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P60228

- EIF3E_HUMAN

UniProt

P60228 - EIF3E_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit E

Gene

EIF3E

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (16 Jan 2004)
      Previous versions | rss
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    Functioni

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins.3 PublicationsUniRule annotation

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein N-terminus binding Source: UniProtKB
    4. translation initiation factor activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. formation of translation preinitiation complex Source: UniProtKB-HAMAP
    3. gene expression Source: Reactome
    4. negative regulation of translational initiation Source: UniProtKB
    5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    6. regulation of translational initiation Source: UniProtKB
    7. translation Source: Reactome
    8. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    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 3 subunit EUniRule annotation
    Short name:
    eIF3eUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 6UniRule annotation
    Viral integration site protein INT-6 homolog
    eIF-3 p48UniRule annotation
    Gene namesi
    Name:EIF3EUniRule annotation
    Synonyms:EIF3S6UniRule annotation, INT6UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3277. EIF3E.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
    4. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
    5. eukaryotic translation initiation factor 3 complex Source: UniProtKB
    6. extracellular vesicular exosome Source: UniProt
    7. membrane Source: UniProtKB
    8. nucleoplasm Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi312 – 3121L → D: Promotes nuclear accumulation. 1 Publication

    Organism-specific databases

    PharmGKBiPA27705.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 PublicationsUniRule annotation
    Chaini2 – 445444Eukaryotic translation initiation factor 3 subunit EPRO_0000123515Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 PublicationsUniRule annotation
    Modified residuei399 – 3991Phosphoserine2 Publications
    Modified residuei439 – 4391PhosphothreonineBy similarity
    Modified residuei445 – 4451PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP60228.
    PaxDbiP60228.
    PeptideAtlasiP60228.
    PRIDEiP60228.

    PTM databases

    PhosphoSiteiP60228.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus.2 Publications

    Gene expression databases

    ArrayExpressiP60228.
    BgeeiP60228.
    CleanExiHS_EIF3E.
    GenevestigatoriP60228.

    Organism-specific databases

    HPAiHPA023973.
    HPA052182.

    Interactioni

    Subunit structurei

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with COPS3, COPS6, COPS7 (COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and UPF2. Interacts with the HTLV-1 protein Tax-1. Interacts with IFIT1 and IFIT2.15 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EPAS1Q9981410EBI-347740,EBI-447470
    ORFQ9Q2G45EBI-347740,EBI-6248094From a different organism.
    TRIM27P143737EBI-347740,EBI-719493
    ZDHHC17Q8IUH52EBI-347740,EBI-524753

    Protein-protein interaction databases

    BioGridi109857. 85 interactions.
    DIPiDIP-32691N.
    IntActiP60228. 37 interactions.
    MINTiMINT-153842.
    STRINGi9606.ENSP00000220849.

    Structurei

    3D structure databases

    ProteinModelPortaliP60228.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini290 – 395106PCIUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 128125Sufficient for interaction with EPAS1Add
    BLAST
    Regioni9 – 195187Sufficient for interaction with TRIM27Add
    BLAST
    Regioni351 – 44595Sufficient for interaction with MCM7Add
    BLAST

    Sequence similaritiesi

    Belongs to the eIF-3 subunit E family.UniRule annotation
    Contains 1 PCI domain.UniRule annotation

    Phylogenomic databases

    eggNOGiNOG324642.
    HOVERGENiHBG001097.
    InParanoidiP60228.
    KOiK03250.
    OMAiDILTGKW.
    PhylomeDBiP60228.
    TreeFamiTF101518.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    HAMAPiMF_03004. eIF3e.
    InterProiIPR016650. eIF3e.
    IPR019010. eIF3e_N.
    IPR000717. PCI_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10317. PTHR10317. 1 hit.
    PfamiPF09440. eIF3_N. 1 hit.
    PF01399. PCI. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016255. eIF3e_su6. 1 hit.
    SMARTiSM00088. PINT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P60228-1 [UniParc]FASTAAdd to Basket

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    MAEYDLTTRI AHFLDRHLVF PLLEFLSVKE IYNEKELLQG KLDLLSDTNM    50
    VDFAMDVYKN LYSDDIPHAL REKRTTVVAQ LKQLQAETEP IVKMFEDPET 100
    TRQMQSTRDG RMLFDYLADK HGFRQEYLDT LYRYAKFQYE CGNYSGAAEY 150
    LYFFRVLVPA TDRNALSSLW GKLASEILMQ NWDAAMEDLT RLKETIDNNS 200
    VSSPLQSLQQ RTWLIHWSLF VFFNHPKGRD NIIDLFLYQP QYLNAIQTMC 250
    PHILRYLTTA VITNKDVRKR RQVLKDLVKV IQQESYTYKD PITEFVECLY 300
    VNFDFDGAQK KLRECESVLV NDFFLVACLE DFIENARLFI FETFCRIHQC 350
    ISINMLADKL NMTPEEAERW IVNLIRNARL DAKIDSKLGH VVMGNNAVSP 400
    YQQVIEKTKS LSFRSQMLAM NIEKKLNQNS RSEAPNWATQ DSGFY 445
    Length:445
    Mass (Da):52,221
    Last modified:January 16, 2004 - v1
    Checksum:iA5368651DD0DDD0C
    GO

    Mass spectrometryi

    Molecular mass is 52131.8 Da from positions 1 - 445. 1 Publication
    Molecular mass is 52133.4±0.2 Da from positions 1 - 445. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti185 – 1851A → V.1 Publication
    Corresponds to variant rs17856554 [ dbSNP | Ensembl ].
    VAR_046480

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U54562 mRNA. Translation: AAC51760.1.
    U94174
    , U94162, U94163, U94164, U94165, U94166, U94167, U94168, U94169, U94170, U94171, U94172, U94173 Genomic DNA. Translation: AAC51917.1.
    U94175 mRNA. Translation: AAC51919.1.
    U62962 mRNA. Translation: AAB58251.1.
    U85947 mRNA. Translation: AAB88873.1.
    CR542275 mRNA. Translation: CAG47071.1.
    CH471060 Genomic DNA. Translation: EAW91918.1.
    BC000734 mRNA. Translation: AAH00734.1.
    BC008419 mRNA. Translation: AAH08419.1.
    BC016706 mRNA. Translation: AAH16706.1.
    BC017887 mRNA. Translation: AAH17887.1.
    BC021679 mRNA. Translation: AAH21679.1.
    CCDSiCCDS6308.1.
    RefSeqiNP_001559.1. NM_001568.2.
    UniGeneiHs.405590.

    Genome annotation databases

    EnsembliENST00000220849; ENSP00000220849; ENSG00000104408.
    GeneIDi3646.
    KEGGihsa:3646.
    UCSCiuc003ymt.3. human.

    Polymorphism databases

    DMDMi41019126.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U54562 mRNA. Translation: AAC51760.1 .
    U94174
    , U94162 , U94163 , U94164 , U94165 , U94166 , U94167 , U94168 , U94169 , U94170 , U94171 , U94172 , U94173 Genomic DNA. Translation: AAC51917.1 .
    U94175 mRNA. Translation: AAC51919.1 .
    U62962 mRNA. Translation: AAB58251.1 .
    U85947 mRNA. Translation: AAB88873.1 .
    CR542275 mRNA. Translation: CAG47071.1 .
    CH471060 Genomic DNA. Translation: EAW91918.1 .
    BC000734 mRNA. Translation: AAH00734.1 .
    BC008419 mRNA. Translation: AAH08419.1 .
    BC016706 mRNA. Translation: AAH16706.1 .
    BC017887 mRNA. Translation: AAH17887.1 .
    BC021679 mRNA. Translation: AAH21679.1 .
    CCDSi CCDS6308.1.
    RefSeqi NP_001559.1. NM_001568.2.
    UniGenei Hs.405590.

    3D structure databases

    ProteinModelPortali P60228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109857. 85 interactions.
    DIPi DIP-32691N.
    IntActi P60228. 37 interactions.
    MINTi MINT-153842.
    STRINGi 9606.ENSP00000220849.

    PTM databases

    PhosphoSitei P60228.

    Polymorphism databases

    DMDMi 41019126.

    Proteomic databases

    MaxQBi P60228.
    PaxDbi P60228.
    PeptideAtlasi P60228.
    PRIDEi P60228.

    Protocols and materials databases

    DNASUi 3646.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000220849 ; ENSP00000220849 ; ENSG00000104408 .
    GeneIDi 3646.
    KEGGi hsa:3646.
    UCSCi uc003ymt.3. human.

    Organism-specific databases

    CTDi 3646.
    GeneCardsi GC08M109284.
    HGNCi HGNC:3277. EIF3E.
    HPAi HPA023973.
    HPA052182.
    MIMi 602210. gene.
    neXtProti NX_P60228.
    PharmGKBi PA27705.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324642.
    HOVERGENi HBG001097.
    InParanoidi P60228.
    KOi K03250.
    OMAi DILTGKW.
    PhylomeDBi P60228.
    TreeFami TF101518.

    Enzyme and pathway databases

    Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Miscellaneous databases

    ChiTaRSi EIF3E. human.
    GeneWikii EIF3S6.
    GenomeRNAii 3646.
    NextBioi 14271.
    PROi P60228.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P60228.
    Bgeei P60228.
    CleanExi HS_EIF3E.
    Genevestigatori P60228.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    HAMAPi MF_03004. eIF3e.
    InterProi IPR016650. eIF3e.
    IPR019010. eIF3e_N.
    IPR000717. PCI_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10317. PTHR10317. 1 hit.
    Pfami PF09440. eIF3_N. 1 hit.
    PF01399. PCI. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016255. eIF3e_su6. 1 hit.
    SMARTi SM00088. PINT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The translation initiation factor eIF3-p48 subunit is encoded by int-6, a site of frequent integration by the mouse mammary tumor virus genome."
      Asano K., Merrick W.C., Hershey J.W.B.
      J. Biol. Chem. 272:23477-23480(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 280-289 AND 427-436, INTERACTION WITH EIF3A, IDENTIFICATION IN THE EIF-3 COMPLEX, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "The chromosome location of the human homolog of the mouse mammary tumor-associated gene INT6 and its status in human breast carcinomas."
      Miyazaki S., Imatani A., Ballard L., Marchetti A., Buttitta F., Albertsen H., Nevanlinna H.A., Gallahan D., Callahan R.
      Genomics 46:155-158(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Lung.
    3. "Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax oncoprotein."
      Desbois C., Rousset R., Bantignies F., Jalinot P.
      Science 273:951-953(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Divergent subcellular locations of HTLV-I Tax and Int-6: a contrast between in vitro protein-protein binding and intracellular protein colocalization."
      Neuvert C., Jin D.-Y., Semmes O.J., Diella F., Callahan R., Jeang K.-T.
      J. Biomed. Sci. 4:229-234(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, SUBCELLULAR LOCATION.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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], VARIANT VAL-185.
      Tissue: Bone marrow, Brain, Lung and Muscle.
    8. Cited for: PROTEIN SEQUENCE OF 2-9; 60-71; 164-172; 256-265 AND 370-376, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma and Mammary carcinoma.
    9. "Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies."
      Morris-Desbois C., Bochard V., Reynaud C., Jalinot P.
      J. Cell Sci. 112:3331-3342(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3C AND TRIM27, SUBCELLULAR LOCATION.
    10. "Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6 interact with the eIF3 core complex by binding to cognate eIF3b subunits."
      Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L., Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.
      J. Biol. Chem. 276:34948-34957(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3B.
    11. "The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3."
      Morris-Desbois C., Rety S., Ferro M., Garin J., Jalinot P.
      J. Biol. Chem. 276:45988-45995(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3L.
    12. "Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome."
      Hoareau Alves K., Bochard V., Rety S., Jalinot P.
      FEBS Lett. 527:15-21(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPS3; COPS6; COPS7 AND PSMC6.
    13. "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association."
      Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.
      RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
    14. "Induction and mode of action of the viral stress-inducible murine proteins, P56 and P54."
      Terenzi F., Pal S., Sen G.C.
      Virology 340:116-124(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFIT1.
    15. "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit."
      LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E.
      J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4G1, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "Distinct induction patterns and functions of two closely related interferon-inducible human genes, ISG54 and ISG56."
      Terenzi F., Hui D.J., Merrick W.C., Sen G.C.
      J. Biol. Chem. 281:34064-34071(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFIT2.
    17. "Reconstitution reveals the functional core of mammalian eIF3."
      Masutani M., Sonenberg N., Yokoyama S., Imataka H.
      EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
    18. "Human INT6/eIF3e is required for nonsense-mediated mRNA decay."
      Morris C., Wittmann J., Jaeck H.-M., Jalinot P.
      EMBO Rep. 8:596-602(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF3A; EIF3B; EIF3C; EIF4G1; NCBP1 AND UPF2.
    19. "Mammalian tumor suppressor Int6 specifically targets hypoxia inducible factor 2 alpha for degradation by hypoxia- and pVHL-independent regulation."
      Chen L., Uchida K., Endler A., Shibasaki F.
      J. Biol. Chem. 282:12707-12716(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EPAS1.
    20. "Isolation of the Schizosaccharomyces pombe proteasome subunit Rpn7 and a structure-function study of the proteasome-COP9-initiation factor domain."
      Sha Z., Yen H.-C.S., Scheel H., Suo J., Hofmann K., Chang E.C.
      J. Biol. Chem. 282:32414-32423(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-312.
    21. "Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry."
      Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.
      Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
    22. "Human INT6 interacts with MCM7 and regulates its stability during S phase of the cell cycle."
      Buchsbaum S., Morris C., Bochard V., Jalinot P.
      Oncogene 26:5132-5144(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MCM7.
    23. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
      Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V.
      Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY, INTERACTION WITH EIF3B.
    26. "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].
    27. "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-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Structural roles for human translation factor eIF3 in initiation of protein synthesis."
      Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.
      Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.

    Entry informationi

    Entry nameiEIF3E_HUMAN
    AccessioniPrimary (citable) accession number: P60228
    Secondary accession number(s): O43902
    , Q64058, Q64059, Q64252, Q6FG33, Q8WVK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: January 16, 2004
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3