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Q14152

- EIF3A_HUMAN

UniProt

Q14152 - EIF3A_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit A

Gene

EIF3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (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.1 PublicationUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. formation of translation initiation complex Source: Ensembl
    3. formation of translation preinitiation complex Source: UniProtKB-HAMAP
    4. gene expression Source: Reactome
    5. regulation of translational initiation Source: UniProtKB-HAMAP
    6. translation Source: Reactome
    7. 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 AUniRule annotation
    Short name:
    eIF3aUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 10UniRule annotation
    eIF-3-thetaUniRule annotation
    eIF3 p167
    eIF3 p180
    eIF3 p185
    Gene namesi
    Name:EIF3AUniRule annotation
    Synonyms:EIF3S10UniRule annotation, KIAA0139
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:3271. EIF3A.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    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-HAMAP
    6. membrane Source: UniProtKB
    7. nucleolus Source: HPA
    8. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27699.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 PublicationsUniRule annotation
    Chaini2 – 13821381Eukaryotic translation initiation factor 3 subunit APRO_0000123537Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681N6-acetyllysine1 Publication
    Modified residuei492 – 4921Phosphoserine1 PublicationUniRule annotation
    Modified residuei881 – 8811Phosphoserine1 PublicationUniRule annotation
    Modified residuei882 – 8821Phosphoserine1 PublicationUniRule annotation
    Modified residuei1198 – 11981Phosphoserine1 PublicationUniRule annotation
    Modified residuei1336 – 13361Phosphoserine1 PublicationUniRule annotation
    Modified residuei1364 – 13641Phosphoserine1 PublicationUniRule annotation

    Post-translational modificationi

    Phosphorylated. Phosphorylation is enhanced upon serum stimulation.3 PublicationsUniRule annotation

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14152.
    PaxDbiQ14152.
    PeptideAtlasiQ14152.
    PRIDEiQ14152.

    2D gel databases

    UCD-2DPAGEQ14152.

    PTM databases

    PhosphoSiteiQ14152.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14152.
    BgeeiQ14152.
    CleanExiHS_EIF3A.
    GenevestigatoriQ14152.

    Organism-specific databases

    HPAiHPA038315.
    HPA038316.

    Interactioni

    Subunit structurei

    Interacts with EIF4G1 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 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. Also interacts with KRT7 and PIWIL2.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF3BP558846EBI-366617,EBI-366696
    KRT7P087293EBI-366617,EBI-297833
    ORFQ9Q2G45EBI-366617,EBI-6248094From a different organism.
    UPF1Q92900-25EBI-366617,EBI-373492

    Protein-protein interaction databases

    BioGridi114210. 88 interactions.
    DIPiDIP-31114N.
    IntActiQ14152. 32 interactions.
    MINTiMINT-1519859.
    STRINGi9606.ENSP00000358140.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14152.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini366 – 494129PCIUniRule annotationAdd
    BLAST
    Repeati925 – 934101
    Repeati935 – 94282; truncated
    Repeati943 – 952103
    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
    Repeati1134 – 11431022
    Repeati1144 – 1152923; truncated
    Repeati1153 – 11621024
    Repeati1163 – 11721025; approximate

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni664 – 835172Interaction with EIF3BAdd
    BLAST
    Regioni925 – 117224825 X 10 AA approximate tandem repeats of [DE]-[DE]-[DE]-R-[SEVGFPILV]-[HPSN]-[RSW]-[RL]-[DRGTIHN]-[EPMANLGDT]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 biasi925 – 1294370Asp-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.
    HOGENOMiHOG000246822.
    HOVERGENiHBG006128.
    InParanoidiQ14152.
    KOiK03254.
    OMAiRGPWRNT.
    OrthoDBiEOG7BGHKJ.
    PhylomeDBiQ14152.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14152-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI     50
    MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKMAEEK 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 TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE 350
    KQRRLATLLG LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP 400
    LKLCERVTKV LNWVREQPEK EPELQQYVPQ LQNNTILRLL QQVSQIYQSI 450
    EFSRLTSLVP FVDAFQLERA IVDAARHCDL QVRIDHTSRT LSFGSDLNYA 500
    TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA HILQEKEEQH 550
    QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE 600
    LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA 650
    KAFKDIDIED LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER 700
    AKRLEEIPLI KSAYEEQRIK DMDLWEQQEE ERITTMQLER EKALEHKNRM 750
    SRMLEDRDLF VMRLKAARQS VYEEKLKQFE ERLAEERHNR LEERKRQRKE 800
    ERRITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE LREYQERVKK 850
    LEEVERKKRQ RELEIEERER RREEERRLGD SSLSRKDSRW GDRDSEGTWR 900
    KGPEADSEWR RGPPEKEWRR GEGRDEDRSH RRDEERPRRL GDDEDREPSL 950
    RPDDDRVPRR GMDDDRGPRR GPEEDRFSRR GADDDRPSWR NTDDDRPPRR 1000
    IADEDRGNWR HADDDRPPRR GLDEDRGSWR TADEDRGPRR GMDDDRGPRR 1050
    GGADDERSSW RNADDDRGPR RGLDDDRGPR RGMDDDRGPR RGMDDDRGPR 1100
    RGMDDDRGPR RGLDDDRGPW RNADDDRIPR RGAEDDRGPW RNMDDDRLSR 1150
    RADDDRFPRR GDDSRPGPWR PLVKPGGWRE KEKAREESWG PPRESRPSEE 1200
    REWDREKERD RDNQDREEND KDPERERDRE RDVDREDRFR RPRDEGGWRR 1250
    GPAEESSSWR DSSRRDDRDR DDRRRERDDR RDLRERRDLR DDRDRRGPPL 1300
    RSEREEVSSW RRADDRKDDR VEERDPPRRV PPPALSRDRE RDRDREREGE 1350
    KEKASWRAEK DRESLRRTKN ETDEDGWTTV RR 1382
    Length:1,382
    Mass (Da):166,569
    Last modified:November 1, 1996 - v1
    Checksum:i485C01B28D67EBBA
    GO
    Isoform 2 (identifier: Q14152-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,348
    Mass (Da):162,636
    Checksum:i97F42E357D8B5405
    GO

    Sequence cautioni

    The sequence BAA09488.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti520 – 5201R → G in BAG63833. (PubMed:14702039)Curated
    Sequence conflicti983 – 9831D → G in BAG63833. (PubMed:14702039)Curated
    Sequence conflicti1272 – 12721D → G in BAG63833. (PubMed:14702039)Curated

    Mass spectrometryi

    Molecular mass is 166758.3 Da from positions 1 - 1382. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti386 – 3861E → K.1 Publication
    Corresponds to variant rs967185 [ dbSNP | Ensembl ].
    VAR_024438
    Natural varianti694 – 6941K → N.
    Corresponds to variant rs431898 [ dbSNP | Ensembl ].
    VAR_048921
    Natural varianti993 – 9931D → E.
    Corresponds to variant rs532138 [ dbSNP | Ensembl ].
    VAR_048922

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434Missing in isoform 2. 1 PublicationVSP_055471Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58046 mRNA. Translation: AAB41584.1.
    U58047 Genomic DNA. Translation: AAB41586.1.
    U78311 mRNA. Translation: AAB80695.1.
    D50929 mRNA. Translation: BAA09488.2. Different initiation.
    AK302575 mRNA. Translation: BAG63833.1.
    AL355598 Genomic DNA. Translation: CAI14127.1.
    CH471066 Genomic DNA. Translation: EAW49408.1.
    CCDSiCCDS7608.1.
    RefSeqiNP_003741.1. NM_003750.2.
    UniGeneiHs.523299.

    Genome annotation databases

    EnsembliENST00000369144; ENSP00000358140; ENSG00000107581. [Q14152-1]
    ENST00000541549; ENSP00000438178; ENSG00000107581. [Q14152-2]
    GeneIDi8661.
    KEGGihsa:8661.
    UCSCiuc001ldu.3. human.

    Polymorphism databases

    DMDMi6685537.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58046 mRNA. Translation: AAB41584.1 .
    U58047 Genomic DNA. Translation: AAB41586.1 .
    U78311 mRNA. Translation: AAB80695.1 .
    D50929 mRNA. Translation: BAA09488.2 . Different initiation.
    AK302575 mRNA. Translation: BAG63833.1 .
    AL355598 Genomic DNA. Translation: CAI14127.1 .
    CH471066 Genomic DNA. Translation: EAW49408.1 .
    CCDSi CCDS7608.1.
    RefSeqi NP_003741.1. NM_003750.2.
    UniGenei Hs.523299.

    3D structure databases

    ProteinModelPortali Q14152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114210. 88 interactions.
    DIPi DIP-31114N.
    IntActi Q14152. 32 interactions.
    MINTi MINT-1519859.
    STRINGi 9606.ENSP00000358140.

    PTM databases

    PhosphoSitei Q14152.

    Polymorphism databases

    DMDMi 6685537.

    2D gel databases

    UCD-2DPAGE Q14152.

    Proteomic databases

    MaxQBi Q14152.
    PaxDbi Q14152.
    PeptideAtlasi Q14152.
    PRIDEi Q14152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369144 ; ENSP00000358140 ; ENSG00000107581 . [Q14152-1 ]
    ENST00000541549 ; ENSP00000438178 ; ENSG00000107581 . [Q14152-2 ]
    GeneIDi 8661.
    KEGGi hsa:8661.
    UCSCi uc001ldu.3. human.

    Organism-specific databases

    CTDi 8661.
    GeneCardsi GC10M120794.
    H-InvDB HIX0170434.
    HGNCi HGNC:3271. EIF3A.
    HPAi HPA038315.
    HPA038316.
    MIMi 602039. gene.
    neXtProti NX_Q14152.
    PharmGKBi PA27699.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236708.
    HOGENOMi HOG000246822.
    HOVERGENi HBG006128.
    InParanoidi Q14152.
    KOi K03254.
    OMAi RGPWRNT.
    OrthoDBi EOG7BGHKJ.
    PhylomeDBi Q14152.
    TreeFami TF101522.

    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 EIF3A. human.
    GeneWikii EIF3A.
    GenomeRNAii 8661.
    NextBioi 32483.
    PROi Q14152.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14152.
    Bgeei Q14152.
    CleanExi HS_EIF3A.
    Genevestigatori Q14152.

    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. "The human p167 gene encodes a unique structural protein that contains centrosomin A homology and associates with a multicomponent complex."
      Scholler J.K., Kanner S.B.
      DNA Cell Biol. 16:515-531(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Lymphoblastoma.
    2. "Identification of cDNA clones for the large subunit of eukaryotic translation initiation factor 3. Comparison of homologues from human, Nicotiana tabacum, Caenorhabditis elegans, and Saccharomyces cerevisiae."
      Johnson K.R., Merrick W.C., Zoll W.L., Zhu Y.
      J. Biol. Chem. 272:7106-7113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Keratinocyte and Liver.
    3. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Myelomonocyte.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LYS-386.
      Tissue: Testis.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: PROTEIN SEQUENCE OF 2-13; 15-36; 69-75; 85-91; 144-151; 173-183; 252-264; 279-298; 309-317; 322-335; 341-351; 368-388; 439-469; 490-546; 582-589; 624-632; 694-711; 719-740; 776-782; 817-824; 838-847; 850-856; 862-868; 877-885; 1071-1080; 1122-1130; 1142-1150 AND 1358-1366, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma and Mammary carcinoma.
    8. "Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7."
      Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.
      J. Cell. Biochem. 80:483-490(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF3B AND KRT7.
    9. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. "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: INTERACTION WITH EIF3E.
    15. "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, PHOSPHORYLATION AT SER-881; SER-1198; SER-1336 AND SER-1364, MASS SPECTROMETRY.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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, IDENTIFICATION BY MASS SPECTROMETRY.
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-882, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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 nameiEIF3A_HUMAN
    AccessioniPrimary (citable) accession number: Q14152
    Secondary accession number(s): B1AMV5
    , B4DYS1, F5H335, O00653, Q15778
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 144 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 10
      Human chromosome 10: 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