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Protein

Eukaryotic translation initiation factor 3 subunit J

Gene

HCR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • translation initiation factor activity Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • formation of translation preinitiation complex Source: UniProtKB-HAMAP
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • regulation of translational initiation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciYEAST:G3O-32314-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit JUniRule annotation
Short name:
eIF3jUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 30 kDa subunit
Short name:
eIF-3 30 kDa
Gene namesi
Name:HCR1UniRule annotation
Ordered Locus Names:YLR192C
ORF Names:L8167.11
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR192c.
EuPathDBiFungiDB:YLR192C.
SGDiS000004182. HCR1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Marked reduction in binding of the eIF-3 core complex to 40S ribosomes.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi215 – 2151R → I: Increased association of the eIF-3 complex and 40S ribosomes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 265265Eukaryotic translation initiation factor 3 subunit JPRO_0000123509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751Phosphothreonine3 Publications
Modified residuei92 – 921Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05775.
PaxDbiQ05775.
PeptideAtlasiQ05775.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
RLI1Q031954EBI-8944,EBI-35146

Protein-protein interaction databases

BioGridi31462. 134 interactions.
DIPiDIP-4532N.
IntActiQ05775. 23 interactions.
MINTiMINT-517104.

Structurei

3D structure databases

ProteinModelPortaliQ05775.
SMRiQ05775. Positions 138-213.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-3 subunit J family.UniRule annotation

Phylogenomic databases

eggNOGiNOG118058.
HOGENOMiHOG000246847.
InParanoidiQ05775.
KOiK03245.
OMAiNAHPRER.
OrthoDBiEOG76X6BX.

Family and domain databases

Gene3Di1.10.246.60. 1 hit.
HAMAPiMF_03009. eIF3j.
InterProiIPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view]
PANTHERiPTHR21681. PTHR21681. 1 hit.
PfamiPF08597. eIF3_subunit. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWDDEAING SMGNDDAVLM DSWDAEIGDD EPVMQSWDAE EEEKKPAPKP
60 70 80 90 100
KKEQPKKVKK GKESSADRAL LDIDTLDEKT RKELIKKAEM ESDLNNAADL
110 120 130 140 150
FAGLGVAEEH PRARALQKEQ EEQALKRPAF TKDTPIETHP LFNAETKREY
160 170 180 190 200
QDLRKALTAA ITPMNKKSPL NYSSSLAIDL IRDVAKPMSI ESIRQTVATL
210 220 230 240 250
NVLIKDKERE ERQARLARVR GGTATGGAGK KKVKGKTNLG GAFKKDQDFD
260
LDGPDDFEFG DDDFM
Length:265
Mass (Da):29,564
Last modified:November 1, 1996 - v1
Checksum:iBDDBC5943DD7F9BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67433.1.
AY557943 Genomic DNA. Translation: AAS56269.1.
BK006945 Genomic DNA. Translation: DAA09511.1.
PIRiS48545.
RefSeqiNP_013293.1. NM_001182079.1.

Genome annotation databases

EnsemblFungiiYLR192C; YLR192C; YLR192C.
GeneIDi850889.
KEGGisce:YLR192C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67433.1.
AY557943 Genomic DNA. Translation: AAS56269.1.
BK006945 Genomic DNA. Translation: DAA09511.1.
PIRiS48545.
RefSeqiNP_013293.1. NM_001182079.1.

3D structure databases

ProteinModelPortaliQ05775.
SMRiQ05775. Positions 138-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31462. 134 interactions.
DIPiDIP-4532N.
IntActiQ05775. 23 interactions.
MINTiMINT-517104.

Proteomic databases

MaxQBiQ05775.
PaxDbiQ05775.
PeptideAtlasiQ05775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR192C; YLR192C; YLR192C.
GeneIDi850889.
KEGGisce:YLR192C.

Organism-specific databases

CYGDiYLR192c.
EuPathDBiFungiDB:YLR192C.
SGDiS000004182. HCR1.

Phylogenomic databases

eggNOGiNOG118058.
HOGENOMiHOG000246847.
InParanoidiQ05775.
KOiK03245.
OMAiNAHPRER.
OrthoDBiEOG76X6BX.

Enzyme and pathway databases

BioCyciYEAST:G3O-32314-MONOMER.

Miscellaneous databases

NextBioi967257.
PROiQ05775.

Family and domain databases

Gene3Di1.10.246.60. 1 hit.
HAMAPiMF_03009. eIF3j.
InterProiIPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view]
PANTHERiPTHR21681. PTHR21681. 1 hit.
PfamiPF08597. eIF3_subunit. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. 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].

Entry informationi

Entry nameiEIF3J_YEAST
AccessioniPrimary (citable) accession number: Q05775
Secondary accession number(s): D6VYJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 17900 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.