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P23588

- IF4B_HUMAN

UniProt

P23588 - IF4B_HUMAN

Protein

Eukaryotic translation initiation factor 4B

Gene

EIF4B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      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.

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. RNA binding Source: ProtInc
    5. translation initiation factor activity Source: ProtInc

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. insulin receptor signaling pathway Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    6. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    7. regulation of translational initiation Source: ProtInc
    8. RNA metabolic process Source: Reactome
    9. translation Source: Reactome
    10. translational initiation Source: Reactome

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
    REACT_1979. Translation initiation complex formation.
    REACT_20514. Deadenylation of mRNA.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_6772. S6K1 signalling.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 4B
    Short name:
    eIF-4B
    Gene namesi
    Name:EIF4B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3285. EIF4B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic translation initiation factor 4F complex Source: ProtInc

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27713.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 611611Eukaryotic translation initiation factor 4BPRO_0000081616Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei93 – 931Phosphoserine2 Publications
    Modified residuei192 – 1921Phosphoserine1 Publication
    Modified residuei219 – 2191Phosphoserine2 Publications
    Modified residuei283 – 2831Phosphoserine1 Publication
    Modified residuei365 – 3651N6-acetyllysineBy similarity
    Modified residuei406 – 4061Phosphoserine3 Publications
    Modified residuei412 – 4121Phosphothreonine1 Publication
    Modified residuei418 – 4181Phosphoserine1 Publication
    Modified residuei422 – 4221Phosphoserine; by RPS6KA1 and RPS6KB13 Publications
    Modified residuei425 – 4251Phosphoserine1 Publication
    Modified residuei445 – 4451Phosphoserine3 Publications
    Modified residuei459 – 4591Phosphoserine1 Publication
    Modified residuei498 – 4981Phosphoserine2 Publications
    Modified residuei504 – 5041Phosphoserine2 Publications
    Modified residuei586 – 5861N6-acetyllysine1 Publication
    Modified residuei597 – 5971Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1; phosphorylation enhances the affinity of EIF4B for the EIF3 complex.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23588.
    PaxDbiP23588.
    PRIDEiP23588.

    PTM databases

    PhosphoSiteiP23588.

    Miscellaneous databases

    PMAP-CutDBP23588.

    Expressioni

    Gene expression databases

    ArrayExpressiP23588.
    BgeeiP23588.
    CleanExiHS_EIF4B.
    GenevestigatoriP23588.

    Organism-specific databases

    HPAiCAB019440.
    HPA046164.

    Interactioni

    Subunit structurei

    Self-associates and interacts with EIF3 p170 subunit.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PLK1P533503EBI-970310,EBI-476768

    Protein-protein interaction databases

    BioGridi108291. 57 interactions.
    IntActiP23588. 22 interactions.
    MINTiMINT-210187.
    STRINGi9606.ENSP00000262056.

    Structurei

    Secondary structure

    1
    611
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi92 – 943
    Beta strandi96 – 1027
    Helixi109 – 1157
    Turni116 – 1183
    Beta strandi121 – 1255
    Turni130 – 1334
    Beta strandi140 – 1467
    Helixi147 – 1548
    Helixi155 – 1573
    Beta strandi167 – 1704

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WI8NMR-A88-178[»]
    2J76NMR-E77-176[»]
    ProteinModelPortaliP23588.
    SMRiP23588. Positions 96-176.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23588.

    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 – 331168Arg-richAdd
    BLAST
    Compositional biasi169 – 325157Asp-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG238591.
    HOGENOMiHOG000006553.
    HOVERGENiHBG006129.
    InParanoidiP23588.
    KOiK03258.
    OrthoDBiEOG7MKW86.
    PhylomeDBiP23588.
    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.

    P23588-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVSKPVSW ADETDDLEGD    50
    VSTTWHSNDD DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL 100
    GNLPYDVTEE SIKEFFRGLN ISAVRLPREP SNPERLKGFG YAEFEDLDSL 150
    LSALSLNEES LGNRRIRVDV ADQAQDKDRD DRSFGRDRNR DSDKTDTDWR 200
    ARPATDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG YRDGPRRDMD 250
    RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED 300
    RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPKLNLKPRS TPKEDDSSAS 350
    TSQSTRAASI FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLERRP 400
    RERHPSWRSE ETQERERSRT GSESSQTGTS TTSSRNARRR ESEKSLENET 450
    LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK ENAWVKRSSN PPARSQSSDT 500
    EQQSPTSGGG KVAPAQPSEE GPGRKDENKV DGMNAPKGQT GNSSRGPGDG 550
    GNRDHWKESD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG 600
    EDENEGEDYA E 611
    Length:611
    Mass (Da):69,151
    Last modified:September 2, 2008 - v2
    Checksum:i31CEFEA865FB10D2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti164 – 1641R → K in BAD96248. 1 PublicationCurated
    Sequence conflicti246 – 2461R → C in AAH98437. (PubMed:15489334)Curated
    Sequence conflicti343 – 3431K → E in CAA39265. (PubMed:2390971)Curated
    Sequence conflicti391 – 3922LD → WN in CAA39265. (PubMed:2390971)Curated
    Sequence conflicti471 – 4711L → Q in AAH73154. (PubMed:15489334)Curated
    Sequence conflicti486 – 4861K → R in BAD96248. 1 PublicationCurated
    Sequence conflicti611 – 6111E → D in CAG33239. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti203 – 2031P → R Found in a renal cell carcinoma case; somatic mutation. 1 Publication
    VAR_064710

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55733 Genomic DNA. Translation: CAA39265.1.
    AB076839 mRNA. Translation: BAB82380.1.
    CR456958 mRNA. Translation: CAG33239.1.
    AK222528 mRNA. Translation: BAD96248.1.
    CH471054 Genomic DNA. Translation: EAW96657.1.
    BC073139 mRNA. Translation: AAH73139.1.
    BC073154 mRNA. Translation: AAH73154.1.
    BC098437 mRNA. Translation: AAH98437.1.
    CCDSiCCDS41788.1.
    PIRiS12566.
    RefSeqiNP_001408.2. NM_001417.4.
    UniGeneiHs.648394.
    Hs.702041.

    Genome annotation databases

    EnsembliENST00000262056; ENSP00000262056; ENSG00000063046.
    GeneIDi1975.
    KEGGihsa:1975.
    UCSCiuc001sbh.4. human.

    Polymorphism databases

    DMDMi205371761.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55733 Genomic DNA. Translation: CAA39265.1 .
    AB076839 mRNA. Translation: BAB82380.1 .
    CR456958 mRNA. Translation: CAG33239.1 .
    AK222528 mRNA. Translation: BAD96248.1 .
    CH471054 Genomic DNA. Translation: EAW96657.1 .
    BC073139 mRNA. Translation: AAH73139.1 .
    BC073154 mRNA. Translation: AAH73154.1 .
    BC098437 mRNA. Translation: AAH98437.1 .
    CCDSi CCDS41788.1.
    PIRi S12566.
    RefSeqi NP_001408.2. NM_001417.4.
    UniGenei Hs.648394.
    Hs.702041.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WI8 NMR - A 88-178 [» ]
    2J76 NMR - E 77-176 [» ]
    ProteinModelPortali P23588.
    SMRi P23588. Positions 96-176.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108291. 57 interactions.
    IntActi P23588. 22 interactions.
    MINTi MINT-210187.
    STRINGi 9606.ENSP00000262056.

    PTM databases

    PhosphoSitei P23588.

    Polymorphism databases

    DMDMi 205371761.

    Proteomic databases

    MaxQBi P23588.
    PaxDbi P23588.
    PRIDEi P23588.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262056 ; ENSP00000262056 ; ENSG00000063046 .
    GeneIDi 1975.
    KEGGi hsa:1975.
    UCSCi uc001sbh.4. human.

    Organism-specific databases

    CTDi 1975.
    GeneCardsi GC12P053400.
    HGNCi HGNC:3285. EIF4B.
    HPAi CAB019440.
    HPA046164.
    MIMi 603928. gene.
    neXtProti NX_P23588.
    PharmGKBi PA27713.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238591.
    HOGENOMi HOG000006553.
    HOVERGENi HBG006129.
    InParanoidi P23588.
    KOi K03258.
    OrthoDBi EOG7MKW86.
    PhylomeDBi P23588.
    TreeFami TF101525.

    Enzyme and pathway databases

    Reactomei REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
    REACT_1979. Translation initiation complex formation.
    REACT_20514. Deadenylation of mRNA.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_6772. S6K1 signalling.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Miscellaneous databases

    EvolutionaryTracei P23588.
    GeneWikii EIF4B.
    GenomeRNAii 1975.
    NextBioi 7995.
    PMAP-CutDB P23588.
    PROi P23588.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23588.
    Bgeei P23588.
    CleanExi HS_EIF4B.
    Genevestigatori P23588.

    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. "Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif."
      Milburn S.C., Hershey J.W.B., Davies M.V., Kelleher K., Kaufman R.J.
      EMBO J. 9:2783-2790(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "Human eukaryotic initiation factor 4B."
      Yokoyama K.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cervix carcinoma.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adipose tissue.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung, Testis and Uterus.
    7. Bienvenut W.V., Calvo F., Kolch W.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 71-87; 118-135; 168-182; 189-225; 235-242; 340-372; 380-398; 473-486 AND 512-537, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    8. "The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence."
      Methot N., Pause A., Hershey J.W., Sonenberg N.
      Mol. Cell. Biol. 14:2307-2316(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3."
      Methot N., Song M.S., Sonenberg N.
      Mol. Cell. Biol. 16:5328-5334(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases."
      Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D., Mayeur G.L., Polakiewicz R.D., Sonenberg N., Hershey J.W.
      EMBO J. 23:1761-1769(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-422.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity."
      Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B., Taunton J., Hershey J.W., Blenis J., Pende M., Sonenberg N.
      EMBO J. 25:2781-2791(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-422.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-219; SER-283; SER-459 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-192; SER-219; SER-406; SER-422; SER-445; SER-498; SER-504 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; THR-412; SER-418; SER-425; SER-445; SER-498; SER-504 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Solution structure of the RNA binding domain of eukaryotic initiation factor 4B."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 88-178.
    24. Cited for: VARIANT ARG-203.

    Entry informationi

    Entry nameiIF4B_HUMAN
    AccessioniPrimary (citable) accession number: P23588
    Secondary accession number(s): Q4G0E3
    , Q53HQ2, Q6GPH5, Q6IB46, Q8WYK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. Translation initiation factors
      List of translation initiation factor entries
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3