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Q5U0F4

- Q5U0F4_HUMAN

UniProt

Q5U0F4 - Q5U0F4_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit I

Gene

EIF3S2

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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.UniRule annotation

    GO - Molecular functioni

    1. translation initiation factor activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. formation of translation preinitiation complex Source: UniProtKB-HAMAP
    2. regulation of translational initiation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Initiation factorUniRule annotationSAAS annotationImported

    Keywords - Biological processi

    Protein biosynthesis

    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
    eIF-3-betaUniRule annotation
    eIF3 p36UniRule annotation
    Gene namesi
    Name:EIF3S2UniRule annotation
    Synonyms:EIF3IUniRule annotation
    ORF Names:hCG_41608Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
    2. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
    3. eukaryotic translation initiation factor 3 complex Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS annotation

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162384875.

    PTM / Processingi

    Post-translational modificationi

    Phosphorylated by TGF-beta type II receptor.UniRule annotation

    Keywords - PTMi

    PhosphoproteinUniRule annotation

    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.UniRule annotation

    Structurei

    3D structure databases

    SMRiQ5U0F4. Positions 1-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

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

    Keywords - Domaini

    RepeatUniRule annotationSAAS annotation, WD repeatUniRule annotationSAAS annotation

    Phylogenomic databases

    HOVERGENiHBG000900.
    KOiK03246.
    OMAiKATVCAF.
    PhylomeDBiQ5U0F4.

    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.

    Q5U0F4-1 [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:February 5, 2008 - v1
    Checksum:i02797BB72A752A96
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT019597 mRNA. Translation: AAV38404.1.
    AK289356 mRNA. Translation: BAF82045.1.
    AK289882 mRNA. Translation: BAF82571.1.
    CH471059 Genomic DNA. Translation: EAX07553.1.
    RefSeqiNP_003748.1. NM_003757.2.
    UniGeneiHs.530096.

    Genome annotation databases

    GeneIDi8668.
    KEGGihsa:8668.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT019597 mRNA. Translation: AAV38404.1 .
    AK289356 mRNA. Translation: BAF82045.1 .
    AK289882 mRNA. Translation: BAF82571.1 .
    CH471059 Genomic DNA. Translation: EAX07553.1 .
    RefSeqi NP_003748.1. NM_003757.2.
    UniGenei Hs.530096.

    3D structure databases

    SMRi Q5U0F4. Positions 1-324.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    DNASUi 8668.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8668.
    KEGGi hsa:8668.

    Organism-specific databases

    CTDi 8668.
    PharmGKBi PA162384875.

    Phylogenomic databases

    HOVERGENi HBG000900.
    KOi K03246.
    OMAi KATVCAF.
    PhylomeDBi Q5U0F4.

    Miscellaneous databases

    ChiTaRSi EIF3I. human.
    GenomeRNAii 8668.
    NextBioi 32515.

    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. "The sequence of the human genome."
      Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
      , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
      Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Cloning of human full-length CDSs in BD Creator(TM) System Donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    3. Cited for: NUCLEOTIDE SEQUENCE.
    4. Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: Caudate nucleusImported.

    Entry informationi

    Entry nameiQ5U0F4_HUMAN
    AccessioniPrimary (citable) accession number: Q5U0F4
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 5, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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.