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P06730

- IF4E_HUMAN

UniProt

P06730 - IF4E_HUMAN

Protein

Eukaryotic translation initiation factor 4E

Gene

EIF4E

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap.2 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. cytokine-mediated signaling pathway Source: Reactome
    3. G1/S transition of mitotic cell cycle Source: UniProtKB
    4. gene expression Source: Reactome
    5. insulin receptor signaling pathway Source: Reactome
    6. lung development Source: Ensembl
    7. mRNA export from nucleus Source: Reactome
    8. mRNA metabolic process Source: Reactome
    9. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    10. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    11. positive regulation of mitotic cell cycle Source: UniProtKB
    12. regulation of translation Source: UniProtKB
    13. RNA metabolic process Source: Reactome
    14. translation Source: Reactome
    15. translational initiation Source: Reactome
    16. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Host-virus interaction, Protein biosynthesis, Translation regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
    REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
    REACT_1979. Translation initiation complex formation.
    REACT_20514. Deadenylation of mRNA.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_405. Transport of the SLBP Dependant Mature mRNA.
    REACT_424. Transport of the SLBP independent Mature mRNA.
    REACT_6836. Release of eIF4E.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.
    SignaLinkiP06730.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 4E
    Short name:
    eIF-4E
    Short name:
    eIF4E
    Alternative name(s):
    eIF-4F 25 kDa subunit
    mRNA cap-binding protein
    Gene namesi
    Name:EIF4E
    Synonyms:EIF4EL1, EIF4F
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:3287. EIF4E.

    Subcellular locationi

    CytoplasmP-body 1 Publication. Cytoplasm By similarity

    GO - Cellular componenti

    1. chromatoid body Source: Ensembl
    2. cytoplasm Source: HPA
    3. cytoplasmic mRNA processing body Source: MGI
    4. cytoplasmic stress granule Source: UniProtKB
    5. cytosol Source: Reactome
    6. eukaryotic translation initiation factor 4F complex Source: UniProtKB
    7. extracellular vesicular exosome Source: UniProt
    8. mRNA cap binding complex Source: UniProtKB
    9. RISC complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Autism 19 (AUTS19) [MIM:615091]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. A heterozygous single-nucleotide insertion has been found in families affected by autism. The variant results in increased promoter activity and is involved in disease pathogenesis through EIF4E deregulation (PubMed:19556253).1 Publication
    A chromosomal aberration involving EIF4E has been found in a patient with classic autism. Translocation t(45)(q23q31.3). The breakpoint on chromosome 4 is located 56 kb downstream of EIF4E (PubMed:19556253).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531S → A or D: No effect on phosphorylation level nor incorporation into eIF4F complex. 2 Publications
    Mutagenesisi73 – 731W → A: Abolishes binding to EIF4EBP1. 1 Publication
    Mutagenesisi102 – 1021W → L: Decrease in mRNA cap binding; when associated with A-105. 1 Publication
    Mutagenesisi103 – 1031E → A: No effect. 1 Publication
    Mutagenesisi104 – 1041D → A: No effect. 1 Publication
    Mutagenesisi105 – 1051E → A: Decrease in mRNA cap binding; when associated with L-102. 1 Publication
    Mutagenesisi119 – 1191K → A: Higher affinity for EIF4G1. 1 Publication

    Organism-specific databases

    MIMi615091. phenotype.
    Orphaneti106. Autism.
    PharmGKBiPA27714.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 217216Eukaryotic translation initiation factor 4EPRO_0000193634Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei209 – 2091Phosphoserine; by PKC and MKNK23 Publications

    Post-translational modificationi

    Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP06730.
    PaxDbiP06730.
    PRIDEiP06730.

    2D gel databases

    OGPiP06730.
    REPRODUCTION-2DPAGEIPI00027485.

    PTM databases

    PhosphoSiteiP06730.

    Expressioni

    Gene expression databases

    ArrayExpressiP06730.
    BgeeiP06730.
    CleanExiHS_EIF4E.
    GenevestigatoriP06730.

    Organism-specific databases

    HPAiCAB004077.
    CAB016316.
    HPA051311.

    Interactioni

    Subunit structurei

    eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4E is also known to interact with other partners. The interaction with EIF4ENIF1 mediates the import into the nucleus. Hypophosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Rapamycin can attenuate insulin stimulation, mediated by FKBPs. Interacts mutually exclusive with EIF4A1 or EIF4A2. Interacts with NGDN and PIWIL2. Component of the CYFIP1-EIF4E-FMR1 complex composed of CYFIP, EIF4E and FMR1. Interacts directly with CYFIP1. Interacts with CLOCK By similarity. Interacts with Lassa virus Z protein. Binds to MKNK2 in nucleus. Interacts with LIMD1, WTIP and AJUBA. Interacts with APOBEC3G in an RNA-dependent manner. Interacts with LARP1.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF4EBP1Q135418EBI-73440,EBI-74090
    EIF4EBP3O605162EBI-73440,EBI-746950
    EIF4ENIF1Q9NRA86EBI-73440,EBI-301024
    EIF4G1Q046372EBI-73440,EBI-73711
    EMX2Q047434EBI-73440,EBI-399831
    GEMIN5Q8TEQ63EBI-73440,EBI-443630
    LRPPRCP427046EBI-73440,EBI-1050853
    SUMO1P631655EBI-73440,EBI-80140

    Protein-protein interaction databases

    BioGridi108292. 39 interactions.
    DIPiDIP-22N.
    IntActiP06730. 30 interactions.
    MINTiMINT-85626.
    STRINGi9606.ENSP00000280892.

    Structurei

    Secondary structure

    1
    217
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 333
    Beta strandi38 – 4811
    Beta strandi52 – 543
    Helixi57 – 593
    Beta strandi60 – 689
    Helixi69 – 7810
    Helixi82 – 843
    Beta strandi90 – 956
    Beta strandi100 – 1034
    Turni105 – 1095
    Beta strandi111 – 1166
    Helixi121 – 1244
    Helixi126 – 13813
    Turni139 – 1424
    Helixi143 – 1486
    Beta strandi149 – 1557
    Beta strandi162 – 1687
    Helixi173 – 18715
    Turni188 – 1925
    Beta strandi196 – 1994
    Helixi200 – 2023
    Beta strandi206 – 2083
    Beta strandi214 – 2163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IPBX-ray2.00A1-217[»]
    1IPCX-ray2.00A1-217[»]
    1WKWX-ray2.10A27-217[»]
    2GPQNMR-A1-217[»]
    2V8WX-ray2.30A/E1-217[»]
    2V8XX-ray2.30A/E1-217[»]
    2V8YX-ray2.10A/E1-217[»]
    2W97X-ray2.29A/B1-217[»]
    3AM7X-ray2.20A27-217[»]
    3TF2X-ray2.10A/B/C/D1-217[»]
    3U7XX-ray2.10A/B1-217[»]
    4AZAX-ray2.16A/C1-217[»]
    4BEAX-ray2.57A1-217[»]
    4DT6X-ray2.60A1-217[»]
    4DUMX-ray2.95A1-217[»]
    ProteinModelPortaliP06730.
    SMRiP06730. Positions 1-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06730.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 404EIF4EBP1/2/3 binding
    Regioni56 – 5727-methylguanosine-containing mRNA cap binding
    Regioni73 – 775EIF4EBP1/2/3 binding
    Regioni102 – 10327-methylguanosine-containing mRNA cap binding
    Regioni132 – 1398EIF4EBP1/2/3 binding
    Regioni157 – 16267-methylguanosine-containing mRNA cap binding
    Regioni205 – 20737-methylguanosine-containing mRNA cap binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5053.
    HOGENOMiHOG000186751.
    HOVERGENiHBG006130.
    KOiK03259.
    OMAiANCGSER.
    OrthoDBiEOG7QRQVM.
    PhylomeDBiP06730.
    TreeFamiTF101526.

    Family and domain databases

    Gene3Di3.30.760.10. 1 hit.
    InterProiIPR023398. TIF_eIF4e-like_dom.
    IPR001040. TIF_eIF_4E.
    IPR019770. TIF_eIF_4E_CS.
    [Graphical view]
    PANTHERiPTHR11960. PTHR11960. 1 hit.
    PfamiPF01652. IF4E. 1 hit.
    [Graphical view]
    SUPFAMiSSF55418. SSF55418. 1 hit.
    PROSITEiPS00813. IF4E. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P06730-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATVEPETTP TPNPPTTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN    50
    DKSKTWQANL RLISKFDTVE DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP 100
    MWEDEKNKRG GRWLITLNKQ QRRSDLDRFW LETLLCLIGE SFDDYSDDVC 150
    GAVVNVRAKG DKIAIWTTEC ENREAVTHIG RVYKERLGLP PKIVIGYQSH 200
    ADTATKSGST TKNRFVV 217
    Length:217
    Mass (Da):25,097
    Last modified:February 1, 1996 - v2
    Checksum:iB869B8DE615E699D
    GO
    Isoform 2 (identifier: P06730-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         133-133: T → TRWDLAMLPRLVSNFWPQVILPLQPPKVLELQ

    Note: No experimental confirmation available.

    Show »
    Length:248
    Mass (Da):28,778
    Checksum:i3869E3249A241190
    GO
    Isoform 3 (identifier: P06730-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MATVEP → MLDLTSRGQVGTSRRMAEAACSAHFL

    Note: No experimental confirmation available.

    Show »
    Length:237
    Mass (Da):27,260
    Checksum:iD4925235C678DE08
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1271D → N in AAH12611. (PubMed:15489334)Curated

    Mass spectrometryi

    Molecular mass is 24964.3 Da from positions 2 - 217. Determined by ESI. 1 Publication
    Molecular mass is 24960 Da from positions 2 - 217. Determined by ESI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MATVEP → MLDLTSRGQVGTSRRMAEAA CSAHFL in isoform 3. 1 PublicationVSP_043591
    Alternative sequencei133 – 1331T → TRWDLAMLPRLVSNFWPQVI LPLQPPKVLELQ in isoform 2. 1 PublicationVSP_042014

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15353 mRNA. Translation: AAC13647.1.
    AK300982 mRNA. Translation: BAH13387.1.
    AC019131 Genomic DNA. No translation available.
    AC093836 Genomic DNA. No translation available.
    BC012611 mRNA. Translation: AAH12611.1.
    BC035166 mRNA. Translation: AAH35166.1.
    BC043226 mRNA. Translation: AAH43226.1.
    BM849222 mRNA. No translation available.
    CCDSiCCDS34031.1. [P06730-1]
    CCDS47109.1. [P06730-3]
    CCDS54779.1. [P06730-2]
    PIRiA26411.
    RefSeqiNP_001124150.1. NM_001130678.1. [P06730-3]
    NP_001124151.1. NM_001130679.1. [P06730-2]
    NP_001959.1. NM_001968.3. [P06730-1]
    UniGeneiHs.249718.

    Genome annotation databases

    EnsembliENST00000280892; ENSP00000280892; ENSG00000151247. [P06730-3]
    ENST00000450253; ENSP00000389624; ENSG00000151247. [P06730-1]
    ENST00000505992; ENSP00000425561; ENSG00000151247. [P06730-2]
    GeneIDi1977.
    KEGGihsa:1977.
    UCSCiuc003hue.2. human. [P06730-1]
    uc011cea.1. human. [P06730-3]
    uc011ceb.1. human. [P06730-2]

    Polymorphism databases

    DMDMi1352435.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15353 mRNA. Translation: AAC13647.1 .
    AK300982 mRNA. Translation: BAH13387.1 .
    AC019131 Genomic DNA. No translation available.
    AC093836 Genomic DNA. No translation available.
    BC012611 mRNA. Translation: AAH12611.1 .
    BC035166 mRNA. Translation: AAH35166.1 .
    BC043226 mRNA. Translation: AAH43226.1 .
    BM849222 mRNA. No translation available.
    CCDSi CCDS34031.1. [P06730-1 ]
    CCDS47109.1. [P06730-3 ]
    CCDS54779.1. [P06730-2 ]
    PIRi A26411.
    RefSeqi NP_001124150.1. NM_001130678.1. [P06730-3 ]
    NP_001124151.1. NM_001130679.1. [P06730-2 ]
    NP_001959.1. NM_001968.3. [P06730-1 ]
    UniGenei Hs.249718.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IPB X-ray 2.00 A 1-217 [» ]
    1IPC X-ray 2.00 A 1-217 [» ]
    1WKW X-ray 2.10 A 27-217 [» ]
    2GPQ NMR - A 1-217 [» ]
    2V8W X-ray 2.30 A/E 1-217 [» ]
    2V8X X-ray 2.30 A/E 1-217 [» ]
    2V8Y X-ray 2.10 A/E 1-217 [» ]
    2W97 X-ray 2.29 A/B 1-217 [» ]
    3AM7 X-ray 2.20 A 27-217 [» ]
    3TF2 X-ray 2.10 A/B/C/D 1-217 [» ]
    3U7X X-ray 2.10 A/B 1-217 [» ]
    4AZA X-ray 2.16 A/C 1-217 [» ]
    4BEA X-ray 2.57 A 1-217 [» ]
    4DT6 X-ray 2.60 A 1-217 [» ]
    4DUM X-ray 2.95 A 1-217 [» ]
    ProteinModelPortali P06730.
    SMRi P06730. Positions 1-217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108292. 39 interactions.
    DIPi DIP-22N.
    IntActi P06730. 30 interactions.
    MINTi MINT-85626.
    STRINGi 9606.ENSP00000280892.

    Chemistry

    BindingDBi P06730.
    ChEMBLi CHEMBL4848.

    PTM databases

    PhosphoSitei P06730.

    Polymorphism databases

    DMDMi 1352435.

    2D gel databases

    OGPi P06730.
    REPRODUCTION-2DPAGE IPI00027485.

    Proteomic databases

    MaxQBi P06730.
    PaxDbi P06730.
    PRIDEi P06730.

    Protocols and materials databases

    DNASUi 1977.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280892 ; ENSP00000280892 ; ENSG00000151247 . [P06730-3 ]
    ENST00000450253 ; ENSP00000389624 ; ENSG00000151247 . [P06730-1 ]
    ENST00000505992 ; ENSP00000425561 ; ENSG00000151247 . [P06730-2 ]
    GeneIDi 1977.
    KEGGi hsa:1977.
    UCSCi uc003hue.2. human. [P06730-1 ]
    uc011cea.1. human. [P06730-3 ]
    uc011ceb.1. human. [P06730-2 ]

    Organism-specific databases

    CTDi 1977.
    GeneCardsi GC04M099799.
    H-InvDB HIX0039231.
    HGNCi HGNC:3287. EIF4E.
    HPAi CAB004077.
    CAB016316.
    HPA051311.
    MIMi 133440. gene.
    615091. phenotype.
    neXtProti NX_P06730.
    Orphaneti 106. Autism.
    PharmGKBi PA27714.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5053.
    HOGENOMi HOG000186751.
    HOVERGENi HBG006130.
    KOi K03259.
    OMAi ANCGSER.
    OrthoDBi EOG7QRQVM.
    PhylomeDBi P06730.
    TreeFami TF101526.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
    REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
    REACT_1979. Translation initiation complex formation.
    REACT_20514. Deadenylation of mRNA.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_405. Transport of the SLBP Dependant Mature mRNA.
    REACT_424. Transport of the SLBP independent Mature mRNA.
    REACT_6836. Release of eIF4E.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.
    SignaLinki P06730.

    Miscellaneous databases

    ChiTaRSi EIF4E. human.
    EvolutionaryTracei P06730.
    GeneWikii EIF4E.
    GenomeRNAii 1977.
    NextBioi 7999.
    PROi P06730.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06730.
    Bgeei P06730.
    CleanExi HS_EIF4E.
    Genevestigatori P06730.

    Family and domain databases

    Gene3Di 3.30.760.10. 1 hit.
    InterProi IPR023398. TIF_eIF4e-like_dom.
    IPR001040. TIF_eIF_4E.
    IPR019770. TIF_eIF_4E_CS.
    [Graphical view ]
    PANTHERi PTHR11960. PTHR11960. 1 hit.
    Pfami PF01652. IF4E. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55418. SSF55418. 1 hit.
    PROSITEi PS00813. IF4E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amino acid sequence of the mRNA cap-binding protein from human tissues."
      Rychlik W., Domier L.L., Gardner P.R., Hellmann G.M., Rhoads R.E.
      Proc. Natl. Acad. Sci. U.S.A. 84:945-949(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. Cited for: SEQUENCE REVISION TO 108 AND 189.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Small intestine.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Brain and Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-214 (ISOFORM 2).
      Tissue: Myeloma.
    7. "Phosphorylation of the proto-oncogene product eukaryotic initiation factor 4E is a common cellular response to tumor necrosis factor."
      Marino M.W., Feld L.J., Jaffe E.A., Pfeffer L.M., Han Y.-M., Donner D.B.
      J. Biol. Chem. 266:2685-2688(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    8. "Combination of Trp and Glu residues for recognition of mRNA cap structure. Analysis of m7G base recognition site of human cap binding protein (IF-4E) by site-directed mutagenesis."
      Ueda H., Iyo H., Doi M., Inoue M., Ishida T., Morioka H., Tanaka T., Nishikawa S., Uesugi S.
      FEBS Lett. 280:207-210(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-102; GLU-103; ASP-104 AND GLU-105.
    9. "Phosphorylation site of eukaryotic initiation factor 4E."
      Rychlik W., Russ M.A., Rhoads R.E.
      J. Biol. Chem. 262:10434-10437(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    10. "Characterization of wild-type and Ser53 mutant eukaryotic initiation factor 4E overexpression in mammalian cells."
      Kaufman R.J., Murtha-Riel P., Pittman D.D., Davies M.V.
      J. Biol. Chem. 268:11902-11909(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-53.
    11. "Role of Ser-53 phosphorylation in the activity of human translation initiation factor eIF-4E in mammalian and yeast cells."
      Zhang Y., Klein H.L., Schneider R.J.
      Gene 163:283-288(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-53.
    12. Cited for: PHOSPHORYLATION AT SER-209.
    13. "Serine 209, not serine 53, is the major site of phosphorylation in initiation factor eIF-4E in serum-treated Chinese hamster ovary cells."
      Flynn A., Proud C.G.
      J. Biol. Chem. 270:21684-21688(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-209.
    14. "Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E."
      Haghighat A., Mader S., Pause A., Sonenberg N.
      EMBO J. 14:5701-5709(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4G AND EIF4EBP1.
    15. "A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E."
      Dostie J., Ferraiuolo M., Pause A., Adam S.A., Sonenberg N.
      EMBO J. 19:3142-3156(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4ENIF1.
      Tissue: Fetal brain and Placenta.
    16. "Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E."
      Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N.
      EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MKNK1.
    17. "Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo."
      Li W., Belsham G.J., Proud C.G.
      J. Biol. Chem. 276:29111-29115(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4A1 AND EIF4A2.
    18. "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
      Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
      Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-209 BY MKNK2.
    19. "The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization."
      Scheper G.C., Parra J.L., Wilson M., Van Kollenburg B., Vertegaal A.C.O., Han Z.-G., Proud C.G.
      Mol. Cell. Biol. 23:5692-5705(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MKNK2.
    20. "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies."
      Wichroski M.J., Robb G.B., Rana T.M.
      PLoS Pathog. 2:E41-E41(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APOBEC3G.
    21. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    22. Cited for: INVOLVEMENT IN AUTS19, CHROMOSOMAL TRANSLOCATION.
    23. Cited for: INTERACTION WITH LARP1.
    24. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMD1; WTIP AND AJUBA.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: FUNCTION, MUTAGENESIS OF TRP-73.
    27. "Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region."
      Tomoo K., Shen X., Okabe K., Nozoe Y., Fukuhara S., Morino S., Ishida T., Taniguchi T., Hasegawa H., Terashima A., Sasaki M., Katsuya Y., Kitamura K., Miyoshi H., Ishikawa M., Miura K.
      Biochem. J. 362:539-544(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MRNA CAP ANALOGS.
    28. "Backbone resonance assignment of human eukaryotic translation initiation factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and a 17-amino acid peptide derived from human eIF4GII."
      Miura T., Shiratori Y., Shimma N.
      J. Biomol. NMR 27:279-280(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH EIF4G3 AND MRNA CAP ANALOGS.
    29. "Structural basis for mRNA cap-binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods."
      Tomoo K., Matsushita Y., Fujisaki H., Abiko F., Shen X., Taniguchi T., Miyagawa H., Kitamura K., Miura K., Ishida T.
      Biochim. Biophys. Acta 1753:191-208(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-217 IN COMPLEX WITH MRNA CAP ANALOG AND EIF4EBP1, FUNCTION, INTERACTION WITH EIF4EBP1; EIF4EBP2 AND EIF4EBP3.
    30. "Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands."
      Volpon L., Osborne M.J., Topisirovic I., Siddiqui N., Borden K.L.B.
      EMBO J. 25:5138-5149(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY, MUTAGENESIS OF LYS-119.
    31. "Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives."
      Brown C.J., McNae I., Fischer P.M., Walkinshaw M.D.
      J. Mol. Biol. 372:7-15(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH MRNA CAP ANALOGS, MASS SPECTROMETRY.

    Entry informationi

    Entry nameiIF4E_HUMAN
    AccessioniPrimary (citable) accession number: P06730
    Secondary accession number(s): B7Z6V1, D6RCQ6, Q96E95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 169 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 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Translation initiation factors
      List of translation initiation factor entries
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3