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P39936

- IF4F2_YEAST

UniProt

P39936 - IF4F2_YEAST

Protein

Eukaryotic initiation factor 4F subunit p130

Gene

TIF4632

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 126 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Component of the eIF4F complex, which interacts with the mRNA cap structure and serves as an initial point of assembly for the translation apparatus. Stimulates translation by interaction with polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. TIF4632 is probably essential when TIF4631 is missing.2 Publications

    GO - Molecular functioni

    1. mRNA binding Source: SGD
    2. protein binding Source: IntAct
    3. translation initiation factor activity Source: SGD
    4. translation initiation factor binding Source: SGD

    GO - Biological processi

    1. regulation of translation Source: UniProtKB-KW
    2. stress granule assembly Source: SGD
    3. translational initiation Source: SGD

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis, Translation regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30559-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic initiation factor 4F subunit p130
    Short name:
    eIF-4F p130
    Short name:
    eIF4F p130
    Alternative name(s):
    eIF4G2
    mRNA cap-binding protein complex subunit p130
    Gene namesi
    Name:TIF4632
    Ordered Locus Names:YGL049C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL049c.
    SGDiS000003017. TIF4632.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: SGD
    2. cytoplasmic stress granule Source: SGD
    3. eukaryotic translation initiation factor 4F complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi233 – 2364RLRK → AVAA in TIF4632-233; abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 914914Eukaryotic initiation factor 4F subunit p130PRO_0000213332Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741Phosphoserine1 Publication
    Modified residuei196 – 1961Phosphothreonine2 Publications
    Modified residuei301 – 3011Phosphothreonine1 Publication
    Modified residuei503 – 5031Phosphoserine1 Publication
    Modified residuei913 – 9131Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP39936.
    PaxDbiP39936.
    PeptideAtlasiP39936.

    Expressioni

    Gene expression databases

    GenevestigatoriP39936.

    Interactioni

    Subunit structurei

    Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) By similarity. Interacts with PAT1 in a RNA-dependent manner.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PAB1P041472EBI-9006,EBI-12823
    PUB1P325883EBI-9006,EBI-14231

    Protein-protein interaction databases

    BioGridi33199. 71 interactions.
    DIPiDIP-330N.
    IntActiP39936. 28 interactions.
    MINTiMINT-424681.
    STRINGi4932.YGL049C.

    Structurei

    3D structure databases

    ProteinModelPortaliP39936.
    SMRiP39936. Positions 382-459, 537-813.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini567 – 810244MIF4GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni201 – 315115Interaction with PAB1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi32 – 9766Asn-richAdd
    BLAST
    Compositional biasi459 – 51052Arg/Ser-richAdd
    BLAST
    Compositional biasi840 – 86324Arg/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MIF4G domain.Curated

    Phylogenomic databases

    eggNOGiNOG301289.
    GeneTreeiENSGT00530000063038.
    HOGENOMiHOG000065985.
    KOiK03260.
    OMAiNIPPRTH.
    OrthoDBiEOG7VTDWG.

    Family and domain databases

    Gene3Di1.25.40.180. 1 hit.
    InterProiIPR016024. ARM-type_fold.
    IPR022745. eIF4G1_eIF4E-bd.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR003890. MIF4G-like_typ-3.
    [Graphical view]
    PfamiPF12152. eIF_4G1. 1 hit.
    PF02854. MIF4G. 1 hit.
    [Graphical view]
    SMARTiSM00543. MIF4G. 1 hit.
    [Graphical view]
    SUPFAMiSSF101489. SSF101489. 1 hit.
    SSF48371. SSF48371. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P39936-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDQRGPPPP HPQQANGYKK FPPHDNQYSG ANNSQPNNHY NENLYSAREP    50
    HNNKQYQSKN GKYGTNKYNN RNNSQGNAQY YNNRFNNGYR LNNNDYNPAM 100
    LPGMQWPANY YAPQMYYIPQ QMVPVASPPY THQPLNTNPE PPSTPKTTKI 150
    EITTKTGERL NLKKFHEEKK ASKGEEKNDG VEQKSKSGTP FEKEATPVLP 200
    ANEAVKDTLT ETSNEKSTSE AENTKRLFLE QVRLRKAAME RKKNGLISET 250
    EKKQETSNHD NTDTTKPNSV IESEPIKEAP KPTGEANEVV IDGKSGASVK 300
    TPQHVTGSVT KSVTFNEPEN ESSSQDVDEL VKDDDTTEIS DTTGGKTVNK 350
    SDDETINSVI TTEENTVKET EPSTSDIEMP TVSQLLETLG KAQPISDIYE 400
    FAYPENVERP DIKYKKPSVK YTYGPTFLLQ FKDKLKFRPD PAWVEAVSSK 450
    IVIPPHIARN KPKDSGRFGG DFRSPSMRGM DHTSSSRVSS KRRSKRMGDD 500
    RRSNRGYTSR KDREKAAEKA EEQAPKEEIA PLVPSANRWI PKSRVKKTEK 550
    KLAPDGKTEL FDKEEVERKM KSLLNKLTLE MFDSISSEIL DIANQSKWED 600
    DGETLKIVIE QIFHKACDEP HWSSMYAQLC GKVVKDLDPN IKDKENEGKN 650
    GPKLVLHYLV ARCHEEFEKG WADKLPAGED GNPLEPEMMS DEYYIAAAAK 700
    RRGLGLVRFI GYLYCLNLLT GKMMFECFRR LMKDLNNDPS EETLESVIEL 750
    LNTVGEQFEH DKFVTPQATL EGSVLLDNLF MLLQHIIDGG TISNRIKFKL 800
    IDVKELREIK HWNSAKKDAG PKTIQQIHQE EEQLRQKKNS QRSNSRFNNH 850
    NQSNSNRYSS NRRNMQNTQR DSFASTKTGS FRNNQRNARK VEEVSQAPRA 900
    NMFDALMNND GDSD 914
    Length:914
    Mass (Da):103,899
    Last modified:February 1, 1995 - v1
    Checksum:iBF5E9805CD47908E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16924 Unassigned DNA. Translation: AAA18474.1.
    Z72571 Genomic DNA. Translation: CAA96751.1.
    BK006941 Genomic DNA. Translation: DAA08052.1.
    PIRiB48086.
    RefSeqiNP_011466.1. NM_001180914.1.

    Genome annotation databases

    EnsemblFungiiYGL049C; YGL049C; YGL049C.
    GeneIDi852833.
    KEGGisce:YGL049C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16924 Unassigned DNA. Translation: AAA18474.1 .
    Z72571 Genomic DNA. Translation: CAA96751.1 .
    BK006941 Genomic DNA. Translation: DAA08052.1 .
    PIRi B48086.
    RefSeqi NP_011466.1. NM_001180914.1.

    3D structure databases

    ProteinModelPortali P39936.
    SMRi P39936. Positions 382-459, 537-813.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33199. 71 interactions.
    DIPi DIP-330N.
    IntActi P39936. 28 interactions.
    MINTi MINT-424681.
    STRINGi 4932.YGL049C.

    Proteomic databases

    MaxQBi P39936.
    PaxDbi P39936.
    PeptideAtlasi P39936.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL049C ; YGL049C ; YGL049C .
    GeneIDi 852833.
    KEGGi sce:YGL049C.

    Organism-specific databases

    CYGDi YGL049c.
    SGDi S000003017. TIF4632.

    Phylogenomic databases

    eggNOGi NOG301289.
    GeneTreei ENSGT00530000063038.
    HOGENOMi HOG000065985.
    KOi K03260.
    OMAi NIPPRTH.
    OrthoDBi EOG7VTDWG.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30559-MONOMER.

    Miscellaneous databases

    NextBioi 972400.

    Gene expression databases

    Genevestigatori P39936.

    Family and domain databases

    Gene3Di 1.25.40.180. 1 hit.
    InterProi IPR016024. ARM-type_fold.
    IPR022745. eIF4G1_eIF4E-bd.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR003890. MIF4G-like_typ-3.
    [Graphical view ]
    Pfami PF12152. eIF_4G1. 1 hit.
    PF02854. MIF4G. 1 hit.
    [Graphical view ]
    SMARTi SM00543. MIF4G. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101489. SSF101489. 1 hit.
    SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function."
      Goyer C., Altmann M., Lee H.S., Blanc A., Deshmukh M., Woolford J.L. Jr., Trachsel H., Sonenberg N.
      Mol. Cell. Biol. 13:4860-4874(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
      Feuermann M., de Montigny J., Potier S., Souciet J.-L.
      Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(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. "Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G."
      Tarun S.Z. Jr., Sachs A.B.
      EMBO J. 15:7168-7177(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAB1.
    6. "Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation."
      Tarun S.Z. Jr., Wells S.E., Deardorff J.A., Sachs A.B.
      Proc. Natl. Acad. Sci. U.S.A. 94:9046-9051(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PAB1, MUTAGENESIS OF 233-ARG--LYS-236.
    7. "RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G."
      Kessler S.H., Sachs A.B.
      Mol. Cell. Biol. 18:51-57(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAB1.
    8. "The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms."
      Otero L.J., Ashe M.P., Sachs A.B.
      EMBO J. 18:3153-3163(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PAB1.
    9. "Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs."
      Tharun S., Parker R.
      Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAT1.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    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 THR-301 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-74; THR-196 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIF4F2_YEAST
    AccessioniPrimary (citable) accession number: P39936
    Secondary accession number(s): D6VU91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 126 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 3390 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3