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A1ZAX1

- EIF3C_DROME

UniProt

A1ZAX1 - EIF3C_DROME

Protein

Eukaryotic translation initiation factor 3 subunit C

Gene

eIF3-S8

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.

    GO - Molecular functioni

    1. translation initiation factor activity Source: FlyBase

    GO - Biological processi

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

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_205240. Formation of a pool of free 40S subunits.
    REACT_207008. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_207218. Translation initiation complex formation.
    REACT_213100. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_215632. Ribosomal scanning and start codon recognition.
    REACT_225982. Formation of the ternary complex, and subsequently, the 43S complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 3 subunit CUniRule annotation
    Short name:
    eIF3cUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 8UniRule annotation
    Gene namesi
    Name:eIF3-S8UniRule annotation
    ORF Names:CG4954
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0034258. eIF3-S8.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 910910Eukaryotic translation initiation factor 3 subunit CPRO_0000365388Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341Phosphoserine1 PublicationUniRule annotation
    Modified residuei165 – 1651Phosphoserine1 PublicationUniRule annotation
    Modified residuei176 – 1761Phosphoserine1 PublicationUniRule annotation
    Modified residuei185 – 1851Phosphoserine1 PublicationUniRule annotation

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiA1ZAX1.
    PRIDEiA1ZAX1.

    Expressioni

    Gene expression databases

    BgeeiA1ZAX1.

    Interactioni

    Subunit structurei

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex. The eIF-3 complex interacts with pix.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi62691. 16 interactions.
    IntActiA1ZAX1. 10 interactions.
    STRINGi7227.FBpp0086013.

    Structurei

    3D structure databases

    ProteinModelPortaliA1ZAX1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini678 – 812135PCIUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG305883.
    GeneTreeiENSGT00390000017900.
    InParanoidiA1ZAX1.
    KOiK03252.
    OMAiWKACKNF.
    OrthoDBiEOG7DC23R.
    PhylomeDBiA1ZAX1.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    HAMAPiMF_03002. eIF3c.
    InterProiIPR027516. EIF3C.
    IPR008905. EIF3C_N_dom.
    IPR000717. PCI_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF05470. eIF-3c_N. 1 hit.
    PF01399. PCI. 1 hit.
    [Graphical view]
    SMARTiSM00088. PINT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A1ZAX1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRFFANGSE SESESSEEEI QATNFNKASA FQFSDDEEEV KRVVRSTKEK    50
    RYENLTSIIK TIRNHKKIKD IPNTLSSFED LTRAYQKALP VISKEENGIT 100
    PRFYIRCLAE LEDFINEVWE DREGRKNLSK NNSKSLGTLR QKVRKYIKDF 150
    EDDLSRFREA PDQESEAEDE VVALESDGGD AGDDSDAGVK PTEAVPKAVK 200
    SAPAKAAPAD DDDSDDSIDW DSDSESETES SDDENQYQNM RERFLKRTTE 250
    KEEKDDDKRK DKRKEQKTKI RKRAEDDEDG EWETVVKGHV VEKPKMFEKD 300
    AEIDVPLVLA KLLEIMSARG KKRTDRRLQI DLLFELRDIS DQHNLGTAVS 350
    VKIHFNIISA IYDYNQKISE PMKLEHWALL LEVMQSMMKL LLANADIIMS 400
    ESVAEEHEEY ATSPFYVRGC PLAAVERLDD EFVKLLKECD PHSNDYVSRL 450
    KDEVNVVKTI ELVLQYFERS GTNNERCRIY LRKIEHLYYK FDPEVLKKKR 500
    GELPATTSTS VDVMDKLCKF IYAKDDTDRI RTRAILAHIY HHAMHDNWFQ 550
    ARDLVLMSHL QDNIDAADPA TRILYNRMMA NLGLCAFRQG NVKDAHHCLV 600
    DLMVTGKPKE LLAQGLLPQR QHERSAEQEK IEKQRQMPFH MHINLELLEC 650
    VYLVSAMLLE IPYIAAHEFD ARRRMISKTF YQQLRSSERQ SLVGPPESMR 700
    EHVVAAAKAM RCGNWQACAN FIVNKKMNTK VWDLFYESDR VREMLTKFIK 750
    EESLRTYLFT YSNVYTSISI PSLAQMYELP VPKVHSIISK MIINEELMAS 800
    LDDPSETVGM HRSEPSRLQA LAMQFVDKVT NLVDVNEKVF DMKQGNFFQR 850
    GNMGNRGDRG YNRNQNNQGG NWLGQRRDRN NRNRNQRGHH KNNQDRQQQQ 900
    QQQVQTIDEE 910
    Length:910
    Mass (Da):105,654
    Last modified:February 6, 2007 - v1
    Checksum:iFC05D6478712684A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti293 – 2931K → N in AAM52637. (PubMed:12537569)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF57818.1.
    AY122125 mRNA. Translation: AAM52637.1.
    BT044242 mRNA. Translation: ACH92307.1.
    RefSeqiNP_611242.1. NM_137398.1.
    UniGeneiDm.7296.

    Genome annotation databases

    EnsemblMetazoaiFBtr0086836; FBpp0086013; FBgn0034258.
    GeneIDi37005.
    KEGGidme:Dmel_CG4954.
    UCSCiCG4954-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF57818.1 .
    AY122125 mRNA. Translation: AAM52637.1 .
    BT044242 mRNA. Translation: ACH92307.1 .
    RefSeqi NP_611242.1. NM_137398.1.
    UniGenei Dm.7296.

    3D structure databases

    ProteinModelPortali A1ZAX1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62691. 16 interactions.
    IntActi A1ZAX1. 10 interactions.
    STRINGi 7227.FBpp0086013.

    Proteomic databases

    PaxDbi A1ZAX1.
    PRIDEi A1ZAX1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0086836 ; FBpp0086013 ; FBgn0034258 .
    GeneIDi 37005.
    KEGGi dme:Dmel_CG4954.
    UCSCi CG4954-RA. d. melanogaster.

    Organism-specific databases

    CTDi 37005.
    FlyBasei FBgn0034258. eIF3-S8.

    Phylogenomic databases

    eggNOGi NOG305883.
    GeneTreei ENSGT00390000017900.
    InParanoidi A1ZAX1.
    KOi K03252.
    OMAi WKACKNF.
    OrthoDBi EOG7DC23R.
    PhylomeDBi A1ZAX1.

    Enzyme and pathway databases

    Reactomei REACT_205240. Formation of a pool of free 40S subunits.
    REACT_207008. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_207218. Translation initiation complex formation.
    REACT_213100. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_215632. Ribosomal scanning and start codon recognition.
    REACT_225982. Formation of the ternary complex, and subsequently, the 43S complex.

    Miscellaneous databases

    ChiTaRSi eIF3-S8. drosophila.
    GenomeRNAii 37005.
    NextBioi 801456.
    PROi A1ZAX1.

    Gene expression databases

    Bgeei A1ZAX1.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    HAMAPi MF_03002. eIF3c.
    InterProi IPR027516. EIF3C.
    IPR008905. EIF3C_N_dom.
    IPR000717. PCI_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF05470. eIF-3c_N. 1 hit.
    PF01399. PCI. 1 hit.
    [Graphical view ]
    SMARTi SM00088. PINT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    4. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
    5. "The essential Drosophila ATP-binding cassette domain protein, pixie, binds the 40 S ribosome in an ATP-dependent manner and is required for translation initiation."
      Andersen D.S., Leevers S.J.
      J. Biol. Chem. 282:14752-14760(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIX, ASSOCIATION WITH THE 40S RIBOSOME.
    6. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-176 AND SER-185, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiEIF3C_DROME
    AccessioniPrimary (citable) accession number: A1ZAX1
    Secondary accession number(s): Q8MR49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 3, 2009
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Translation initiation factors
      List of translation initiation factor entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3