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P32497

- EIF3C_YEAST

UniProt

P32497 - EIF3C_YEAST

Protein

Eukaryotic translation initiation factor 3 subunit C

Gene

NIP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.1 PublicationUniRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. translation initiation factor activity Source: SGD
    3. translation initiation factor binding Source: SGD

    GO - Biological processi

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

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32973-MONOMER.

    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 93 kDa subunit
    Short name:
    eIF3 p93UniRule annotation
    Nuclear transport protein NIP1
    Translation initiation factor eIF3, p93 subunit
    Gene namesi
    Name:NIP1UniRule annotation
    Ordered Locus Names:YMR309C
    ORF Names:YM9924.01C, YM9952.11C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR309c.
    SGDiS000004926. NIP1.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation
    Note: Mainly cytoplasmic.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. cytoplasmic stress granule Source: SGD
    3. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
    4. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
    5. eukaryotic translation initiation factor 3 complex Source: SGD
    6. multi-eIF complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 812812Eukaryotic translation initiation factor 3 subunit CPRO_0000123530Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei98 – 981Phosphoserine2 PublicationsUniRule annotation
    Modified residuei99 – 991Phosphoserine2 PublicationsUniRule annotation
    Modified residuei103 – 1031Phosphoserine2 PublicationsUniRule annotation

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32497.
    PaxDbiP32497.
    PeptideAtlasiP32497.

    Expressioni

    Gene expression databases

    GenevestigatoriP32497.

    Interactioni

    Subunit structurei

    The eukaryotic translation initiation factor 3 (eIF-3) core complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5 and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome. TIF32, NIP1 and TIF5/eIF-5 comprise a minimal 40S-ribosome-binding unit. NIP1 interacts with TIF5/eIF-5 and SUI1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRT1P061037EBI-8965,EBI-8973
    RPB4P204335EBI-8965,EBI-15777
    TIF5P384315EBI-8965,EBI-9038

    Protein-protein interaction databases

    BioGridi35489. 89 interactions.
    DIPiDIP-1470N.
    IntActiP32497. 57 interactions.
    MINTiMINT-388745.
    STRINGi4932.YMR309C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32497.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini650 – 780131PCIUniRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi15 – 147133Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi15 – 3622Ser-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG305883.
    GeneTreeiENSGT00390000017900.
    HOGENOMiHOG000029414.
    KOiK03252.
    OMAiAYLTSCM.
    OrthoDBiEOG75QRCP.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P32497-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRFFSSNYE YDVASSSSEE DLLSSSEEDL LSSSSSESEL DQESDDSFFN    50
    ESESESEADV DSDDSDAKPY GPDWFKKSEF RKQGGGSNKF LKSSNYDSSD 100
    EESDEEDGKK VVKSAKEKLL DEMQDVYNKI SQAENSDDWL TISNEFDLIS 150
    RLLVRAQQQN WGTPNIFIKV VAQVEDAVNN TQQADLKNKA VARAYNTTKQ 200
    RVKKVSRENE DSMAKFRNDP ESFDKEPTAD LDISANGFTI SSSQGNDQAV 250
    QEDFFTRLQT IIDSRGKKTV NQQSLISTLE ELLTVAEKPY EFIMAYLTLI 300
    PSRFDASANL SYQPIDQWKS SFNDISKLLS ILDQTIDTYQ VNEFADPIDF 350
    IEDEPKEDSD GVKRILGSIF SFVERLDDEF MKSLLNIDPH SSDYLIRLRD 400
    EQSIYNLILR TQLYFEATLK DEHDLERALT RPFVKRLDHI YYKSENLIKI 450
    METAAWNIIP AQFKSKFTSK DQLDSADYVD NLIDGLSTIL SKQNNIAVQK 500
    RAILYNIYYT ALNKDFQTAK DMLLTSQVQT NINQFDSSLQ ILFNRVVVQL 550
    GLSAFKLCLI EECHQILNDL LSSSHLREIL GQQSLHRISL NSSNNASADE 600
    RARQCLPYHQ HINLDLIDVV FLTCSLLIEI PRMTAFYSGI KVKRIPYSPK 650
    SIRRSLEHYD KLSFQGPPET LRDYVLFAAK SMQKGNWRDS VKYLREIKSW 700
    ALLPNMETVL NSLTERVQVE SLKTYFFSFK RFYSSFSVAK LAELFDLPEN 750
    KVVEVLQSVI AELEIPAKLN DEKTIFVVEK GDEITKLEEA MVKLNKEYKI 800
    AKERLNPPSN RR 812
    Length:812
    Mass (Da):93,204
    Last modified:October 1, 1996 - v2
    Checksum:iEE05097C44C45A4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111V → D in L02899. (PubMed:1332047)Curated
    Sequence conflicti583 – 5831Q → H in L02899. (PubMed:1332047)Curated
    Sequence conflicti641 – 6411K → N in L02899. (PubMed:1332047)Curated
    Sequence conflicti643 – 6431K → N in L02899. (PubMed:1332047)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02899 Genomic DNA. No translation available.
    Z54141 Genomic DNA. Translation: CAA90827.1.
    Z49212 Genomic DNA. Translation: CAA89142.1.
    BK006946 Genomic DNA. Translation: DAA10210.1.
    PIRiA46417.
    RefSeqiNP_014040.1. NM_001182820.1.

    Genome annotation databases

    EnsemblFungiiYMR309C; YMR309C; YMR309C.
    GeneIDi855357.
    KEGGisce:YMR309C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02899 Genomic DNA. No translation available.
    Z54141 Genomic DNA. Translation: CAA90827.1 .
    Z49212 Genomic DNA. Translation: CAA89142.1 .
    BK006946 Genomic DNA. Translation: DAA10210.1 .
    PIRi A46417.
    RefSeqi NP_014040.1. NM_001182820.1.

    3D structure databases

    ProteinModelPortali P32497.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35489. 89 interactions.
    DIPi DIP-1470N.
    IntActi P32497. 57 interactions.
    MINTi MINT-388745.
    STRINGi 4932.YMR309C.

    Proteomic databases

    MaxQBi P32497.
    PaxDbi P32497.
    PeptideAtlasi P32497.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR309C ; YMR309C ; YMR309C .
    GeneIDi 855357.
    KEGGi sce:YMR309C.

    Organism-specific databases

    CYGDi YMR309c.
    SGDi S000004926. NIP1.

    Phylogenomic databases

    eggNOGi NOG305883.
    GeneTreei ENSGT00390000017900.
    HOGENOMi HOG000029414.
    KOi K03252.
    OMAi AYLTSCM.
    OrthoDBi EOG75QRCP.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32973-MONOMER.

    Miscellaneous databases

    NextBioi 979121.
    PROi P32497.

    Gene expression databases

    Genevestigatori P32497.

    Family and domain databases

    HAMAPi MF_03002. eIF3c.
    InterProi IPR027516. EIF3C.
    IPR008905. EIF3C_N_dom.
    IPR000717. PCI_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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein."
      Naranda T., MacMillan S.E., Hershey J.W.B.
      J. Biol. Chem. 269:32286-32292(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX.
    5. "Nip1p associates with 40 S ribosomes and the Prt1p subunit of eukaryotic initiation factor 3 and is required for efficient translation initiation."
      Greenberg J.R., Phan L., Gu Z., deSilva A., Apolito C., Sherman F., Hinnebusch A.G., Goldfarb D.S.
      J. Biol. Chem. 273:23485-23494(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRT1, ASSOCIATION WITH 40S RIBOSOMES.
    6. "Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5."
      Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R., Qin J., Hinnebusch A.G.
      Mol. Cell. Biol. 18:4935-4946(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EIF-3 CORE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TIF5 AND SUI1.
    7. "Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2."
      Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.
      EMBO J. 18:1673-1688(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIF5.
    8. "The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo."
      Valasek L., Mathew A.A., Shin B.-S., Nielsen K.H., Szamecz B., Hinnebusch A.G.
      Genes Dev. 17:786-799(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE 40S RIBOSOME, INTERACTION WITH RPS0A.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast."
      Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.
      Mol. Cell. Biol. 26:2984-2998(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRT1, ASSOCIATION WITH THE 40S RIBOSOME.
    11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-99 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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 WITH PRT1; TIF32; TIF34 AND TIF35.
    14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-99 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEIF3C_YEAST
    AccessioniPrimary (citable) accession number: P32497
    Secondary accession number(s): D6W0D6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 78900 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Translation initiation factors
      List of translation initiation factor entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3