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Q05775 (EIF3J_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 111. 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 J

Short name=eIF3j
Alternative name(s):
Eukaryotic translation initiation factor 3 30 kDa subunit
Short name=eIF-3 30 kDa
Gene names
Name:HCR1
Ordered Locus Names:YLR192C
ORF Names:L8167.11
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable 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. HAMAP-Rule MF_03009

Subunit structure

Probable component of the eukaryotic translation initiation factor 3 (eIF-3) complex. Is not part of the eIF-3 core complex, with which it is associated in substochiometric amounts.

Subcellular location

Cytoplasm Ref.5.

Disruption phenotype

Marked reduction in binding of the eIF-3 core complex to 40S ribosomes. Ref.7

Miscellaneous

Present with 17900 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the eIF-3 subunit J family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RLI1Q031954EBI-8944,EBI-35146

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 265265Eukaryotic translation initiation factor 3 subunit J HAMAP-Rule MF_03009
PRO_0000123509

Amino acid modifications

Modified residue751Phosphothreonine Ref.8 Ref.9 Ref.10
Modified residue921Phosphoserine Ref.10

Experimental info

Mutagenesis2151R → I: Increased association of the eIF-3 complex and 40S ribosomes. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q05775 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BDDBC5943DD7F9BB

FASTA26529,564
        10         20         30         40         50         60 
MSWDDEAING SMGNDDAVLM DSWDAEIGDD EPVMQSWDAE EEEKKPAPKP KKEQPKKVKK 

        70         80         90        100        110        120 
GKESSADRAL LDIDTLDEKT RKELIKKAEM ESDLNNAADL FAGLGVAEEH PRARALQKEQ 

       130        140        150        160        170        180 
EEQALKRPAF TKDTPIETHP LFNAETKREY QDLRKALTAA ITPMNKKSPL NYSSSLAIDL 

       190        200        210        220        230        240 
IRDVAKPMSI ESIRQTVATL NVLIKDKERE ERQARLARVR GGTATGGAGK KKVKGKTNLG 

       250        260 
GAFKKDQDFD LDGPDDFEFG DDDFM 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The Saccharomyces cerevisiae HCR1 gene encoding a homologue of the p35 subunit of human translation initiation factor 3 (eIF3) is a high copy suppressor of a temperature-sensitive mutation in the Rpg1p subunit of yeast eIF3."
Valasek L., Hasek J., Trachsel H., Imre E.M., Ruis H.
J. Biol. Chem. 274:27567-27572(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"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].
[7]"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, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-215.
[8]"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 THR-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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 THR-75 AND SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14913 Genomic DNA. Translation: AAB67433.1.
AY557943 Genomic DNA. Translation: AAS56269.1.
BK006945 Genomic DNA. Translation: DAA09511.1.
PIRS48545.
RefSeqNP_013293.1. NM_001182079.1.

3D structure databases

ProteinModelPortalQ05775.
SMRQ05775. Positions 138-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31462. 134 interactions.
DIPDIP-4532N.
IntActQ05775. 23 interactions.
MINTMINT-517104.
STRING4932.YLR192C.

Proteomic databases

PaxDbQ05775.
PeptideAtlasQ05775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR192C; YLR192C; YLR192C.
GeneID850889.
KEGGsce:YLR192C.

Organism-specific databases

CYGDYLR192c.
SGDS000004182. HCR1.

Phylogenomic databases

eggNOGNOG118058.
HOGENOMHOG000246847.
KOK03245.
OMAINEHPRE.
OrthoDBEOG76X6BX.

Enzyme and pathway databases

BioCycYEAST:G3O-32314-MONOMER.

Gene expression databases

GenevestigatorQ05775.

Family and domain databases

Gene3D1.10.246.60. 1 hit.
HAMAPMF_03009. eIF3j.
InterProIPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view]
PANTHERPTHR21681. PTHR21681. 1 hit.
PfamPF08597. eIF3_subunit. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967257.
PROQ05775.

Entry information

Entry nameEIF3J_YEAST
AccessionPrimary (citable) accession number: Q05775
Secondary accession number(s): D6VYJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: 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