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P29547

- EF1G1_YEAST

UniProt

P29547 - EF1G1_YEAST

Protein

Elongation factor 1-gamma 1

Gene

CAM1

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 144 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components. May be involved in transcriptional regulation of MXR1.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. calcium ion binding Source: SGD
    2. phospholipid binding Source: SGD
    3. transcription coactivator activity Source: SGD
    4. translation elongation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. positive regulation of transcription from RNA polymerase II promoter Source: SGD
    2. ribosome biogenesis Source: SGD

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33961-MONOMER.
    UniPathwayiUPA00345.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 1-gamma 1
    Short name:
    EF-1-gamma 1
    Alternative name(s):
    Calcium and membrane-binding protein 1
    Calcium phospholipid-binding protein
    Short name:
    CPBP
    Eukaryotic elongation factor 1Bgamma 1
    Short name:
    eEF1Bgamma 1
    Translation elongation factor 1B gamma 1
    Gene namesi
    Name:CAM1
    Synonyms:TEF3
    Ordered Locus Names:YPL048W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPL048w.
    SGDiS000005969. CAM1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 415414Elongation factor 1-gamma 1PRO_0000208831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei32 – 321Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP29547.
    PaxDbiP29547.
    PeptideAtlasiP29547.

    Expressioni

    Gene expression databases

    GenevestigatoriP29547.

    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. The eEF1B subcomplex with the GEF activity is formed of eEF1Balpha and eEF1Bgamma. CAM1 interacts with EFB1. Component of a complex bound to MXR1 promoter region.1 Publication

    Protein-protein interaction databases

    BioGridi36132. 53 interactions.
    DIPiDIP-6813N.
    IntActiP29547. 11 interactions.
    MINTiMINT-644858.
    STRINGi4932.YPL048W.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Helixi12 – 2413
    Beta strandi29 – 313
    Helixi33 – 353
    Helixi37 – 437
    Beta strandi49 – 535
    Helixi55 – 573
    Beta strandi59 – 624
    Helixi63 – 7311
    Helixi77 – 837
    Helixi90 – 10415
    Turni105 – 1084
    Helixi109 – 1135
    Helixi115 – 1184
    Helixi126 – 14722
    Beta strandi151 – 1577
    Helixi160 – 17516
    Helixi179 – 1846
    Helixi186 – 19712
    Turni199 – 2013
    Helixi202 – 2043

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NHYX-ray3.00A1-219[»]
    ProteinModelPortaliP29547.
    SMRiP29547. Positions 1-219, 255-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29547.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7877GST N-terminalAdd
    BLAST
    Domaini89 – 215127GST C-terminalAdd
    BLAST
    Domaini254 – 415162EF-1-gamma C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Ths GST-like domain mediates the interaction to eEFB1 and may be responsible for dimerization of the eEF1 complex.

    Sequence similaritiesi

    Contains 1 EF-1-gamma C-terminal domain.PROSITE-ProRule annotation
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    GeneTreeiENSGT00390000007552.
    HOGENOMiHOG000201196.
    KOiK03233.
    OMAiENYSIWY.
    OrthoDBiEOG7RBZK2.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.30.70.1010. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    IPR001662. Transl_elong_EF1_G_con.
    [Graphical view]
    PfamiPF00647. EF1G. 1 hit.
    PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    SSF89942. SSF89942. 1 hit.
    PROSITEiPS50040. EF1G_C. 1 hit.
    PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29547-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQGTLYANF RIRTWVPRGL VKALKLDVKV VTPDAAAEQF ARDFPLKKVP    50
    AFVGPKGYKL TEAMAINYYL VKLSQDDKMK TQLLGADDDL NAQAQIIRWQ 100
    SLANSDLCIQ IANTIVPLKG GAPYNKKSVD SAMDAVDKIV DIFENRLKNY 150
    TYLATENISL ADLVAASIFT RYFESLFGTE WRAQHPAIVR WFNTVRASPF 200
    LKDEYKDFKF ADKPLSPPQK KKEKKAPAAA PAASKKKEEA KPAATETETS 250
    SKKPKHPLEL LGKSTFVLDD WKRKYSNEDT RPVALPWFWE HYNPEEYSLW 300
    KVTYKYNDEL TLTFMSNNLV GGFFNRLSAS TKYMFGCLVV YGENNNNGIV 350
    GAVMVRGQDY VPAFDVAPDW ESYDYAKLDP TNDDDKEFIN NMWAWDKPVS 400
    VNGEPKEIVD GKVLK 415
    Length:415
    Mass (Da):47,088
    Last modified:October 1, 1996 - v2
    Checksum:i17BCE60FFB7B2890
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911W → C in AAA16892. (PubMed:8247005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01879 Unassigned DNA. Translation: AAA16892.1.
    X67917 Genomic DNA. Translation: CAA48116.1.
    U44030 Genomic DNA. Translation: AAB68173.1.
    BK006949 Genomic DNA. Translation: DAA11382.1.
    PIRiS29345.
    RefSeqiNP_015277.1. NM_001183862.1.

    Genome annotation databases

    EnsemblFungiiYPL048W; YPL048W; YPL048W.
    GeneIDi856059.
    KEGGisce:YPL048W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01879 Unassigned DNA. Translation: AAA16892.1 .
    X67917 Genomic DNA. Translation: CAA48116.1 .
    U44030 Genomic DNA. Translation: AAB68173.1 .
    BK006949 Genomic DNA. Translation: DAA11382.1 .
    PIRi S29345.
    RefSeqi NP_015277.1. NM_001183862.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NHY X-ray 3.00 A 1-219 [» ]
    ProteinModelPortali P29547.
    SMRi P29547. Positions 1-219, 255-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36132. 53 interactions.
    DIPi DIP-6813N.
    IntActi P29547. 11 interactions.
    MINTi MINT-644858.
    STRINGi 4932.YPL048W.

    Proteomic databases

    MaxQBi P29547.
    PaxDbi P29547.
    PeptideAtlasi P29547.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL048W ; YPL048W ; YPL048W .
    GeneIDi 856059.
    KEGGi sce:YPL048W.

    Organism-specific databases

    CYGDi YPL048w.
    SGDi S000005969. CAM1.

    Phylogenomic databases

    eggNOGi COG0625.
    GeneTreei ENSGT00390000007552.
    HOGENOMi HOG000201196.
    KOi K03233.
    OMAi ENYSIWY.
    OrthoDBi EOG7RBZK2.

    Enzyme and pathway databases

    UniPathwayi UPA00345 .
    BioCyci YEAST:G3O-33961-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P29547.
    NextBioi 981032.

    Gene expression databases

    Genevestigatori P29547.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.30.70.1010. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    IPR001662. Transl_elong_EF1_G_con.
    [Graphical view ]
    Pfami PF00647. EF1G. 1 hit.
    PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    SSF89942. SSF89942. 1 hit.
    PROSITEi PS50040. EF1G_C. 1 hit.
    PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae."
      Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr.
      Mol. Cell. Biol. 13:7901-7912(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and genetic characterization of a calcium- and phospholipid-binding protein from Saccharomyces cerevisiae that is homologous to translation elongation factor-1 gamma."
      Kambouris N.G., Burke D.J., Creutz C.E.
      Yeast 9:151-163(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Calcium-dependent secretory vesicle-binding and lipid-binding proteins of Saccharomyces cerevisiae."
      Creutz C.E., Snyder S.L., Kambouris N.G.
      Yeast 7:229-244(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 357-373.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "A homologue of elongation factor 1 gamma regulates methionine sulfoxide reductase A gene expression in Saccharomyces cerevisiae."
      Hanbauer I., Boja E.S., Moskovitz J.
      Proc. Natl. Acad. Sci. U.S.A. 100:8199-8204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae."
      Jeppesen M.G., Ortiz P.A., Shepard W., Kinzy T.G., Nyborg J., Andersen G.R.
      J. Biol. Chem. 278:47190-47198(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-219, INTERACTION WITH EFB1, PUTATIVE STRUCTURE OF THE EEF1 COMPLEX.

    Entry informationi

    Entry nameiEF1G1_YEAST
    AccessioniPrimary (citable) accession number: P29547
    Secondary accession number(s): D6W3W6, Q9URC6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 60865 molecules/cell in log phase SD medium.1 Publication
    There are 2 isoforms for eEF1Bgamma 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

    External Data

    Dasty 3