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Q13347

- EIF3I_HUMAN

UniProt

Q13347 - EIF3I_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit I

Gene

EIF3I

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. 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. regulation of translational initiation Source: UniProtKB-HAMAP
    5. translation Source: Reactome
    6. 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.
    SignaLinkiQ13347.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 3 subunit IUniRule annotation
    Short name:
    eIF3iUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 2UniRule annotation
    TGF-beta receptor-interacting protein 1
    Short name:
    TRIP-1
    eIF-3-betaUniRule annotation
    eIF3 p36UniRule annotation
    Gene namesi
    Name:EIF3IUniRule annotation
    Synonyms:EIF3S2UniRule annotation, TRIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3272. EIF3I.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
    3. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
    4. eukaryotic translation initiation factor 3 complex Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162384875.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 325325Eukaryotic translation initiation factor 3 subunit IPRO_0000051036Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei264 – 2641N6-acetyllysine1 Publication
    Cross-linki282 – 282Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei308 – 3081Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylated by TGF-beta type II receptor.1 PublicationUniRule annotation

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13347.
    PaxDbiQ13347.
    PeptideAtlasiQ13347.
    PRIDEiQ13347.

    2D gel databases

    DOSAC-COBS-2DPAGEQ13347.
    OGPiQ13347.

    PTM databases

    PhosphoSiteiQ13347.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13347.
    BgeeiQ13347.
    CleanExiHS_EIF3I.
    GenevestigatoriQ13347.

    Organism-specific databases

    HPAiHPA029939.
    HPA029940.

    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-3.5 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CLEC4GQ6UXB43EBI-354047,EBI-2114729
    EIF3BP558844EBI-354047,EBI-366696

    Protein-protein interaction databases

    BioGridi114217. 74 interactions.
    DIPiDIP-31116N.
    IntActiQ13347. 22 interactions.
    MINTiMINT-5004513.
    STRINGi9606.ENSP00000362688.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13347.
    SMRiQ13347. Positions 1-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati8 – 4740WD 1Add
    BLAST
    Repeati50 – 9142WD 2Add
    BLAST
    Repeati144 – 18340WD 3Add
    BLAST
    Repeati186 – 22540WD 4Add
    BLAST
    Repeati283 – 32442WD 5Add
    BLAST

    Sequence similaritiesi

    Belongs to the eIF-3 subunit I family.UniRule annotation
    Contains 5 WD repeats.UniRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000231322.
    HOVERGENiHBG000900.
    InParanoidiQ13347.
    KOiK03246.
    OMAiKATVCAF.
    PhylomeDBiQ13347.
    TreeFamiTF101515.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    HAMAPiMF_03008. eIF3i.
    InterProiIPR027525. eIF3i.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 4 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 5 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 4 hits.
    PS50294. WD_REPEATS_REGION. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13347-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG    50
    HTGAVWCVDA DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG 100
    FDFGGNIIMF STDKQMGYQC FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT 150
    SAVWGPLGEC IIAGHESGEL NQYSAKSGEV LVNVKEHSRQ INDIQLSRDM 200
    TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN YDHVVLGGGQ 250
    EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY 300
    SSGGEDGYVR IHYFDPQYFE FEFEA 325
    Length:325
    Mass (Da):36,502
    Last modified:November 1, 1996 - v1
    Checksum:i02797BB72A752A96
    GO

    Mass spectrometryi

    Molecular mass is 36501.9 Da from positions 1 - 325. 1 Publication
    Molecular mass is 36503.2±0.4 Da from positions 1 - 325. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39067 mRNA. Translation: AAC97144.1.
    U36764 mRNA. Translation: AAC50224.1.
    BC000413 mRNA. Translation: AAH00413.1.
    BC003140 mRNA. Translation: AAH03140.1.
    CCDSiCCDS357.1.
    PIRiS60335.
    RefSeqiNP_003748.1. NM_003757.2.
    UniGeneiHs.530096.

    Genome annotation databases

    EnsembliENST00000373586; ENSP00000362688; ENSG00000084623.
    GeneIDi8668.
    KEGGihsa:8668.
    UCSCiuc001bur.4. human.

    Polymorphism databases

    DMDMi2494895.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39067 mRNA. Translation: AAC97144.1 .
    U36764 mRNA. Translation: AAC50224.1 .
    BC000413 mRNA. Translation: AAH00413.1 .
    BC003140 mRNA. Translation: AAH03140.1 .
    CCDSi CCDS357.1.
    PIRi S60335.
    RefSeqi NP_003748.1. NM_003757.2.
    UniGenei Hs.530096.

    3D structure databases

    ProteinModelPortali Q13347.
    SMRi Q13347. Positions 1-324.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114217. 74 interactions.
    DIPi DIP-31116N.
    IntActi Q13347. 22 interactions.
    MINTi MINT-5004513.
    STRINGi 9606.ENSP00000362688.

    PTM databases

    PhosphoSitei Q13347.

    Polymorphism databases

    DMDMi 2494895.

    2D gel databases

    DOSAC-COBS-2DPAGE Q13347.
    OGPi Q13347.

    Proteomic databases

    MaxQBi Q13347.
    PaxDbi Q13347.
    PeptideAtlasi Q13347.
    PRIDEi Q13347.

    Protocols and materials databases

    DNASUi 8668.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373586 ; ENSP00000362688 ; ENSG00000084623 .
    GeneIDi 8668.
    KEGGi hsa:8668.
    UCSCi uc001bur.4. human.

    Organism-specific databases

    CTDi 8668.
    GeneCardsi GC01P032687.
    HGNCi HGNC:3272. EIF3I.
    HPAi HPA029939.
    HPA029940.
    MIMi 603911. gene.
    neXtProti NX_Q13347.
    PharmGKBi PA162384875.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000231322.
    HOVERGENi HBG000900.
    InParanoidi Q13347.
    KOi K03246.
    OMAi KATVCAF.
    PhylomeDBi Q13347.
    TreeFami TF101515.

    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.
    SignaLinki Q13347.

    Miscellaneous databases

    ChiTaRSi EIF3I. human.
    GeneWikii EIF3I.
    GenomeRNAii 8668.
    NextBioi 32515.
    PROi Q13347.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13347.
    Bgeei Q13347.
    CleanExi HS_EIF3I.
    Genevestigatori Q13347.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    HAMAPi MF_03008. eIF3i.
    InterProi IPR027525. eIF3i.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 4 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 5 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 4 hits.
    PS50294. WD_REPEATS_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conservation and diversity of eukaryotic translation initiation factor eIF3."
      Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.
      J. Biol. Chem. 272:1101-1109(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor."
      Chen R.H., Miettinen P.J., Maruka E.M., Choy L., Derynck R.
      Nature 377:548-552(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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 and Muscle.
    4. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 269-280 AND 283-298, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    5. "Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3."
      Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.
      Eur. J. Biochem. 270:4133-4139(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3B.
    6. "The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro."
      Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A., Hershey J.W.B.
      J. Biol. Chem. 279:8946-8956(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3B.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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.
    9. "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: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "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.
    11. "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, MASS SPECTROMETRY.
    12. "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.
    13. "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-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 nameiEIF3I_HUMAN
    AccessioniPrimary (citable) accession number: Q13347
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 146 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 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3