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P32497

- EIF3C_YEAST

UniProt

P32497 - EIF3C_YEAST

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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

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. translation initiation factor activity Source: SGD
  2. 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
Complete GO annotation...

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
Complete GO annotation...

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

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4U1CX-ray3.50C247-812[»]
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.
InParanoidiP32497.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRFFSSNYE YDVASSSSEE DLLSSSEEDL LSSSSSESEL DQESDDSFFN
60 70 80 90 100
ESESESEADV DSDDSDAKPY GPDWFKKSEF RKQGGGSNKF LKSSNYDSSD
110 120 130 140 150
EESDEEDGKK VVKSAKEKLL DEMQDVYNKI SQAENSDDWL TISNEFDLIS
160 170 180 190 200
RLLVRAQQQN WGTPNIFIKV VAQVEDAVNN TQQADLKNKA VARAYNTTKQ
210 220 230 240 250
RVKKVSRENE DSMAKFRNDP ESFDKEPTAD LDISANGFTI SSSQGNDQAV
260 270 280 290 300
QEDFFTRLQT IIDSRGKKTV NQQSLISTLE ELLTVAEKPY EFIMAYLTLI
310 320 330 340 350
PSRFDASANL SYQPIDQWKS SFNDISKLLS ILDQTIDTYQ VNEFADPIDF
360 370 380 390 400
IEDEPKEDSD GVKRILGSIF SFVERLDDEF MKSLLNIDPH SSDYLIRLRD
410 420 430 440 450
EQSIYNLILR TQLYFEATLK DEHDLERALT RPFVKRLDHI YYKSENLIKI
460 470 480 490 500
METAAWNIIP AQFKSKFTSK DQLDSADYVD NLIDGLSTIL SKQNNIAVQK
510 520 530 540 550
RAILYNIYYT ALNKDFQTAK DMLLTSQVQT NINQFDSSLQ ILFNRVVVQL
560 570 580 590 600
GLSAFKLCLI EECHQILNDL LSSSHLREIL GQQSLHRISL NSSNNASADE
610 620 630 640 650
RARQCLPYHQ HINLDLIDVV FLTCSLLIEI PRMTAFYSGI KVKRIPYSPK
660 670 680 690 700
SIRRSLEHYD KLSFQGPPET LRDYVLFAAK SMQKGNWRDS VKYLREIKSW
710 720 730 740 750
ALLPNMETVL NSLTERVQVE SLKTYFFSFK RFYSSFSVAK LAELFDLPEN
760 770 780 790 800
KVVEVLQSVI AELEIPAKLN DEKTIFVVEK GDEITKLEEA MVKLNKEYKI
810
AKERLNPPSN RR
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

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4U1C X-ray 3.50 C 247-812 [» ]
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.
InParanoidi P32497.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 132 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3