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P23116

- EIF3A_MOUSE

UniProt

P23116 - EIF3A_MOUSE

Protein

Eukaryotic translation initiation factor 3 subunit A

Gene

Eif3a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 5 (27 Jul 2011)
      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: UniProtKB
    2. translation initiation factor activity Source: UniProtKB-HAMAP

    GO - Biological processi

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

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 3 subunit AUniRule annotation
    Short name:
    eIF3aUniRule annotation
    Alternative name(s):
    Centrosomin
    Eukaryotic translation initiation factor 3 subunit 10UniRule annotation
    eIF-3-thetaUniRule annotation
    eIF3 p167
    eIF3 p180
    eIF3 p185
    p162
    Gene namesi
    Name:Eif3a
    Synonyms:Csma, Eif3, Eif3s10
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:95301. Eif3a.

    Subcellular locationi

    Cytoplasm UniRule annotation. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Nucleus 1 Publication
    Note: Centrosomin-A is found in the centrosome. Centrosomin-B is found in the nucleus.

    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
    4. eukaryotic translation initiation factor 3 complex, eIF3m Source: MGI
    5. microtubule organizing center Source: UniProtKB-SubCell
    6. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedUniRule annotation
    Chaini2 – 13441343Eukaryotic translation initiation factor 3 subunit APRO_0000123538Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681N6-acetyllysineBy similarity
    Modified residuei492 – 4921PhosphoserineUniRule annotation
    Modified residuei1159 – 11591PhosphoserineUniRule annotation
    Modified residuei1300 – 13001PhosphoserineUniRule annotation
    Modified residuei1326 – 13261PhosphoserineUniRule annotation

    Post-translational modificationi

    Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23116.
    PaxDbiP23116.
    PRIDEiP23116.

    PTM databases

    PhosphoSiteiP23116.

    Expressioni

    Gene expression databases

    ArrayExpressiP23116.
    BgeeiP23116.
    GenevestigatoriP23116.

    Interactioni

    Subunit structurei

    Interacts with KRT7 By similarity. 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, EIF3L and EIF3K. 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 may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead 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 EIF4G1 and PIWIL2.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi199415. 21 interactions.
    IntActiP23116. 33 interactions.
    MINTiMINT-1860578.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini366 – 494129PCIUniRule annotationAdd
    BLAST
    Repeati924 – 93181; truncated
    Repeati932 – 941102
    Repeati942 – 951103; approximate
    Repeati953 – 962104
    Repeati963 – 972105
    Repeati973 – 982106
    Repeati983 – 992107
    Repeati993 – 1002108
    Repeati1003 – 1012109
    Repeati1013 – 10221010
    Repeati1023 – 10321011
    Repeati1033 – 10421012
    Repeati1043 – 10521013
    Repeati1054 – 10631014
    Repeati1064 – 10731015
    Repeati1074 – 10831016
    Repeati1084 – 10931017
    Repeati1094 – 11031018
    Repeati1104 – 11131019
    Repeati1114 – 11231020
    Repeati1124 – 11331021; approximate

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni664 – 835172Interaction with EIF3BUniRule annotationAdd
    BLAST
    Regioni924 – 113321021 X 10 AA approximate tandem repeats of [DA]-[DE]-[ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM]Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili82 – 12039UniRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi576 – 875300Glu-richAdd
    BLAST
    Compositional biasi924 – 1258335Asp-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG236708.
    GeneTreeiENSGT00730000111063.
    HOGENOMiHOG000246822.
    HOVERGENiHBG006128.
    InParanoidiP23116.
    KOiK03254.
    OMAiRGPWRNT.
    OrthoDBiEOG7BGHKJ.
    TreeFamiTF101522.

    Family and domain databases

    HAMAPiMF_03000. eIF3a.
    InterProiIPR027512. EIF3A.
    IPR000717. PCI_dom.
    [Graphical view]
    PANTHERiPTHR14005:SF0. PTHR14005:SF0. 1 hit.
    PfamiPF01399. PCI. 1 hit.
    [Graphical view]
    SMARTiSM00088. PINT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23116-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI     50
    MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK 100
    TEAAKEESQQ MVLDIEDLDN IQTPESVLLS AVSGEDTQDR TDRLLLTPWV 150
    KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ AFKFCLQYTR KAEFRKLCDN 200
    LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA ISMELWQEAF 250
    KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY 300
    HLSREMRKNL TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE 350
    KQRRLATLLG LQAPPTRIGL INDMVRFSVL QYVVPEVKDL YNWLEVEFNP 400
    LKLCERVTKV LNWVREQPEK EPELQQYVPQ LQNNTILRLL QQVAQIYQSI 450
    EFSRLTSLVP FVDAFQLERA IVDAARHCDL QVRIDHTSRT LSFGSDLNYA 500
    TREDAPVGPH LQSMPSEQIR NQLTAMSSVL AKALEVIRPA HILQEKEEQH 550
    QLAVNAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE 600
    LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA 650
    KAFKDIDIED LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER 700
    AKRLEEIPLI KSAYEEQRVK DMDLWEQQEE ERITTMQLER EKALEHKNRM 750
    SRMLEDRDLF VMRLKAARQS VYEEKLKQFE ERLAEERHSR LEDRKRQRKE 800
    ERKITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE LREYQERVKK 850
    LEEVERKKRQ RELEIEERER RREEERRLGD DPLSRKDSRW GDRDSEGTWR 900
    KGPEADSEWR RGPPEKEWRR ETRDDERPHR RDEDRLRRLG GDDEERESSL 950
    RPDDDRIPRR GLDDDRGPRR GPDEDRFSRR GTDDDRPSWR NADDDRPPRR 1000
    IGDDDRGSWR HTDDDRPPRR GLDDERGSWR TADEDRGPRR GMDDDRGPRR 1050
    GGADDERSSW RNADDDRGPR RGMDDDRGPR RGLDDDRGPW RNAAEDRISR 1100
    RGADDDRGPW RNMDDDRVPR RGDDARPGPW RPFVKPGGWR EKEKAREESW 1150
    GPPRESRPSE EREWDRDKEK DRDNQDREEN DKDLERDRDR ERDGDREDRF 1200
    RRPRDEGGWR RGPAEESSSW RDSSRRDDRD REDRRRDRDD RRDLRDLRDR 1250
    RDLRDDRDRR GPPLRSEREE ASSWRRTDDR KDDRTEERDP PRRVPPPALS 1300
    RDRERERERE GEKEKASWRA EKDRESLRRT KNETDEDGWT TVRR 1344
    Length:1,344
    Mass (Da):161,936
    Last modified:July 27, 2011 - v5
    Checksum:i215F5CCB8A2C7296
    GO

    Sequence cautioni

    The sequence CAA35246.1 differs from that shown. Reason: Frameshift at positions 421, 468, 613, 648 and 787.
    The sequence CAA59144.1 differs from that shown. Reason: Frameshift at positions 421, 468, 613, 648, 962 and 1059.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti534 – 5341L → I in AAA90910. 1 PublicationCurated
    Sequence conflicti534 – 5341L → I in CAA35246. (PubMed:9372446)Curated
    Sequence conflicti534 – 5341L → I in CAA59144. (PubMed:9372446)Curated
    Sequence conflicti683 – 6842EL → DY in CAA35246. (PubMed:9372446)Curated
    Sequence conflicti683 – 6842EL → DY in CAA59144. (PubMed:9372446)Curated
    Sequence conflicti717 – 7171Q → H in CAA35246. (PubMed:9372446)Curated
    Sequence conflicti717 – 7171Q → H in CAA59144. (PubMed:9372446)Curated
    Sequence conflicti766 – 7661A → V in CAA35246. (PubMed:9372446)Curated
    Sequence conflicti766 – 7661A → V in CAA59144. (PubMed:9372446)Curated
    Sequence conflicti793 – 7931D → E in AAA90910. 1 PublicationCurated
    Sequence conflicti1007 – 10071G → A in CAA59144. (PubMed:9372446)Curated
    Sequence conflicti1056 – 10561E → D in CAA59144. (PubMed:9372446)Curated

    RNA editingi

    Some positions are modified by RNA editing via nucleotide deletion, up to position 787. The unedited version gives rise to centrosomin-B (shown here). The fully edited version gives rise to centrosomin-A, in which the C-terminal sequence is replaced up to position 787 by Ser-Ile-Val-Ala-STOP. A combination of alternative splicing and RNA editing resulting in this template G deletion could also explain the generation of centrosomin-A mRNA.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14172 mRNA. Translation: AAA90910.1.
    AC163019 Genomic DNA. No translation available.
    X84651 mRNA. Translation: CAA59144.1. Frameshift.
    X17373 mRNA. Translation: CAA35246.1. Frameshift.
    CCDSiCCDS38035.1.
    PIRiS13800.
    T42637.
    RefSeqiNP_034253.3. NM_010123.3.
    UniGeneiMm.2238.
    Mm.482533.

    Genome annotation databases

    EnsembliENSMUST00000025955; ENSMUSP00000025955; ENSMUSG00000024991.
    GeneIDi13669.
    KEGGimmu:13669.
    UCSCiuc008ibx.1. mouse.

    Keywords - Coding sequence diversityi

    RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14172 mRNA. Translation: AAA90910.1 .
    AC163019 Genomic DNA. No translation available.
    X84651 mRNA. Translation: CAA59144.1 . Frameshift.
    X17373 mRNA. Translation: CAA35246.1 . Frameshift.
    CCDSi CCDS38035.1.
    PIRi S13800.
    T42637.
    RefSeqi NP_034253.3. NM_010123.3.
    UniGenei Mm.2238.
    Mm.482533.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199415. 21 interactions.
    IntActi P23116. 33 interactions.
    MINTi MINT-1860578.

    PTM databases

    PhosphoSitei P23116.

    Proteomic databases

    MaxQBi P23116.
    PaxDbi P23116.
    PRIDEi P23116.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025955 ; ENSMUSP00000025955 ; ENSMUSG00000024991 .
    GeneIDi 13669.
    KEGGi mmu:13669.
    UCSCi uc008ibx.1. mouse.

    Organism-specific databases

    CTDi 8661.
    MGIi MGI:95301. Eif3a.

    Phylogenomic databases

    eggNOGi NOG236708.
    GeneTreei ENSGT00730000111063.
    HOGENOMi HOG000246822.
    HOVERGENi HBG006128.
    InParanoidi P23116.
    KOi K03254.
    OMAi RGPWRNT.
    OrthoDBi EOG7BGHKJ.
    TreeFami TF101522.

    Miscellaneous databases

    ChiTaRSi EIF3A. mouse.
    NextBioi 284428.
    PROi P23116.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23116.
    Bgeei P23116.
    Genevestigatori P23116.

    Family and domain databases

    HAMAPi MF_03000. eIF3a.
    InterProi IPR027512. EIF3A.
    IPR000717. PCI_dom.
    [Graphical view ]
    PANTHERi PTHR14005:SF0. PTHR14005:SF0. 1 hit.
    Pfami PF01399. PCI. 1 hit.
    [Graphical view ]
    SMARTi SM00088. PINT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the 162 kDa component of a multi-protein complex phosphorylated by Src."
      Fisher R., Fillmore H., Reynolds A.B.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lymphoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "The centrosomal protein centrosomin A and the nuclear protein centrosomin B derive from one gene by post-transcriptional processes involving RNA editing."
      Petzelt C., Joswig G., Mincheva A., Lichter P., Stammer H., Werner D.
      J. Cell Sci. 110:2573-2578(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 401-1142 (CENTROSOMIN B), SUBCELLULAR LOCATION, RNA EDITING.
      Tissue: Ehrlich ascites tumor cell.
    4. "Murine cDNAs coding for the centrosomal antigen centrosomin A."
      Joswig G., Petzelt C., Werner D.
      J. Cell Sci. 98:37-43(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 514-790 (CENTROSOMIN A).
      Tissue: Ehrlich ascites tumor cell.
    5. Joswig G., Petzelt C., Werner D.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin."
      Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr.
      EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3B AND EIF4G1.
    7. "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, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "MILI, a PIWI-interacting RNA-binding protein, is required for germ Line stem cell self-renewal and appears to positively regulate translation."
      Unhavaithaya Y., Hao Y., Beyret E., Yin H., Kuramochi-Miyagawa S., Nakano T., Lin H.
      J. Biol. Chem. 284:6507-6519(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIWIL2.

    Entry informationi

    Entry nameiEIF3A_MOUSE
    AccessioniPrimary (citable) accession number: P23116
    Secondary accession number(s): E9QQ50, Q60697, Q62162
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 126 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Translation initiation factors
      List of translation initiation factor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3