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Q99613

- EIF3C_HUMAN

UniProt

Q99613 - EIF3C_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit C

Gene

EIF3C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    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 CUniRule annotation
    Short name:
    eIF3cUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 8UniRule annotation
    eIF3 p110UniRule annotation
    Gene namesi
    Name:EIF3CUniRule annotation
    Synonyms:EIF3S8UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:3279. EIF3C.

    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

    PharmGKBiPA162384646.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 913913Eukaryotic translation initiation factor 3 subunit CPRO_0000123525Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphoserine1 PublicationUniRule annotation
    Modified residuei11 – 111Phosphoserine1 PublicationUniRule annotation
    Modified residuei13 – 131Phosphoserine1 PublicationUniRule annotation
    Modified residuei15 – 151Phosphoserine1 PublicationUniRule annotation
    Modified residuei16 – 161Phosphoserine1 PublicationUniRule annotation
    Modified residuei18 – 181Phosphoserine1 PublicationUniRule annotation
    Modified residuei39 – 391Phosphoserine1 PublicationUniRule annotation
    Modified residuei99 – 991N6-acetyllysineBy similarity
    Modified residuei166 – 1661Phosphoserine1 PublicationUniRule annotation
    Modified residuei524 – 5241Phosphothreonine1 PublicationUniRule annotation
    Modified residuei643 – 6431N6-acetyllysineBy similarity
    Modified residuei909 – 9091Phosphoserine1 PublicationUniRule annotation

    Post-translational modificationi

    Phosphorylated. Phosphorylation is enhanced upon serum stimulation.1 PublicationUniRule annotation

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99613.
    PaxDbiQ99613.
    PeptideAtlasiQ99613.
    PRIDEiQ99613.

    PTM databases

    PhosphoSiteiQ99613.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99613.
    BgeeiQ99613.
    CleanExiHS_EIF3C.
    HS_EIF3CL.
    GenevestigatoriQ99613.

    Organism-specific databases

    HPAiCAB034045.

    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. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Interacts with ALKBH4, IFIT1 and IFIT2.10 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX3XO005713EBI-353741,EBI-353779
    ORFQ9Q2G45EBI-353741,EBI-6248094From a different organism.

    Protein-protein interaction databases

    BioGridi114212. 70 interactions.
    DIPiDIP-32865N.
    IntActiQ99613. 23 interactions.
    MINTiMINT-5000313.
    STRINGi9606.ENSP00000332604.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99613.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini712 – 846135PCIUniRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi164 – 18926Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi243 – 2464Poly-Glu
    Compositional biasi291 – 2944Poly-Glu

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG305883.
    HOGENOMiHOG000029414.
    HOVERGENiHBG035174.
    InParanoidiQ99613.
    KOiK03252.
    OMAiENLHNVD.
    OrthoDBiEOG7DC23R.
    PhylomeDBiQ99613.
    TreeFamiTF101520.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    HAMAPiMF_03002. eIF3c.
    InterProiIPR027516. EIF3C.
    IPR008905. EIF3C_N_dom.
    IPR000717. PCI_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF05470. eIF-3c_N. 2 hits.
    PF01399. PCI. 1 hit.
    [Graphical view]
    SMARTiSM00088. PINT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99613-1) [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

    MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR    50
    SAKDKRFEEL TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE 100
    GVPRFYIRIL ADLEDYLNEL WEDKEGKKKM NKNNAKALST LRQKIRKYNR 150
    DFESHITSYK QNPEQSADED AEKNEEDSEG SSDEDEDEDG VSAATFLKKK 200
    SEAPSGESRK FLKKMDDEDE DSEDSEDDED WDTGSTSSDS DSEEEEGKQT 250
    ALASRFLKKA PTTDEDKKAA EKKREDKAKK KHDRKSKRLD EEEEDNEGGE 300
    WERVRGGVPL VKEKPKMFAK GTEITHAVVI KKLNEILQAR GKKGTDRAAQ 350
    IELLQLLVQI AAENNLGEGV IVKIKFNIIA SLYDYNPNLA TYMKPEMWGK 400
    CLDCINELMD ILFANPNIFV GENILEESEN LHNADQPLRV RGCILTLVER 450
    MDEEFTKIMQ NTDPHSQEYV EHLKDEAQVC AIIERVQRYL EEKGTTEEVC 500
    RIYLLRILHT YYKFDYKAHQ RQLTPPEGSS KSEQDQAENE GEDSAVLMER 550
    LCKYIYAKDR TDRIRTCAIL CHIYHHALHS RWYQARDLML MSHLQDNIQH 600
    ADPPVQILYN RTMVQLGICA FRQGLTKDAH NALLDIQSSG RAKELLGQGL 650
    LLRSLQERNQ EQEKVERRRQ VPFHLHINLE LLECVYLVSA MLLEIPYMAA 700
    HESDARRRMI SKQFHHQLRV GERQPLLGPP ESMREHVVAA SKAMKMGDWK 750
    TCHSFIINEK MNGKVWDLFP EADKVRTMLV RKIQEESLRT YLFTYSSVYD 800
    SISMETLSDM FELDLPTVHS IISKMIINEE LMASLDQPTQ TVVMHRTEPT 850
    AQQNLALQLA EKLGSLVENN ERVFDHKQGT YGGYFRDQKD GYRKNEGYMR 900
    RGGYRQQQSQ TAY 913
    Length:913
    Mass (Da):105,344
    Last modified:May 1, 1997 - v1
    Checksum:iCE5029F4EB51C1AA
    GO
    Isoform 2 (identifier: Q99613-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         120-129: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:903
    Mass (Da):104,101
    Checksum:iF877B86AD029CD67
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti313 – 3142EK → VR in AAC27674. (PubMed:10493829)Curated
    Sequence conflicti737 – 7371V → A in BAG64747. (PubMed:14702039)Curated

    Mass spectrometryi

    Molecular mass is 106143.8 Da from positions 1 - 913. 1 Publication
    Molecular mass is 106855±40 Da from positions 1 - 913. Determined by MALDI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei120 – 12910Missing in isoform 2. 1 PublicationVSP_055472

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46025 Genomic DNA. Translation: AAD03462.1.
    AC002544 Genomic DNA. Translation: AAC27426.1.
    U91326 Genomic DNA. Translation: AAC27674.1.
    AK000739 mRNA. Translation: BAA91352.1.
    AK292155 mRNA. Translation: BAF84844.1.
    AK303790 mRNA. Translation: BAG64747.1.
    AC145285 Genomic DNA. No translation available.
    BC000533 mRNA. Translation: AAH00533.1.
    BC001571 mRNA. Translation: AAH01571.1.
    BC071705 mRNA. Translation: AAH71705.1.
    BC157842 mRNA. Translation: AAI57843.1.
    BC157849 mRNA. Translation: AAI57850.1.
    CH878380 Genomic DNA. Translation: EAW50492.1.
    BT007335 mRNA. Translation: AAP35999.1.
    CCDSiCCDS10638.1.
    RefSeqiNP_001032897.1. NM_001037808.2.
    NP_001186071.1. NM_001199142.1.
    NP_001254503.1. NM_001267574.2.
    NP_001273407.1. NM_001286478.1.
    NP_003743.1. NM_003752.4.
    UniGeneiHs.567374.

    Genome annotation databases

    EnsembliENST00000331666; ENSP00000332604; ENSG00000184110. [Q99613-1]
    ENST00000395587; ENSP00000378953; ENSG00000184110. [Q99613-1]
    ENST00000564243; ENSP00000456416; ENSG00000184110. [Q99613-2]
    ENST00000566501; ENSP00000457963; ENSG00000184110. [Q99613-1]
    ENST00000566866; ENSP00000457418; ENSG00000184110. [Q99613-1]
    GeneIDi8663.
    KEGGihsa:8663.
    UCSCiuc002dpg.5. human.

    Polymorphism databases

    DMDMi6685539.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46025 Genomic DNA. Translation: AAD03462.1 .
    AC002544 Genomic DNA. Translation: AAC27426.1 .
    U91326 Genomic DNA. Translation: AAC27674.1 .
    AK000739 mRNA. Translation: BAA91352.1 .
    AK292155 mRNA. Translation: BAF84844.1 .
    AK303790 mRNA. Translation: BAG64747.1 .
    AC145285 Genomic DNA. No translation available.
    BC000533 mRNA. Translation: AAH00533.1 .
    BC001571 mRNA. Translation: AAH01571.1 .
    BC071705 mRNA. Translation: AAH71705.1 .
    BC157842 mRNA. Translation: AAI57843.1 .
    BC157849 mRNA. Translation: AAI57850.1 .
    CH878380 Genomic DNA. Translation: EAW50492.1 .
    BT007335 mRNA. Translation: AAP35999.1 .
    CCDSi CCDS10638.1.
    RefSeqi NP_001032897.1. NM_001037808.2.
    NP_001186071.1. NM_001199142.1.
    NP_001254503.1. NM_001267574.2.
    NP_001273407.1. NM_001286478.1.
    NP_003743.1. NM_003752.4.
    UniGenei Hs.567374.

    3D structure databases

    ProteinModelPortali Q99613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114212. 70 interactions.
    DIPi DIP-32865N.
    IntActi Q99613. 23 interactions.
    MINTi MINT-5000313.
    STRINGi 9606.ENSP00000332604.

    PTM databases

    PhosphoSitei Q99613.

    Polymorphism databases

    DMDMi 6685539.

    Proteomic databases

    MaxQBi Q99613.
    PaxDbi Q99613.
    PeptideAtlasi Q99613.
    PRIDEi Q99613.

    Protocols and materials databases

    DNASUi 8663.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331666 ; ENSP00000332604 ; ENSG00000184110 . [Q99613-1 ]
    ENST00000395587 ; ENSP00000378953 ; ENSG00000184110 . [Q99613-1 ]
    ENST00000564243 ; ENSP00000456416 ; ENSG00000184110 . [Q99613-2 ]
    ENST00000566501 ; ENSP00000457963 ; ENSG00000184110 . [Q99613-1 ]
    ENST00000566866 ; ENSP00000457418 ; ENSG00000184110 . [Q99613-1 ]
    GeneIDi 8663.
    KEGGi hsa:8663.
    UCSCi uc002dpg.5. human.

    Organism-specific databases

    CTDi 8663.
    GeneCardsi GC16P028700.
    H-InvDB HIX0038592.
    HGNCi HGNC:3279. EIF3C.
    HPAi CAB034045.
    MIMi 603916. gene.
    neXtProti NX_Q99613.
    PharmGKBi PA162384646.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305883.
    HOGENOMi HOG000029414.
    HOVERGENi HBG035174.
    InParanoidi Q99613.
    KOi K03252.
    OMAi ENLHNVD.
    OrthoDBi EOG7DC23R.
    PhylomeDBi Q99613.
    TreeFami TF101520.

    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 EIF3CL. human.
    GeneWikii EIF3C.
    GenomeRNAii 8663.
    NextBioi 32493.
    PROi Q99613.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99613.
    Bgeei Q99613.
    CleanExi HS_EIF3C.
    HS_EIF3CL.
    Genevestigatori Q99613.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    HAMAPi MF_03002. eIF3c.
    InterProi IPR027516. EIF3C.
    IPR008905. EIF3C_N_dom.
    IPR000717. PCI_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF05470. eIF-3c_N. 2 hits.
    PF01399. PCI. 1 hit.
    [Graphical view ]
    SMARTi SM00088. PINT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conservation and diversity of eukaryotic translation initiation factor eIF3."
      Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.
      J. Biol. Chem. 272:1101-1109(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Liver and Synovium.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain, Lymph and Placenta.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-913 (ISOFORM 1).
    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 EIF3B.
    9. "mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events."
      Holz M.K., Ballif B.A., Gygi S.P., Blenis J.
      Cell 123:569-580(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTOR; RPTOR AND RPS6KB1.
    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. "Induction and mode of action of the viral stress-inducible murine proteins, P56 and P54."
      Terenzi F., Pal S., Sen G.C.
      Virology 340:116-124(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFIT1 AND IFIT2.
    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. "Distinct induction patterns and functions of two closely related interferon-inducible human genes, ISG54 and ISG56."
      Terenzi F., Hui D.J., Merrick W.C., Sen G.C.
      J. Biol. Chem. 281:34064-34071(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFIT2.
    14. "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.
    15. "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.
    16. "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, PHOSPHORYLATION AT SER-9; SER-11; SER-13; SER-15; SER-16; SER-18; SER-39; SER-166; THR-524 AND SER-909, MASS SPECTROMETRY.
    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, MASS SPECTROMETRY.
    18. "IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."
      Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H.
      RNA 15:1528-1542(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Human ALKBH4 interacts with proteins associated with transcription."
      Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
      PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALKBH4.
    21. "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 nameiEIF3C_HUMAN
    AccessioniPrimary (citable) accession number: Q99613
    Secondary accession number(s): A8K7Z0
    , B2RXG3, B4E1D5, H3BRV0, O00215, Q9BW98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 154 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, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3