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P39935

- IF4F1_YEAST

UniProt

P39935 - IF4F1_YEAST

Protein

Eukaryotic initiation factor 4F subunit p150

Gene

TIF4631

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 145 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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. TIF4631 is probably essential when TIF4632 is missing.2 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. regulation of translation Source: UniProtKB-KW
    2. ribosomal large subunit biogenesis Source: SGD
    3. stress granule assembly Source: SGD
    4. 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-30861-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic initiation factor 4F subunit p150
    Short name:
    eIF-4F p150
    Short name:
    eIF4F p150
    Alternative name(s):
    eIF4G1
    mRNA cap-binding protein complex subunit p150
    Gene namesi
    Name:TIF4631
    Ordered Locus Names:YGR162W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR162w.
    SGDiS000003394. TIF4631.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi214 – 2174KLRK → AAAA in TIF4631-213; abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 952952Eukaryotic initiation factor 4F subunit p150PRO_0000213331Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811Phosphothreonine1 Publication
    Modified residuei883 – 8831Phosphoserine1 Publication
    Modified residuei888 – 8881Phosphothreonine1 Publication
    Modified residuei908 – 9081Phosphoserine1 Publication
    Modified residuei948 – 9481Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP39935.
    PaxDbiP39935.
    PeptideAtlasiP39935.

    Expressioni

    Gene expression databases

    GenevestigatoriP39935.

    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
    CDC33P0726015EBI-9002,EBI-150
    PAB1P0414716EBI-9002,EBI-12823
    TIF2P100817EBI-9002,EBI-9017

    Protein-protein interaction databases

    BioGridi33414. 143 interactions.
    DIPiDIP-985N.
    IntActiP39935. 62 interactions.
    MINTiMINT-617040.
    STRINGi4932.YGR162W.

    Structurei

    Secondary structure

    1
    952
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi411 – 4199
    Helixi427 – 4293
    Helixi443 – 4453
    Helixi454 – 46411
    Helixi471 – 4766
    Helixi603 – 61513
    Beta strandi619 – 6213
    Helixi622 – 63413
    Helixi635 – 6384
    Helixi643 – 65816
    Helixi660 – 6623
    Helixi663 – 67614
    Helixi692 – 70918
    Helixi733 – 75523
    Helixi761 – 77616
    Helixi781 – 79818
    Helixi812 – 82716
    Helixi834 – 84815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RF8NMR-B391-488[»]
    2VSOX-ray2.60E/F572-854[»]
    2VSXX-ray2.80E/F572-854[»]
    DisProtiDP00082.
    ProteinModelPortaliP39935.
    SMRiP39935. Positions 391-488, 577-853.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39935.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini607 – 850244MIF4GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni188 – 299112Interaction with PAB1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi173 – 20028Pro/Ser/Thr-richAdd
    BLAST
    Compositional biasi375 – 38410Ala/Glu-rich
    Compositional biasi488 – 55366Arg/Ser-richAdd
    BLAST
    Compositional biasi869 – 8724Poly-Glu
    Compositional biasi873 – 89927Arg/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MIF4G domain.Curated

    Phylogenomic databases

    eggNOGiNOG301289.
    GeneTreeiENSGT00530000063038.
    HOGENOMiHOG000065985.
    KOiK03260.
    OMAiEQFETDS.
    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.

    P39935-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDETAHPTQ SASKQESAAL KQTGDDQQES QQQRGYTNYN NGSNYTQKKP    50
    YNSNRPHQQR GGKFGPNRYN NRGNYNGGGS FRGGHMGANS SNVPWTGYYN 100
    NYPVYYQPQQ MAAAGSAPAN PIPVEEKSPV PTKIEITTKS GEHLDLKEQH 150
    KAKLQSQERS TVSPQPESKL KETSDSTSTS TPTPTPSTND SKASSEENIS 200
    EAEKTRRNFI EQVKLRKAAL EKKRKEQLEG SSGNNNIPMK TTPENVEEKG 250
    SDKPEVTEKT KPAEEKSAEP EVKQETPAEE GEQGEKGQIK EESTPKVLTF 300
    AERLKLKKQQ KEREEKTEGK ENKEVPVQEE TKSAIESAPV PPSEQVKEET 350
    EVAETEQSNI DESATTPAIP TKSDEAEAEV EAEAGDAGTK IGLEAEIETT 400
    TDETDDGTNT VSHILNVLKD ATPIEDVFSF NYPEGIEGPD IKYKKEHVKY 450
    TYGPTFLLQF KDKLNVKADA EWVQSTASKI VIPPGMGRGN RSRDSGRFGN 500
    NSSRGHDFRN TSVRNMDDRA NSRTSSKRRS KRMNDDRRSN RSYTSRRDRE 550
    RGSYRNEEKR EDDKPKEEVA PLVPSANRWV PKFKSKKTEK KLAPDGKTEL 600
    LDKDEVERKM KSLLNKLTLE MFDAISSEIL AIANISVWET NGETLKAVIE 650
    QIFLKACDEP HWSSMYAQLC GKVVKELNPD ITDETNEGKT GPKLVLHYLV 700
    ARCHAEFDKG WTDKLPTNED GTPLEPEMMS EEYYAAASAK RRGLGLVRFI 750
    GFLYRLNLLT GKMMFECFRR LMKDLTDSPS EETLESVVEL LNTVGEQFET 800
    DSFRTGQATL EGSQLLDSLF GILDNIIQTA KISSRIKFKL IDIKELRHDK 850
    NWNSDKKDNG PKTIQQIHEE EERQRQLKNN SRSNSRRTNN SSNRHSFRRD 900
    APPASKDSFI TTRTYSQRNS QRAPPPKEEP AAPTSTATNM FSALMGESDD 950
    EE 952
    Length:952
    Mass (Da):107,101
    Last modified:October 1, 1996 - v2
    Checksum:i391256802F86118E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71H → Q in AAA02757. (PubMed:8336723)Curated
    Sequence conflicti37 – 371T → N in AAA02757. (PubMed:8336723)Curated
    Sequence conflicti110 – 1101Q → K in AAA02757. (PubMed:8336723)Curated
    Sequence conflicti207 – 2071R → K in AAA02757. (PubMed:8336723)Curated
    Sequence conflicti361 – 3611D → E in AAA02757. (PubMed:8336723)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16923 Genomic DNA. Translation: AAA02757.1.
    Z72947 Genomic DNA. Translation: CAA97184.1.
    AY692973 Genomic DNA. Translation: AAT92992.1.
    BK006941 Genomic DNA. Translation: DAA08257.1.
    PIRiS64473.
    RefSeqiNP_011678.3. NM_001181291.3.

    Genome annotation databases

    EnsemblFungiiYGR162W; YGR162W; YGR162W.
    GeneIDi853071.
    KEGGisce:YGR162W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16923 Genomic DNA. Translation: AAA02757.1 .
    Z72947 Genomic DNA. Translation: CAA97184.1 .
    AY692973 Genomic DNA. Translation: AAT92992.1 .
    BK006941 Genomic DNA. Translation: DAA08257.1 .
    PIRi S64473.
    RefSeqi NP_011678.3. NM_001181291.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RF8 NMR - B 391-488 [» ]
    2VSO X-ray 2.60 E/F 572-854 [» ]
    2VSX X-ray 2.80 E/F 572-854 [» ]
    DisProti DP00082.
    ProteinModelPortali P39935.
    SMRi P39935. Positions 391-488, 577-853.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33414. 143 interactions.
    DIPi DIP-985N.
    IntActi P39935. 62 interactions.
    MINTi MINT-617040.
    STRINGi 4932.YGR162W.

    Proteomic databases

    MaxQBi P39935.
    PaxDbi P39935.
    PeptideAtlasi P39935.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR162W ; YGR162W ; YGR162W .
    GeneIDi 853071.
    KEGGi sce:YGR162W.

    Organism-specific databases

    CYGDi YGR162w.
    SGDi S000003394. TIF4631.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30861-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P39935.
    NextBioi 973024.

    Gene expression databases

    Genevestigatori P39935.

    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. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
      Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
      Yeast 13:1077-1090(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    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 214-LYS--LYS-217.
    7. "Circularization of mRNA by eukaryotic translation initiation factors."
      Wells S.E., Hillner P.E., Vale R.D., Sachs A.B.
      Mol. Cell 2:135-140(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAB1, ATOMIC FORCE MICROSCOPY OF CIRCULAR MRNP STRUCTURE.
    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. "The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex."
      Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.
      EMBO J. 19:4372-4382(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAB1.
    10. "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.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "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-181 AND SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    14. "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-883 AND THR-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-908 AND SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E."
      Gross J.D., Moerke N.J., von der Haar T., Lugovskoy A.A., Sachs A.B., McCarthy J.E.G., Wagner G.
      Cell 115:739-750(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 389-488.

    Entry informationi

    Entry nameiIF4F1_YEAST
    AccessioniPrimary (citable) accession number: P39935
    Secondary accession number(s): D6VUU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 145 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 9760 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3