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P32501

- EI2BE_YEAST

UniProt

P32501 - EI2BE_YEAST

Protein

Translation initiation factor eIF-2B subunit epsilon

Gene

GCD6

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 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Acts as a catalytic component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD6 and GCD7 repress GCN4 expression at the translational level by ensuring that ribosomes which have translated UORF1 will reinitiate at UORF2, -3, or -4 and thus fail to reach the GCN4 start site.2 Publications

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: SGD
    2. nucleotidyltransferase activity Source: InterPro
    3. translation initiation factor activity Source: SGD

    GO - Biological processi

    1. positive regulation of GTPase activity Source: GOC
    2. regulation of translational initiation Source: SGD

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis, Translation regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29793-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Translation initiation factor eIF-2B subunit epsilon
    Alternative name(s):
    GCD complex subunit GCD6
    Guanine nucleotide exchange factor subunit GCD6
    eIF-2B GDP-GTP exchange factor subunit epsilon
    Gene namesi
    Name:GCD6
    Synonyms:TIF225
    Ordered Locus Names:YDR211W
    ORF Names:YD8142.12, YD8142B.03
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR211w.
    SGDiS000002619. GCD6.

    Subcellular locationi

    GO - Cellular componenti

    1. eukaryotic translation initiation factor 2B complex Source: SGD
    2. guanyl-nucleotide exchange factor complex Source: SGD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi552 – 5521T → I: Reduced exchange activity. 2 Publications
    Mutagenesisi569 – 5691E → A: Lethal. 2 Publications
    Mutagenesisi576 – 5761S → N: Reduced exchange activity. 2 Publications
    Mutagenesisi655 – 67723LFSAL…IYKWW → AFSAAVSAADNDAAEAAVAA KWA: Abolishes binding to SUI3. 1 PublicationAdd
    BLAST
    Mutagenesisi696 – 70611WVEWLQNADEE → AAEAAQNAAAA: Abolishes binding to SUI3; probably impairs the conversion of eIF-2-GDP to eIF-2-GTP. 1 PublicationAdd
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 712712Translation initiation factor eIF-2B subunit epsilonPRO_0000156078Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei478 – 4781Phosphoserine2 Publications
    Modified residuei481 – 4811Phosphoserine2 Publications
    Modified residuei507 – 5071Phosphoserine1 Publication
    Modified residuei525 – 5251Phosphoserine1 Publication
    Modified residuei538 – 5381Phosphoserine2 Publications
    Modified residuei707 – 7071Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32501.
    PaxDbiP32501.
    PeptideAtlasiP32501.

    Expressioni

    Gene expression databases

    GenevestigatoriP32501.

    Interactioni

    Subunit structurei

    Translation initiation factor 2B (eIF2-B) is composed of five different subunits; alpha (GCN3), beta (GCD7), gamma (GCD1), delta (GCD2) and epsilon (GCD6). A catalytic subcomplex comprising GCD1 and GCD6 interacts with both, phosphorylated and non-phosphorylated eIF-2 and has exchange activity in vitro. GCD6 interacts with SUI3.3 Publications

    Protein-protein interaction databases

    BioGridi32265. 47 interactions.
    DIPiDIP-2328N.
    IntActiP32501. 29 interactions.
    MINTiMINT-527627.
    STRINGi4932.YDR211W.

    Structurei

    Secondary structure

    1
    712
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi545 – 55814
    Helixi563 – 57614
    Helixi581 – 60121
    Helixi607 – 61812
    Helixi619 – 6246
    Helixi629 – 64618
    Helixi651 – 66414
    Helixi670 – 6789
    Helixi684 – 6863
    Helixi687 – 70216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PAQX-ray2.30A524-712[»]
    ProteinModelPortaliP32501.
    SMRiP32501. Positions 36-149, 324-433, 544-704.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32501.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini539 – 710172W2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 W2 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1208.
    GeneTreeiENSGT00510000047568.
    HOGENOMiHOG000216610.
    KOiK03240.
    OMAiEGKGYIW.
    OrthoDBiEOG7NSBB4.

    Family and domain databases

    Gene3Di1.25.40.180. 1 hit.
    3.90.550.10. 1 hit.
    InterProiIPR016024. ARM-type_fold.
    IPR001451. Hexapep_transf.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR005835. NTP_transferase.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR011004. Trimer_LpxA-like.
    IPR003307. W2_domain.
    [Graphical view]
    PfamiPF00132. Hexapep. 2 hits.
    PF00483. NTP_transferase. 1 hit.
    PF02020. W2. 1 hit.
    [Graphical view]
    SMARTiSM00515. eIF5C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    SSF51161. SSF51161. 1 hit.
    SSF53448. SSF53448. 2 hits.
    PROSITEiPS51363. W2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32501-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGKKGQKKS GLGNHGKNSD MDVEDRLQAV VLTDSYETRF MPLTAVKPRC    50
    LLPLANVPLI EYTLEFLAKA GVHEVFLICS SHANQINDYI ENSKWNLPWS 100
    PFKITTIMSP EARCTGDVMR DLDNRGIITG DFILVSGDVL TNIDFSKMLE 150
    FHKKMHLQDK DHISTMCLSK ASTYPKTRTI EPAAFVLDKS TSRCIYYQDL 200
    PLPSSREKTS IQIDPELLDN VDEFVIRNDL IDCRIDICTS HVPLIFQENF 250
    DYQSLRTDFV KGVISSDILG KHIYAYLTDE YAVRVESWQT YDTISQDFLG 300
    RWCYPLVLDS NIQDDQTYSY ESRHIYKEKD VVLAQSCKIG KCTAIGSGTK 350
    IGEGTKIENS VIGRNCQIGE NIRIKNSFIW DDCIIGNNSI IDHSLIASNA 400
    TLGSNVRLND GCIIGFNVKI DDNMDLDRNT KISASPLKNA GSRMYDNESN 450
    EQFDQDLDDQ TLAVSIVGDK GVGYIYESEV SDDEDSSTEA CKEINTLSNQ 500
    LDELYLSDDS ISSATKKTKK RRTMSVNSIY TDREEIDSEF EDEDFEKEGI 550
    ATVERAMENN HDLDTALLEL NTLRMSMNVT YHEVRIATIT ALLRRVYHFI 600
    ATQTLGPKDA VVKVFNQWGL LFKRQAFDEE EYIDLMNIIM EKIVEQSFDK 650
    PDLILFSALV SLYDNDIIEE DVIYKWWDNV STDPRYDEVK KLTVKWVEWL 700
    QNADEESSSE EE 712
    Length:712
    Mass (Da):81,161
    Last modified:October 1, 1993 - v1
    Checksum:iEFE87F6AE2941619
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07115 Genomic DNA. Translation: AAA65498.1.
    Z68194 Genomic DNA. Translation: CAA92354.1.
    Z68195 Genomic DNA. Translation: CAA92362.1.
    BK006938 Genomic DNA. Translation: DAA12055.1.
    PIRiA48156.
    RefSeqiNP_010497.3. NM_001180519.3.

    Genome annotation databases

    EnsemblFungiiYDR211W; YDR211W; YDR211W.
    GeneIDi851797.
    KEGGisce:YDR211W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07115 Genomic DNA. Translation: AAA65498.1 .
    Z68194 Genomic DNA. Translation: CAA92354.1 .
    Z68195 Genomic DNA. Translation: CAA92362.1 .
    BK006938 Genomic DNA. Translation: DAA12055.1 .
    PIRi A48156.
    RefSeqi NP_010497.3. NM_001180519.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PAQ X-ray 2.30 A 524-712 [» ]
    ProteinModelPortali P32501.
    SMRi P32501. Positions 36-149, 324-433, 544-704.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32265. 47 interactions.
    DIPi DIP-2328N.
    IntActi P32501. 29 interactions.
    MINTi MINT-527627.
    STRINGi 4932.YDR211W.

    Proteomic databases

    MaxQBi P32501.
    PaxDbi P32501.
    PeptideAtlasi P32501.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR211W ; YDR211W ; YDR211W .
    GeneIDi 851797.
    KEGGi sce:YDR211W.

    Organism-specific databases

    CYGDi YDR211w.
    SGDi S000002619. GCD6.

    Phylogenomic databases

    eggNOGi COG1208.
    GeneTreei ENSGT00510000047568.
    HOGENOMi HOG000216610.
    KOi K03240.
    OMAi EGKGYIW.
    OrthoDBi EOG7NSBB4.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29793-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32501.
    NextBioi 969629.
    PROi P32501.

    Gene expression databases

    Genevestigatori P32501.

    Family and domain databases

    Gene3Di 1.25.40.180. 1 hit.
    3.90.550.10. 1 hit.
    InterProi IPR016024. ARM-type_fold.
    IPR001451. Hexapep_transf.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR005835. NTP_transferase.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR011004. Trimer_LpxA-like.
    IPR003307. W2_domain.
    [Graphical view ]
    Pfami PF00132. Hexapep. 2 hits.
    PF00483. NTP_transferase. 1 hit.
    PF02020. W2. 1 hit.
    [Graphical view ]
    SMARTi SM00515. eIF5C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    SSF51161. SSF51161. 1 hit.
    SSF53448. SSF53448. 2 hits.
    PROSITEi PS51363. W2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae."
      Bushman J.L., Asuru A.I., Matts R.L., Hinnebusch A.G.
      Mol. Cell. Biol. 13:1920-1932(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast."
      Cigan A.M., Bushman J.L., Boal T.R., Hinnebusch A.G.
      Proc. Natl. Acad. Sci. U.S.A. 90:5350-5354(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EIF2-B COMPLEX, FUNCTION OF THE EIF2-B COMPLEX.
    5. "eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange."
      Pavitt G.D., Ramaiah K.V., Kimball S.R., Hinnebusch A.G.
      Genes Dev. 12:514-526(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A EIF2-B SUBCOMPLEX.
    6. "Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2."
      Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.
      EMBO J. 18:1673-1688(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUI3, MUTAGENESIS OF 655-THR--TRP-677 AND 696-TRP--GLU-706.
    7. "Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation."
      Gomez E., Pavitt G.D.
      Mol. Cell. Biol. 20:3965-3976(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-552 AND SER-576.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "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-478; SER-481 AND SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "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-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-478; SER-481; SER-525; SER-538 AND SER-707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue."
      Boesen T., Mohammad S.S., Pavitt G.D., Andersen G.R.
      J. Biol. Chem. 279:10584-10592(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 524-712, MUTAGENESIS OF GLU-569.

    Entry informationi

    Entry nameiEI2BE_YEAST
    AccessioniPrimary (citable) accession number: P32501
    Secondary accession number(s): D6VSJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 139 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 33800 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3