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Q8BGD9

- IF4B_MOUSE

UniProt

Q8BGD9 - IF4B_MOUSE

Protein

Eukaryotic translation initiation factor 4B

Gene

Eif4b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F By similarity.By similarity

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. translation initiation factor activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 4B
    Short name:
    eIF-4B
    Gene namesi
    Name:Eif4b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:95304. Eif4b.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 611611Eukaryotic translation initiation factor 4BPRO_0000081617Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei93 – 931Phosphoserine1 Publication
    Modified residuei192 – 1921PhosphoserineBy similarity
    Modified residuei219 – 2191PhosphoserineBy similarity
    Modified residuei283 – 2831PhosphoserineBy similarity
    Modified residuei365 – 3651N6-acetyllysine1 Publication
    Modified residuei406 – 4061Phosphoserine1 Publication
    Modified residuei412 – 4121PhosphothreonineBy similarity
    Modified residuei418 – 4181PhosphoserineBy similarity
    Modified residuei422 – 4221Phosphoserine; by RPS6KA1 and RPS6KB1By similarity
    Modified residuei425 – 4251PhosphoserineBy similarity
    Modified residuei445 – 4451PhosphoserineBy similarity
    Modified residuei459 – 4591PhosphoserineBy similarity
    Modified residuei498 – 4981Phosphoserine1 Publication
    Modified residuei504 – 5041PhosphoserineBy similarity
    Modified residuei586 – 5861N6-acetyllysineBy similarity
    Modified residuei597 – 5971Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1; phosphorylation enhances the affinity of EIF4B for the EIF3 complex.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8BGD9.
    PaxDbiQ8BGD9.
    PRIDEiQ8BGD9.

    PTM databases

    PhosphoSiteiQ8BGD9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BGD9.
    BgeeiQ8BGD9.
    CleanExiMM_EIF4B.
    GenevestigatoriQ8BGD9.

    Interactioni

    Subunit structurei

    Self-associates and interacts with EIF3 p170 subunit.By similarity

    Protein-protein interaction databases

    BioGridi217684. 3 interactions.
    IntActiQ8BGD9. 2 interactions.
    MINTiMINT-1954873.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BGD9.
    SMRiQ8BGD9. Positions 96-176.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini96 – 17378RRMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi164 – 440277Arg-richAdd
    BLAST
    Compositional biasi169 – 325157Asp-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG238591.
    GeneTreeiENSGT00530000063406.
    HOGENOMiHOG000006553.
    HOVERGENiHBG006129.
    InParanoidiQ8BGD9.
    KOiK03258.
    OMAiSYRDGPR.
    OrthoDBiEOG7MKW86.
    PhylomeDBiQ8BGD9.
    TreeFamiTF101525.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BGD9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVPKPVSW ADETDDLEGD    50
    VSTTWHSNDD DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL 100
    GNLPYDVTED SIKDFFRGLN ISAVRLPREP SNPDRLKGFG YAEFEDLDSL 150
    LSALSLNEES LGNRRIRVDV ADQAQDKDRD DRSFGRDRNR DSDKTDTDWR 200
    ARPTTDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG YRDGPRRDMD 250
    RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED 300
    RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPRLNLKPRS APKEDDASAS 350
    TSQSSRAASI FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLDRRP 400
    RERHPSWRSE ETQERERSRT GSESSQTGAS ATSGRNTRRR ESEKSLENET 450
    LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK ENAWVKRSSN PPARSQSSDT 500
    EQPSPTSGGG KVAAVQPPEE GPSRKDGNKV DVVGATQGQA GSCSRGPGDG 550
    GSRDHWKDLD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG 600
    EDEDEGDDCT E 611
    Length:611
    Mass (Da):68,840
    Last modified:March 1, 2003 - v1
    Checksum:iA3254EBF55EDB6F2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK045250 mRNA. Translation: BAC32280.1.
    AK077423 mRNA. Translation: BAC36793.1.
    AK170354 mRNA. Translation: BAE41740.1.
    CCDSiCCDS49737.1.
    RefSeqiNP_663600.2. NM_145625.3.
    UniGeneiMm.290022.
    Mm.391795.

    Genome annotation databases

    EnsembliENSMUST00000169681; ENSMUSP00000127774; ENSMUSG00000058655.
    GeneIDi75705.
    KEGGimmu:75705.
    UCSCiuc007xuk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK045250 mRNA. Translation: BAC32280.1 .
    AK077423 mRNA. Translation: BAC36793.1 .
    AK170354 mRNA. Translation: BAE41740.1 .
    CCDSi CCDS49737.1.
    RefSeqi NP_663600.2. NM_145625.3.
    UniGenei Mm.290022.
    Mm.391795.

    3D structure databases

    ProteinModelPortali Q8BGD9.
    SMRi Q8BGD9. Positions 96-176.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 217684. 3 interactions.
    IntActi Q8BGD9. 2 interactions.
    MINTi MINT-1954873.

    PTM databases

    PhosphoSitei Q8BGD9.

    Proteomic databases

    MaxQBi Q8BGD9.
    PaxDbi Q8BGD9.
    PRIDEi Q8BGD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000169681 ; ENSMUSP00000127774 ; ENSMUSG00000058655 .
    GeneIDi 75705.
    KEGGi mmu:75705.
    UCSCi uc007xuk.2. mouse.

    Organism-specific databases

    CTDi 1975.
    MGIi MGI:95304. Eif4b.

    Phylogenomic databases

    eggNOGi NOG238591.
    GeneTreei ENSGT00530000063406.
    HOGENOMi HOG000006553.
    HOVERGENi HBG006129.
    InParanoidi Q8BGD9.
    KOi K03258.
    OMAi SYRDGPR.
    OrthoDBi EOG7MKW86.
    PhylomeDBi Q8BGD9.
    TreeFami TF101525.

    Miscellaneous databases

    ChiTaRSi EIF4B. mouse.
    NextBioi 343748.
    PROi Q8BGD9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BGD9.
    Bgeei Q8BGD9.
    CleanExi MM_EIF4B.
    Genevestigatori Q8BGD9.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
    2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiIF4B_MOUSE
    AccessioniPrimary (citable) accession number: Q8BGD9
    Secondary accession number(s): Q3TD64
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Translation initiation factors
      List of translation initiation factor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3