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Q9UBQ5

- EIF3K_HUMAN

UniProt

Q9UBQ5 - EIF3K_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit K

Gene

EIF3K

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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: IntAct
    2. ribosome binding Source: InterPro
    3. 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 KUniRule annotation
    Short name:
    eIF3kUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 12UniRule annotation
    Muscle-specific gene M9 protein
    PLAC-24
    eIF-3 p25UniRule annotation
    eIF-3 p28
    Gene namesi
    Name:EIF3KUniRule annotation
    Synonyms:EIF3S12UniRule annotation
    ORF Names:ARG134, HSPC029, MSTP001, PTD001
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:24656. EIF3K.

    Subcellular locationi

    Nucleus 1 PublicationUniRule annotation. Cytoplasm 1 PublicationUniRule 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
    5. extracellular vesicular exosome Source: UniProt
    6. membrane Source: UniProtKB
    7. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162384923.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 PublicationsUniRule annotation
    Chaini2 – 218217Eukaryotic translation initiation factor 3 subunit KPRO_0000123546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 PublicationsUniRule annotation
    Modified residuei217 – 2171Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UBQ5.
    PaxDbiQ9UBQ5.
    PeptideAtlasiQ9UBQ5.
    PRIDEiQ9UBQ5.

    PTM databases

    PhosphoSiteiQ9UBQ5.

    Expressioni

    Tissue specificityi

    Ubiquitous, with the highest levels of expression in brain, testis and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBQ5.
    BgeeiQ9UBQ5.
    CleanExiHS_EIF3K.
    GenevestigatoriQ9UBQ5.

    Organism-specific databases

    HPAiHPA045446.

    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. Interacts with CCND3, but not with CCND1 and CCND2.5 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ORFQ9Q2G45EBI-354344,EBI-6248094From a different organism.

    Protein-protein interaction databases

    BioGridi118148. 46 interactions.
    DIPiDIP-32880N.
    IntActiQ9UBQ5. 12 interactions.
    MINTiMINT-5002042.
    STRINGi9606.ENSP00000248342.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Helixi18 – 214
    Helixi23 – 253
    Helixi26 – 3914
    Helixi44 – 5613
    Helixi58 – 603
    Helixi63 – 7513
    Turni76 – 783
    Helixi81 – 877
    Helixi91 – 944
    Helixi99 – 11012
    Helixi114 – 1207
    Helixi126 – 1294
    Helixi134 – 14916
    Beta strandi151 – 1533
    Helixi155 – 1617
    Helixi167 – 17711
    Helixi192 – 1954
    Helixi207 – 2148

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RZ4X-ray2.10A1-218[»]
    ProteinModelPortaliQ9UBQ5.
    SMRiQ9UBQ5. Positions 2-216.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBQ5.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG311878.
    HOGENOMiHOG000008222.
    HOVERGENiHBG052081.
    InParanoidiQ9UBQ5.
    KOiK15028.
    OMAiGLERYNP.
    PhylomeDBiQ9UBQ5.
    TreeFamiTF314893.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.25.40.250. 1 hit.
    HAMAPiMF_03010. eIF3k.
    InterProiIPR016024. ARM-type_fold.
    IPR009374. eIF3k.
    IPR016020. Transl_init_fac_sub12_N_euk.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR13022. PTHR13022. 1 hit.
    SUPFAMiSSF48371. SSF48371. 1 hit.

    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: Q9UBQ5-1) [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

    MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV    50
    LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR 100
    QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY 150
    QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN 200
    IVEKIDFDSV SSIMASSQ 218
    Length:218
    Mass (Da):25,060
    Last modified:May 1, 2000 - v1
    Checksum:i6B2CBBE8A9D1F28F
    GO
    Isoform 2 (identifier: Q9UBQ5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         210-218: VSSIMASSQ → EW

    Note: No experimental confirmation available.

    Show »
    Length:211
    Mass (Da):24,484
    Checksum:i59CDE70AC1995450
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191Q → K in AAD40193. (PubMed:11042152)Curated

    Mass spectrometryi

    Molecular mass is 24970.6 Da from positions 1 - 218. 1 Publication
    Molecular mass is 24971.1±0.2 Da from positions 1 - 218. Determined by MALDI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei210 – 2189VSSIMASSQ → EW in isoform 2. 1 PublicationVSP_055475

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY245432 mRNA. Translation: AAP22070.1.
    AB019392 mRNA. Translation: BAA76626.1.
    AF077051 mRNA. Translation: AAD27784.1.
    AF109355 mRNA. Translation: AAQ13503.1.
    AF315506 mRNA. Translation: AAK01365.1.
    AF085358 mRNA. Translation: AAD40193.1.
    AK289554 mRNA. Translation: BAF82243.1.
    AK316344 mRNA. Translation: BAH14715.1.
    AC008649 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW56807.1.
    BC001031 mRNA. Translation: AAH01031.1.
    BC007335 mRNA. Translation: AAH07335.2.
    BC007559 mRNA. Translation: AAH07559.1.
    CCDSiCCDS12517.1.
    RefSeqiNP_037366.1. NM_013234.2.
    UniGeneiHs.314359.

    Genome annotation databases

    EnsembliENST00000248342; ENSP00000248342; ENSG00000178982. [Q9UBQ5-1]
    ENST00000545173; ENSP00000438145; ENSG00000178982. [Q9UBQ5-2]
    GeneIDi27335.
    KEGGihsa:27335.
    UCSCiuc002oiz.1. human.

    Polymorphism databases

    DMDMi23396628.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY245432 mRNA. Translation: AAP22070.1 .
    AB019392 mRNA. Translation: BAA76626.1 .
    AF077051 mRNA. Translation: AAD27784.1 .
    AF109355 mRNA. Translation: AAQ13503.1 .
    AF315506 mRNA. Translation: AAK01365.1 .
    AF085358 mRNA. Translation: AAD40193.1 .
    AK289554 mRNA. Translation: BAF82243.1 .
    AK316344 mRNA. Translation: BAH14715.1 .
    AC008649 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW56807.1 .
    BC001031 mRNA. Translation: AAH01031.1 .
    BC007335 mRNA. Translation: AAH07335.2 .
    BC007559 mRNA. Translation: AAH07559.1 .
    CCDSi CCDS12517.1.
    RefSeqi NP_037366.1. NM_013234.2.
    UniGenei Hs.314359.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RZ4 X-ray 2.10 A 1-218 [» ]
    ProteinModelPortali Q9UBQ5.
    SMRi Q9UBQ5. Positions 2-216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118148. 46 interactions.
    DIPi DIP-32880N.
    IntActi Q9UBQ5. 12 interactions.
    MINTi MINT-5002042.
    STRINGi 9606.ENSP00000248342.

    PTM databases

    PhosphoSitei Q9UBQ5.

    Polymorphism databases

    DMDMi 23396628.

    Proteomic databases

    MaxQBi Q9UBQ5.
    PaxDbi Q9UBQ5.
    PeptideAtlasi Q9UBQ5.
    PRIDEi Q9UBQ5.

    Protocols and materials databases

    DNASUi 27335.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000248342 ; ENSP00000248342 ; ENSG00000178982 . [Q9UBQ5-1 ]
    ENST00000545173 ; ENSP00000438145 ; ENSG00000178982 . [Q9UBQ5-2 ]
    GeneIDi 27335.
    KEGGi hsa:27335.
    UCSCi uc002oiz.1. human.

    Organism-specific databases

    CTDi 27335.
    GeneCardsi GC19P039109.
    HGNCi HGNC:24656. EIF3K.
    HPAi HPA045446.
    MIMi 609596. gene.
    neXtProti NX_Q9UBQ5.
    PharmGKBi PA162384923.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311878.
    HOGENOMi HOG000008222.
    HOVERGENi HBG052081.
    InParanoidi Q9UBQ5.
    KOi K15028.
    OMAi GLERYNP.
    PhylomeDBi Q9UBQ5.
    TreeFami TF314893.

    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 EIF3K. human.
    EvolutionaryTracei Q9UBQ5.
    GeneWikii EIF3K.
    GenomeRNAii 27335.
    NextBioi 50392.
    PROi Q9UBQ5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBQ5.
    Bgeei Q9UBQ5.
    CleanExi HS_EIF3K.
    Genevestigatori Q9UBQ5.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.25.40.250. 1 hit.
    HAMAPi MF_03010. eIF3k.
    InterProi IPR016024. ARM-type_fold.
    IPR009374. eIF3k.
    IPR016020. Transl_init_fac_sub12_N_euk.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR13022. PTHR13022. 1 hit.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 21-31, IDENTIFICATION IN THE EIF-3 COMPLEX, INTERACTION WITH EIF3B; EIF3C; EIF3G AND EIF3J, TISSUE SPECIFICITY, BLOCKAGE OF N-TERMINUS.
      Tissue: Cervix carcinoma.
    2. "Muscle specific gene M9."
      Nawa G., Miyoshi Y., Nakamura Y.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    3. Ye M., Song H., Peng Y., Huang Q., Dai M., Mao Y., Zhu H., Li G., Luo M., Hu R., Chen J.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Pituitary tumor.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Aorta.
    5. "Gene cloning of human adenocarcinoma cell line."
      Yanqiu Z., Huazhang A., Fei L., Baojun C., Taidong Q., Kaichun W., Jie D., Daiming F.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Stomach cancer.
    6. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    7. "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).
      Tissue: Cerebellum and Spleen.
    8. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Placenta, Skin and Uterus.
    11. Bienvenut W.V., Zebisch A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-8; 21-31 AND 39-52, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    12. "Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3k) as a new interaction partner of cyclin D3."
      Shen X., Yang Y., Liu W., Sun M., Jiang J., Zong H., Gu J.
      FEBS Lett. 573:139-146(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCND3, SUBCELLULAR LOCATION.
    13. "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.
    14. "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.
    15. "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.
    16. "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.
    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, MASS SPECTROMETRY.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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. "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-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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].
    25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Crystal structure of human eIF3k, the first structure of eIF3 subunits."
      Wei Z., Zhang P., Zhou Z., Cheng Z., Wan M., Gong W.
      J. Biol. Chem. 279:34983-34990(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

    Entry informationi

    Entry nameiEIF3K_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBQ5
    Secondary accession number(s): A8K0I9
    , B7ZAM9, Q96IQ0, Q9Y6D1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 139 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

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

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Translation initiation factors
      List of translation initiation factor entries
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3