Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32497 (EIF3C_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 3 subunit C

Short name=eIF3c
Alternative name(s):
Eukaryotic translation initiation factor 3 93 kDa subunit
Short name=eIF3 p93
Nuclear transport protein NIP1
Translation initiation factor eIF3, p93 subunit
Gene names
Name:NIP1
Ordered Locus Names:YMR309C
ORF Names:YM9924.01C, YM9952.11C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length812 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.13

Subcellular location

Cytoplasm. Note: Mainly cytoplasmic. Ref.1

Miscellaneous

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

Sequence similarities

Belongs to the eIF-3 subunit C family.

Contains 1 PCI domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 812812Eukaryotic translation initiation factor 3 subunit C HAMAP-Rule MF_03002
PRO_0000123530

Regions

Domain650 – 780131PCI
Compositional bias15 – 147133Asp/Glu-rich (acidic) HAMAP-Rule MF_03002
Compositional bias15 – 3622Ser-rich HAMAP-Rule MF_03002

Amino acid modifications

Modified residue981Phosphoserine Ref.11 Ref.14
Modified residue991Phosphoserine Ref.11 Ref.14
Modified residue1031Phosphoserine Ref.11 Ref.14

Experimental info

Sequence conflict1111V → D in L02899. Ref.1
Sequence conflict5831Q → H in L02899. Ref.1
Sequence conflict6411K → N in L02899. Ref.1
Sequence conflict6431K → N in L02899. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32497 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: EE05097C44C45A4C

FASTA81293,204
        10         20         30         40         50         60 
MSRFFSSNYE YDVASSSSEE DLLSSSEEDL LSSSSSESEL DQESDDSFFN ESESESEADV 

        70         80         90        100        110        120 
DSDDSDAKPY GPDWFKKSEF RKQGGGSNKF LKSSNYDSSD EESDEEDGKK VVKSAKEKLL 

       130        140        150        160        170        180 
DEMQDVYNKI SQAENSDDWL TISNEFDLIS RLLVRAQQQN WGTPNIFIKV VAQVEDAVNN 

       190        200        210        220        230        240 
TQQADLKNKA VARAYNTTKQ RVKKVSRENE DSMAKFRNDP ESFDKEPTAD LDISANGFTI 

       250        260        270        280        290        300 
SSSQGNDQAV QEDFFTRLQT IIDSRGKKTV NQQSLISTLE ELLTVAEKPY EFIMAYLTLI 

       310        320        330        340        350        360 
PSRFDASANL SYQPIDQWKS SFNDISKLLS ILDQTIDTYQ VNEFADPIDF IEDEPKEDSD 

       370        380        390        400        410        420 
GVKRILGSIF SFVERLDDEF MKSLLNIDPH SSDYLIRLRD EQSIYNLILR TQLYFEATLK 

       430        440        450        460        470        480 
DEHDLERALT RPFVKRLDHI YYKSENLIKI METAAWNIIP AQFKSKFTSK DQLDSADYVD 

       490        500        510        520        530        540 
NLIDGLSTIL SKQNNIAVQK RAILYNIYYT ALNKDFQTAK DMLLTSQVQT NINQFDSSLQ 

       550        560        570        580        590        600 
ILFNRVVVQL GLSAFKLCLI EECHQILNDL LSSSHLREIL GQQSLHRISL NSSNNASADE 

       610        620        630        640        650        660 
RARQCLPYHQ HINLDLIDVV FLTCSLLIEI PRMTAFYSGI KVKRIPYSPK SIRRSLEHYD 

       670        680        690        700        710        720 
KLSFQGPPET LRDYVLFAAK SMQKGNWRDS VKYLREIKSW ALLPNMETVL NSLTERVQVE 

       730        740        750        760        770        780 
SLKTYFFSFK RFYSSFSVAK LAELFDLPEN KVVEVLQSVI AELEIPAKLN DEKTIFVVEK 

       790        800        810 
GDEITKLEEA MVKLNKEYKI AKERLNPPSN RR 

« Hide

References

« Hide 'large scale' references
[1]"NIP1, a gene required for nuclear transport in yeast."
Gu Z., Moerschell R.P., Sherman F., Goldfarb D.S.
Proc. Natl. Acad. Sci. U.S.A. 89:10355-10359(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02899 Genomic DNA. No translation available.
Z54141 Genomic DNA. Translation: CAA90827.1.
Z49212 Genomic DNA. Translation: CAA89142.1.
BK006946 Genomic DNA. Translation: DAA10210.1.
PIRA46417.
RefSeqNP_014040.1. NM_001182820.1.

3D structure databases

ProteinModelPortalP32497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35489. 89 interactions.
DIPDIP-1470N.
IntActP32497. 57 interactions.
MINTMINT-388745.
STRING4932.YMR309C.

Proteomic databases

MaxQBP32497.
PaxDbP32497.
PeptideAtlasP32497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR309C; YMR309C; YMR309C.
GeneID855357.
KEGGsce:YMR309C.

Organism-specific databases

CYGDYMR309c.
SGDS000004926. NIP1.

Phylogenomic databases

eggNOGNOG305883.
GeneTreeENSGT00390000017900.
HOGENOMHOG000029414.
KOK03252.
OMAAYLTSCM.
OrthoDBEOG75QRCP.

Enzyme and pathway databases

BioCycYEAST:G3O-32973-MONOMER.

Gene expression databases

GenevestigatorP32497.

Family and domain databases

HAMAPMF_03002. eIF3c.
InterProIPR027516. EIF3C.
IPR008905. EIF3C_N_dom.
IPR000717. PCI_dom.
[Graphical view]
PfamPF05470. eIF-3c_N. 2 hits.
PF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979121.
PROP32497.

Entry information

Entry nameEIF3C_YEAST
AccessionPrimary (citable) accession number: P32497
Secondary accession number(s): D6W0D6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Translation initiation factors

List of translation initiation factor entries