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P10081

- IF4A_YEAST

UniProt

P10081 - IF4A_YEAST

Protein

ATP-dependent RNA helicase eIF4A

Gene

TIF1

more
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 174 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.6 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Kineticsi

    1. KM=470 µM for ATP2 Publications

    Vmax=2.6 pmol/sec/µg enzyme for ATP2 Publications

    pH dependencei

    Optimum pH is 6.0.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi66 – 738ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent RNA helicase activity Source: SGD
    3. protein binding Source: IntAct
    4. RNA-dependent ATPase activity Source: SGD
    5. translation initiation factor activity Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. regulation of translational initiation Source: SGD
    3. translational initiation Source: SGD

    Keywords - Molecular functioni

    Helicase, Hydrolase, Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31584-MONOMER.
    YEAST:G3O-32027-MONOMER.
    SABIO-RKP10081.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase eIF4A (EC:3.6.4.13)
    Alternative name(s):
    Eukaryotic initiation factor 4A
    Short name:
    eIF-4A
    Stimulator factor I 37 kDa component
    Translation initiation factor 1/2
    p37
    Gene namesi
    Name:TIF1
    Synonyms:TIF41A
    Ordered Locus Names:YKR059W
    AND
    Name:TIF2
    Synonyms:TIF41B
    Ordered Locus Names:YJL138C
    ORF Names:J0660
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X, UP000002311: Chromosome XI

    Organism-specific databases

    SGDiS000001767. TIF1.
    S000003674. TIF2.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. eukaryotic translation initiation factor 4F complex Source: SGD
    3. ribosome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241F → A: Lethal in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication
    Mutagenesisi42 – 421F → A: Slow growth in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication
    Mutagenesisi46 – 461S → A: Reduces ATP binding and ATPase activity in vitro. 1 Publication
    Mutagenesisi49 – 491Q → A: Reduces ATP binding and ATPase activity in vitro. 1 Publication
    Mutagenesisi49 – 491Q → E: Increases about 3-fold ATP binding but reduces about 2-fold ATPase activity in vitro. 1 Publication
    Mutagenesisi66 – 661A → D: Slow growth. 2 Publications
    Mutagenesisi66 – 661A → V: Lethal and dominant negative if overexpressed in vivo. Impairs ATP hydrolysis, RNA-helicase and translation activity in vitro. 2 Publications
    Mutagenesisi72 – 721K → A: Lethal in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication
    Mutagenesisi79 – 791A → V in TIF1-1; no growth at 36 degrees Celsius. 1 Publication
    Mutagenesisi126 – 1261G → D: Lethal. 1 Publication
    Mutagenesisi127 – 1271G → D: Slow growth. 1 Publication
    Mutagenesisi145 – 1451G → D: Lethal. 1 Publication
    Mutagenesisi145 – 1451G → S: Slow growth. 1 Publication
    Mutagenesisi170 – 1701D → E: Lethal. 1 Publication
    Mutagenesisi173 – 1731D → H: Lethal. 1 Publication
    Mutagenesisi311 – 3111S → F: Slow growth. 1 Publication
    Mutagenesisi347 – 3471R → E, G, I, S or T: Lethal and dominant negative if overexpressed. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 395394ATP-dependent RNA helicase eIF4APRO_0000054968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei73 – 731Phosphothreonine1 Publication
    Modified residuei77 – 771Phosphoserine1 Publication
    Modified residuei129 – 1291Phosphoserine1 Publication
    Modified residuei146 – 1461Phosphothreonine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP10081.
    PaxDbiP10081.

    2D gel databases

    SWISS-2DPAGEP10081.

    Expressioni

    Gene expression databases

    GenevestigatoriP10081.

    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 eIF4G1/TIF4631 and eIF4G2/TIF4632.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TIF4631P399357EBI-9017,EBI-9002

    Protein-protein interaction databases

    BioGridi33619. 156 interactions.
    34190. 123 interactions.
    DIPiDIP-4571N.
    IntActiP10081. 51 interactions.
    MINTiMINT-8285693.
    STRINGi4932.YKR059W.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 175
    Helixi24 – 274
    Helixi31 – 4010
    Helixi47 – 5711
    Beta strandi62 – 654
    Helixi72 – 8312
    Beta strandi93 – 964
    Helixi100 – 11314
    Turni114 – 1163
    Beta strandi121 – 1244
    Helixi130 – 13910
    Beta strandi141 – 1455
    Helixi147 – 1559
    Beta strandi166 – 1705
    Helixi172 – 1776
    Helixi181 – 19010
    Beta strandi196 – 2038
    Helixi206 – 21510
    Beta strandi220 – 2223
    Beta strandi235 – 2439
    Helixi244 – 2463
    Helixi247 – 25711
    Beta strandi263 – 2697
    Helixi270 – 28213
    Beta strandi287 – 2904
    Helixi296 – 30712
    Beta strandi312 – 3176
    Helixi318 – 3203
    Turni321 – 3233
    Beta strandi330 – 3367
    Helixi341 – 3466
    Beta strandi359 – 3657
    Turni366 – 3683
    Helixi369 – 37810
    Turni391 – 3944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FUKX-ray1.75A231-395[»]
    1FUUX-ray2.50A/B2-395[»]
    1QDEX-ray2.00A9-232[»]
    1QVAX-ray2.50A2-224[»]
    2VSOX-ray2.60A/B1-395[»]
    2VSXX-ray2.80A/B1-395[»]
    ProteinModelPortaliP10081.
    SMRiP10081. Positions 12-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10081.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 222170Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini233 – 394162Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi22 – 5029Q motifAdd
    BLAST
    Motifi170 – 1734DEAD box

    Domaini

    The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.1 Publication

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    GeneTreeiENSGT00740000115544.
    HOGENOMiHOG000268797.
    KOiK03257.
    OMAiVMNGNQI.
    OrthoDBiEOG7FNCJ0.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10081-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEGITDIEE SQIQTNYDKV VYKFDDMELD ENLLRGVFGY GFEEPSAIQQ    50
    RAIMPIIEGH DVLAQAQSGT GKTGTFSIAA LQRIDTSVKA PQALMLAPTR 100
    ELALQIQKVV MALAFHMDIK VHACIGGTSF VEDAEGLRDA QIVVGTPGRV 150
    FDNIQRRRFR TDKIKMFILD EADEMLSSGF KEQIYQIFTL LPPTTQVVLL 200
    SATMPNDVLE VTTKFMRNPV RILVKKDELT LEGIKQFYVN VEEEEYKYEC 250
    LTDLYDSISV TQAVIFCNTR RKVEELTTKL RNDKFTVSAI YSDLPQQERD 300
    TIMKEFRSGS SRILISTDLL ARGIDVQQVS LVINYDLPAN KENYIHRIGR 350
    GGRFGRKGVA INFVTNEDVG AMRELEKFYS TQIEELPSDI ATLLN 395
    Length:395
    Mass (Da):44,697
    Last modified:January 23, 2007 - v3
    Checksum:i19D8C133C815DD48
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12813 Genomic DNA. Translation: CAA31301.1.
    X12814 Genomic DNA. Translation: CAA31302.1.
    X58099 Genomic DNA. Translation: CAA41110.1.
    X87371 Genomic DNA. Translation: CAA60817.1.
    Z49413 Genomic DNA. Translation: CAA89433.1.
    U25436 Genomic DNA. Translation: AAA91645.1.
    Z28284 Genomic DNA. Translation: CAA82138.1.
    BK006943 Genomic DNA. Translation: DAA08662.1.
    BK006944 Genomic DNA. Translation: DAA09210.1.
    PIRiS05835. FIBY1.
    RefSeqiNP_012397.1. NM_001181571.1.
    NP_012985.3. NM_001179849.3.

    Genome annotation databases

    EnsemblFungiiYJL138C; YJL138C; YJL138C.
    YKR059W; YKR059W; YKR059W.
    GeneIDi853303.
    853933.
    KEGGisce:YJL138C.
    sce:YKR059W.

    Cross-referencesi

    Web resourcesi

    RNA helicases from the baker's yeast Saccharomyces cerevisiae

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12813 Genomic DNA. Translation: CAA31301.1 .
    X12814 Genomic DNA. Translation: CAA31302.1 .
    X58099 Genomic DNA. Translation: CAA41110.1 .
    X87371 Genomic DNA. Translation: CAA60817.1 .
    Z49413 Genomic DNA. Translation: CAA89433.1 .
    U25436 Genomic DNA. Translation: AAA91645.1 .
    Z28284 Genomic DNA. Translation: CAA82138.1 .
    BK006943 Genomic DNA. Translation: DAA08662.1 .
    BK006944 Genomic DNA. Translation: DAA09210.1 .
    PIRi S05835. FIBY1.
    RefSeqi NP_012397.1. NM_001181571.1.
    NP_012985.3. NM_001179849.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FUK X-ray 1.75 A 231-395 [» ]
    1FUU X-ray 2.50 A/B 2-395 [» ]
    1QDE X-ray 2.00 A 9-232 [» ]
    1QVA X-ray 2.50 A 2-224 [» ]
    2VSO X-ray 2.60 A/B 1-395 [» ]
    2VSX X-ray 2.80 A/B 1-395 [» ]
    ProteinModelPortali P10081.
    SMRi P10081. Positions 12-395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33619. 156 interactions.
    34190. 123 interactions.
    DIPi DIP-4571N.
    IntActi P10081. 51 interactions.
    MINTi MINT-8285693.
    STRINGi 4932.YKR059W.

    2D gel databases

    SWISS-2DPAGE P10081.

    Proteomic databases

    MaxQBi P10081.
    PaxDbi P10081.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL138C ; YJL138C ; YJL138C .
    YKR059W ; YKR059W ; YKR059W .
    GeneIDi 853303.
    853933.
    KEGGi sce:YJL138C.
    sce:YKR059W.

    Organism-specific databases

    SGDi S000001767. TIF1.
    S000003674. TIF2.

    Phylogenomic databases

    eggNOGi COG0513.
    GeneTreei ENSGT00740000115544.
    HOGENOMi HOG000268797.
    KOi K03257.
    OMAi VMNGNQI.
    OrthoDBi EOG7FNCJ0.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31584-MONOMER.
    YEAST:G3O-32027-MONOMER.
    SABIO-RK P10081.

    Miscellaneous databases

    EvolutionaryTracei P10081.
    NextBioi 973627.

    Gene expression databases

    Genevestigatori P10081.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the genes TIF1 and TIF2 from Saccharomyces cerevisiae coding for a translation initiation factor."
      Linder P., Slonimski P.P.
      Nucleic Acids Res. 16:10359-10359(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF1 AND TIF2).
      Strain: CD11/B1830/50.
    2. "An essential yeast protein, encoded by duplicated genes TIF1 and TIF2 and homologous to the mammalian translation initiation factor eIF-4A, can suppress a mitochondrial missense mutation."
      Linder P., Slonimski P.P.
      Proc. Natl. Acad. Sci. U.S.A. 86:2286-2290(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF1 AND TIF2).
      Strain: CD11/B1830/50.
    3. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TIF1).
      Strain: ATCC 204508 / S288c.
    4. "Sequence analysis of a 40.7 kb segment from the left arm of yeast chromosome X reveals 14 known genes and 13 new open reading frames including homologues of genes clustered on the right arm of chromosome XI."
      Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.
      Yeast 12:787-797(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF2).
      Strain: ATCC 96604 / S288c / FY1679.
    5. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TIF2).
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION (TIF1 AND TIF2).
      Strain: ATCC 204508 / S288c.
    7. "Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p for glycogen accumulation in Saccharomyces cerevisiae."
      Cheng C., Mu J., Farkas I., Huang D., Goebl M.G., Roach P.J.
      Mol. Cell. Biol. 15:6632-6640(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93 (TIF2).
    8. "The Saccharomyces cerevisiae RPB4 gene is tightly linked to the TIF2 gene."
      Foreman P.K., Davis R.W., Sachs A.B.
      Nucleic Acids Res. 19:2781-2781(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-395 (TIF2).
    9. "The 66 kDa component of yeast SFI, stimulatory factor I, is hsp60."
      Smiley J.K., Brown W.C., Campbell J.L.
      Nucleic Acids Res. 20:4913-4918(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 332-340; 342-347 AND 378-391.
    10. "Translation in Saccharomyces cerevisiae: initiation factor 4A-dependent cell-free system."
      Blum S., Mueller M., Schmid S.R., Linder P., Trachsel H.
      Proc. Natl. Acad. Sci. U.S.A. 86:6043-6046(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Translation initiation factor-dependent extracts from Saccharomyces cerevisiae."
      Altmann M., Blum S., Pelletier J., Sonenberg N., Wilson T.M., Trachsel H.
      Biochim. Biophys. Acta 1050:155-159(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Translation initiation factor 4A from Saccharomyces cerevisiae: analysis of residues conserved in the D-E-A-D family of RNA helicases."
      Schmid S.R., Linder P.
      Mol. Cell. Biol. 11:3463-3471(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF ALA-66; ALA-79; GLY-126; GLY-127; GLY-145; ASP-170; ASP-173; SER-311 AND ARG-347.
    13. "ATP hydrolysis by initiation factor 4A is required for translation initiation in Saccharomyces cerevisiae."
      Blum S., Schmid S.R., Pause A., Buser P., Linder P., Sonenberg N., Trachsel H.
      Proc. Natl. Acad. Sci. U.S.A. 89:7664-7668(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-66.
    14. "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 SER-2.
    15. "Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally."
      Neff C.L., Sachs A.B.
      Mol. Cell. Biol. 19:5557-5564(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TIF4631 AND TIF4632.
    16. "Interaction of translation initiation factor eIF4G with eIF4A in the yeast Saccharomyces cerevisiae."
      Dominguez D., Altmann M., Benz J., Baumann U., Trachsel H.
      J. Biol. Chem. 274:26720-26726(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TIF4631.
    17. "The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis."
      Tanner N.K., Cordin O., Banroques J., Doere M., Linder P.
      Mol. Cell 11:127-138(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-24; PHE-42; SER-46; GLN-49 AND LYS-72.
    18. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    19. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    20. "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-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    21. "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-129 AND THR-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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 THR-73; SER-77 AND THR-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase."
      Johnson E.R., McKay D.B.
      RNA 5:1526-1534(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-225.
    25. "Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae -- the prototype of the DEAD box protein family."
      Benz J., Trachsel H., Baumann U.
      Structure 7:671-679(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 10-233.
    26. "Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase."
      Caruthers J.M., Johnson E.R., McKay D.B.
      Proc. Natl. Acad. Sci. U.S.A. 97:13080-13085(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 231-395.

    Entry informationi

    Entry nameiIF4A_YEAST
    AccessioniPrimary (citable) accession number: P10081
    Secondary accession number(s): D6VW46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 174 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    TIF1 and TIF2 code for the same protein.
    Present with 106000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Translation initiation factors
      List of translation initiation factor entries
    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 X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
    6. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3