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O75822

- EIF3J_HUMAN

UniProt

O75822 - EIF3J_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit J

Gene

EIF3J

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 2 (19 Sep 2002)
      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. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. translation initiation factor activity Source: UniProtKB-HAMAP

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 3 subunit JUniRule annotation
    Short name:
    eIF3jUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 1UniRule annotation
    eIF-3-alphaUniRule annotation
    eIF3 p35UniRule annotation
    Gene namesi
    Name:EIF3JUniRule annotation
    Synonyms:EIF3S1UniRule annotation
    ORF Names:PRO0391
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:3270. EIF3J.

    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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162384902.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed8 PublicationsUniRule annotation
    Chaini2 – 258257Eukaryotic translation initiation factor 3 subunit JPRO_0000123506Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine8 PublicationsUniRule annotation
    Modified residuei11 – 111Phosphoserine3 PublicationsUniRule annotation
    Modified residuei13 – 131Phosphoserine3 PublicationsUniRule annotation
    Modified residuei20 – 201Phosphoserine1 PublicationUniRule annotation
    Modified residuei109 – 1091Phosphothreonine5 PublicationsUniRule annotation
    Modified residuei127 – 1271Phosphoserine1 PublicationUniRule annotation
    Modified residuei254 – 2541Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylated. Phosphorylation is enhanced upon serum stimulation.6 PublicationsUniRule annotation

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75822.
    PaxDbiO75822.
    PeptideAtlasiO75822.
    PRIDEiO75822.

    PTM databases

    PhosphoSiteiO75822.

    Miscellaneous databases

    PMAP-CutDBO75822.

    Expressioni

    Gene expression databases

    ArrayExpressiO75822.
    BgeeiO75822.
    CleanExiHS_EIF3J.
    GenevestigatoriO75822.

    Organism-specific databases

    HPAiHPA050977.

    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-3.8 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF3BP558845EBI-366647,EBI-366696
    EIF4G1Q046372EBI-366647,EBI-73711

    Protein-protein interaction databases

    BioGridi114218. 23 interactions.
    DIPiDIP-31117N.
    IntActiO75822. 15 interactions.
    MINTiMINT-5003918.
    STRINGi9606.ENSP00000261868.

    Structurei

    Secondary structure

    1
    258
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni145 – 1473
    Helixi153 – 16715
    Helixi168 – 1703
    Helixi176 – 18813
    Helixi193 – 21220

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KRBNMR-B45-55[»]
    3BPJX-ray1.85A/B/C/D141-220[»]
    ProteinModelPortaliO75822.
    SMRiO75822. Positions 141-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75822.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 6968Sufficient for interaction with EIF3BAdd
    BLAST
    Regioni243 – 25816Promotes stable association with the 40S ribosomeAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili70 – 13566UniRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 87Poly-Ala
    Compositional biasi29 – 324Poly-Gly
    Compositional biasi53 – 575Poly-Asp
    Compositional biasi218 – 2247Poly-Lys

    Sequence similaritiesi

    Belongs to the eIF-3 subunit J family.UniRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG247523.
    HOGENOMiHOG000048982.
    InParanoidiO75822.
    KOiK03245.
    OMAiHESNPLY.
    OrthoDBiEOG7J70H8.
    PhylomeDBiO75822.
    TreeFamiTF101514.

    Family and domain databases

    Gene3Di1.10.246.60. 1 hit.
    HAMAPiMF_03009. eIF3j.
    InterProiIPR023194. eIF3-like_dom.
    IPR013906. eIF3j.
    [Graphical view]
    PANTHERiPTHR21681. PTHR21681. 1 hit.
    PfamiPF08597. eIF3_subunit. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75822-1) [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

    MAAAAAAAGD SDSWDADAFS VEDPVRKVGG GGTAGGDRWE GEDEDEDVKD    50
    NWDDDDDEKK EEAEVKPEVK ISEKKKIAEK IKEKERQQKK RQEEIKKRLE 100
    EPEEPKVLTP EEQLADKLRL KKLQEESDLE LAKETFGVNN AVYGIDAMNP 150
    SSRDDFTEFG KLLKDKITQY EKSLYYASFL EVLVRDVCIS LEIDDLKKIT 200
    NSLTVLCSEK QKQEKQSKAK KKKKGVVPGG GLKATMKDDL ADYGGYDGGY 250
    VQDYEDFM 258
    Length:258
    Mass (Da):29,062
    Last modified:September 19, 2002 - v2
    Checksum:i83624235424445AA
    GO
    Isoform 2 (identifier: O75822-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         137-191: GVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISL → V

    Note: No experimental confirmation available.

    Show »
    Length:204
    Mass (Da):22,941
    Checksum:iB2F463EE48927284
    GO
    Isoform 3 (identifier: O75822-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         50-98: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:209
    Mass (Da):23,027
    Checksum:iCA7D79180C47F1A0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401E → G in AAC78729. (PubMed:9822659)Curated

    Mass spectrometryi

    Molecular mass is 29293.2 Da from positions 1 - 258. 1 Publication
    Molecular mass is 28974.2±0.3 Da from positions 1 - 258. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti141 – 1411A → T.1 Publication
    Corresponds to variant rs2303578 [ dbSNP | Ensembl ].
    VAR_034007

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei50 – 9849Missing in isoform 3. 1 PublicationVSP_054776Add
    BLAST
    Alternative sequencei137 – 19155GVNNA…VCISL → V in isoform 2. 1 PublicationVSP_054593Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97670 mRNA. Translation: AAC78729.1.
    AK023388 mRNA. Translation: BAB14555.1.
    AK300659 mRNA. Translation: BAG62345.1.
    CR606839 mRNA. No translation available.
    AC009996 Genomic DNA. No translation available.
    BC002719 mRNA. Translation: AAH02719.1.
    AF090923 mRNA. Translation: AAF24039.1.
    CCDSiCCDS10111.1. [O75822-1]
    CCDS61612.1. [O75822-2]
    CCDS61613.1. [O75822-3]
    RefSeqiNP_001271264.1. NM_001284335.1. [O75822-2]
    NP_001271265.1. NM_001284336.1. [O75822-3]
    NP_003749.2. NM_003758.3. [O75822-1]
    UniGeneiHs.404056.

    Genome annotation databases

    EnsembliENST00000261868; ENSP00000261868; ENSG00000104131. [O75822-1]
    ENST00000424492; ENSP00000414548; ENSG00000104131. [O75822-3]
    ENST00000535391; ENSP00000440221; ENSG00000104131. [O75822-2]
    GeneIDi8669.
    KEGGihsa:8669.
    UCSCiuc001ztv.3. human. [O75822-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97670 mRNA. Translation: AAC78729.1 .
    AK023388 mRNA. Translation: BAB14555.1 .
    AK300659 mRNA. Translation: BAG62345.1 .
    CR606839 mRNA. No translation available.
    AC009996 Genomic DNA. No translation available.
    BC002719 mRNA. Translation: AAH02719.1 .
    AF090923 mRNA. Translation: AAF24039.1 .
    CCDSi CCDS10111.1. [O75822-1 ]
    CCDS61612.1. [O75822-2 ]
    CCDS61613.1. [O75822-3 ]
    RefSeqi NP_001271264.1. NM_001284335.1. [O75822-2 ]
    NP_001271265.1. NM_001284336.1. [O75822-3 ]
    NP_003749.2. NM_003758.3. [O75822-1 ]
    UniGenei Hs.404056.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KRB NMR - B 45-55 [» ]
    3BPJ X-ray 1.85 A/B/C/D 141-220 [» ]
    ProteinModelPortali O75822.
    SMRi O75822. Positions 141-211.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114218. 23 interactions.
    DIPi DIP-31117N.
    IntActi O75822. 15 interactions.
    MINTi MINT-5003918.
    STRINGi 9606.ENSP00000261868.

    PTM databases

    PhosphoSitei O75822.

    Proteomic databases

    MaxQBi O75822.
    PaxDbi O75822.
    PeptideAtlasi O75822.
    PRIDEi O75822.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261868 ; ENSP00000261868 ; ENSG00000104131 . [O75822-1 ]
    ENST00000424492 ; ENSP00000414548 ; ENSG00000104131 . [O75822-3 ]
    ENST00000535391 ; ENSP00000440221 ; ENSG00000104131 . [O75822-2 ]
    GeneIDi 8669.
    KEGGi hsa:8669.
    UCSCi uc001ztv.3. human. [O75822-1 ]

    Organism-specific databases

    CTDi 8669.
    GeneCardsi GC15P044829.
    HGNCi HGNC:3270. EIF3J.
    HPAi HPA050977.
    MIMi 603910. gene.
    neXtProti NX_O75822.
    PharmGKBi PA162384902.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247523.
    HOGENOMi HOG000048982.
    InParanoidi O75822.
    KOi K03245.
    OMAi HESNPLY.
    OrthoDBi EOG7J70H8.
    PhylomeDBi O75822.
    TreeFami TF101514.

    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

    EvolutionaryTracei O75822.
    GeneWikii EIF3J.
    GenomeRNAii 8669.
    NextBioi 32519.
    PMAP-CutDB O75822.
    PROi O75822.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75822.
    Bgeei O75822.
    CleanExi HS_EIF3J.
    Genevestigatori O75822.

    Family and domain databases

    Gene3Di 1.10.246.60. 1 hit.
    HAMAPi MF_03009. eIF3j.
    InterProi IPR023194. eIF3-like_dom.
    IPR013906. eIF3j.
    [Graphical view ]
    PANTHERi PTHR21681. PTHR21681. 1 hit.
    Pfami PF08597. eIF3_subunit. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3."
      Block K.L., Vornlocher H.-P., Hershey J.W.B.
      J. Biol. Chem. 273:31901-31908(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, INTERACTION WITH EIF3A.
    2. "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] (ISOFORMS 1 AND 2), VARIANT THR-141.
      Tissue: Ovarian carcinoma and Skeletal muscle.
    3. Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Fetal brain.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Uterus.
    6. Bienvenut W.V., Vousden K.H., Lukashchuk N.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-27; 99-119; 123-133 AND 199-210, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Lung carcinoma.
    7. "Functional prediction of the coding sequences of 50 new genes deduced by analysis of cDNA clones from human fetal liver."
      Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S., Liu M., He F.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-258 (ISOFORM 1).
      Tissue: Fetal liver.
    8. "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 EIF3K.
    9. "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 AND THE 40S RIBOSOMAL SUBUNIT.
    10. "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.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit."
      ElAntak L., Tzakos A.G., Locker N., Lukavsky P.J.
      J. Biol. Chem. 282:8165-8174(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3B AND THE 40S RIBOSOMAL SUBUNIT.
    15. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "eIF3j is located in the decoding center of the human 40S ribosomal subunit."
      Fraser C.S., Berry K.E., Hershey J.W.B., Doudna J.A.
      Mol. Cell 26:811-819(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE 40S RIBOSOMAL SUBUNIT.
    17. "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, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-11; SER-13; SER-20 AND THR-109, MASS SPECTROMETRY.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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.
    20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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 TYR-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; THR-109 AND SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13 AND THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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.
    29. "Crystal structure of human translation initiation factor 3, subunit 1 alpha."
      Structural genomics consortium (SGC)
      Submitted (JAN-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 141-220.

    Entry informationi

    Entry nameiEIF3J_HUMAN
    AccessioniPrimary (citable) accession number: O75822
    Secondary accession number(s): B4DUI3
    , F5H425, Q9BUD2, Q9H8Q2, Q9UI65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3