[»]
    2B7BX-ray2.60B113-204[»]
    2B7CX-ray1.80B113-204[»]
    ProteinModelPortaliP32471.
    SMRiP32471. Positions 117-206.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32471.

    Family & Domainsi

    Domaini

    The C-terminus (pos. 119-205) exhibits guanine nucleotide exchange activity.

    Sequence similaritiesi

    Belongs to the EF-1-beta/EF-1-delta family.Curated

    Phylogenomic databases

    eggNOGiCOG2092.
    GeneTreeiENSGT00390000011747.
    HOGENOMiHOG000207273.
    KOiK03232.
    OMAiYLECENN.
    OrthoDBiEOG7M3J9X.

    Family and domain databases

    Gene3Di3.30.70.60. 1 hit.
    InterProiIPR018940. EF-1_beta_acid_region_euk.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR014717. Transl_elong_EF1B/ribosomal_S6.
    IPR001326. Transl_elong_EF1B_B/D_CS.
    IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
    [Graphical view]
    PfamiPF10587. EF-1_beta_acid. 1 hit.
    PF00736. EF1_GNE. 1 hit.
    [Graphical view]
    SMARTiSM00888. EF1_GNE. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF54984. SSF54984. 1 hit.
    PROSITEiPS00824. EF1BD_1. 1 hit.
    PS00825. EF1BD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P32471-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTDFSKIE TLKQLNASLA DKSYIEGTAV SQADVTVFKA FQSAYPEFSR    50
    WFNHIASKAD EFDSFPAASA AAAEEEEDDD VDLFGSDDEE ADAEAEKLKA 100
    ERIAAYNAKK AAKPAKPAAK SIVTLDVKPW DDETNLEEMV ANVKAIEMEG 150
    LTWGAHQFIP IGFGIKKLQI NCVVEDDKVS LDDLQQSIEE DEDHVQSTDI 200
    AAMQKL 206
    Length:206
    Mass (Da):22,627
    Last modified:January 23, 2007 - v4
    Checksum:iBEA764852CE125F7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491S → F in BAA03165. (PubMed:8420802)Curated
    Sequence conflicti57 – 571S → F in BAA03165. (PubMed:8420802)Curated
    Sequence conflicti98 – 981L → W in BAA03165. (PubMed:8420802)Curated
    Sequence conflicti168 – 1681L → E AA sequence (PubMed:7895733)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14080 Genomic DNA. Translation: BAA03165.1.
    L22015 Genomic DNA. Translation: AAC04954.1.
    BK006935 Genomic DNA. Translation: DAA06983.1.
    PIRiS43445.
    RefSeqiNP_009398.1. NM_001178150.1.

    Genome annotation databases

    EnsemblFungiiYAL003W; YAL003W; YAL003W.
    GeneIDi851260.
    KEGGisce:YAL003W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14080 Genomic DNA. Translation: BAA03165.1 .
    L22015 Genomic DNA. Translation: AAC04954.1 .
    BK006935 Genomic DNA. Translation: DAA06983.1 .
    PIRi S43445.
    RefSeqi NP_009398.1. NM_001178150.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F60 X-ray 1.67 B 113-206 [» ]
    1G7C X-ray 2.05 B 113-206 [» ]
    1IJE X-ray 2.40 B 117-206 [» ]
    1IJF X-ray 3.00 B 117-206 [» ]
    2B7B X-ray 2.60 B 113-204 [» ]
    2B7C X-ray 1.80 B 113-204 [» ]
    ProteinModelPortali P32471.
    SMRi P32471. Positions 117-206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31787. 56 interactions.
    DIPi DIP-6445N.
    IntActi P32471. 6 interactions.
    MINTi MINT-441798.
    STRINGi 4932.YAL003W.

    2D gel databases

    SWISS-2DPAGE P32471.

    Proteomic databases

    MaxQBi P32471.
    PaxDbi P32471.
    PeptideAtlasi P32471.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YAL003W ; YAL003W ; YAL003W .
    GeneIDi 851260.
    KEGGi sce:YAL003W.

    Organism-specific databases

    SGDi S000000003. EFB1.

    Phylogenomic databases

    eggNOGi COG2092.
    GeneTreei ENSGT00390000011747.
    HOGENOMi HOG000207273.
    KOi K03232.
    OMAi YLECENN.
    OrthoDBi EOG7M3J9X.

    Enzyme and pathway databases

    UniPathwayi UPA00345 .
    BioCyci YEAST:G3O-28818-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32471.
    NextBioi 968216.
    PROi P32471.

    Gene expression databases

    Genevestigatori P32471.

    Family and domain databases

    Gene3Di 3.30.70.60. 1 hit.
    InterProi IPR018940. EF-1_beta_acid_region_euk.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR014717. Transl_elong_EF1B/ribosomal_S6.
    IPR001326. Transl_elong_EF1B_B/D_CS.
    IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
    [Graphical view ]
    Pfami PF10587. EF-1_beta_acid. 1 hit.
    PF00736. EF1_GNE. 1 hit.
    [Graphical view ]
    SMARTi SM00888. EF1_GNE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF54984. SSF54984. 1 hit.
    PROSITEi PS00824. EF1BD_1. 1 hit.
    PS00825. EF1BD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the elongation factor EF-1 beta homologue of Saccharomyces cerevisiae. EF-1 beta is essential for growth."
      Hiraga K., Suzuki K., Tsuchiya E., Miyakawa T.
      FEBS Lett. 316:165-169(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
      Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
      Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
      Norbeck J., Blomberg A.
      FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 14-22 AND 51-56.
      Strain: ATCC 38531 / Y41.
    6. Cited for: PROTEIN SEQUENCE OF 168-178.
      Strain: ATCC 204508 / S288c.
    7. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
      Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
      Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT ALA-2.
    8. "Mutations in elongation factor 1beta, a guanine nucleotide exchange factor, enhance translational fidelity."
      Carr-Schmid A., Valente L., Loik V.I., Williams T., Starita L.M., Kinzy T.G.
      Mol. Cell. Biol. 19:5257-5266(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-121.
    9. "A sampling of the yeast proteome."
      Futcher B., Latter G.I., Monardo P., McLaughlin C.S., Garrels J.I.
      Mol. Cell. Biol. 19:7357-7368(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    10. "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.
    11. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "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 SER-31 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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].
    16. "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) OF 113-206 IN COMPLEX WITH EEF1A, MUTAGENESIS OF PHE-163.
    17. "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) OF 113-206 IN COMPLEX WITH EEF1A, MUTAGENESIS OF LYS-205.

    Entry informationi

    Entry nameiEF1B_YEAST
    AccessioniPrimary (citable) accession number: P32471
    Secondary accession number(s): D6VPL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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 I
      Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

    External Data

    Dasty 3