Q05775 (EIF3J_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	265 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP-Rule MF_03009
Sequence similarities	Belongs to the eIF-3 subunit J family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytoplasmic translation Inferred from physical interaction PubMed 11179233. Source: SGD maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from mutant phenotype PubMed 11560931. Source: SGD
Cellular_component	eukaryotic translation initiation factor 3 complex Inferred from physical interaction PubMed 11179233. Source: SGD
Molecular_function	translation initiation factor activity Inferred from physical interaction PubMed 11179233. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 265	265	Eukaryotic translation initiation factor 3 subunit J HAMAP-Rule MF_03009		PRO_0000123509
Amino acid modifications
	Modified residue	64	1	Phosphoserine Ref.10
	Modified residue	65	1	Phosphoserine Ref.9
	Modified residue	75	1	Phosphothreonine Ref.8 Ref.10
	Modified residue	189	1	Phosphoserine Ref.10
Experimental info
	Mutagenesis	215	1	R → I: Increased association of the eIF-3 complex and 40S ribosomes. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q05775 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BDDBC5943DD7F9BB	FASTA	265	29,564
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[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. , 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, MASS SPECTROMETRY. Strain: ADR376.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY.
[10]	"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 SER-64; THR-75 AND SER-189, MASS SPECTROMETRY.
+	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.
PIR	S48545.
RefSeq	NP_013293.1. NM_001182079.1.
3D structure databases
ProteinModelPortal	Q05775.
SMR	Q05775. Positions 138-213.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4532N.
IntAct	Q05775. 23 interactions.
MINT	MINT-517104.
STRING	4932.YLR192C.
Proteomic databases
PaxDb	Q05775.
PeptideAtlas	Q05775.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR192C; YLR192C; YLR192C.
GeneID	850889.
KEGG	sce:YLR192C.
Organism-specific databases
CYGD	YLR192c.
SGD	S000004182. HCR1.
Phylogenomic databases
eggNOG	NOG118058.
GeneTree	ENSGT00390000018400.
HOGENOM	HOG000246847.
KO	K03245.
OMA	HPLFQPT.
OrthoDB	EOG47DDRP.
Gene expression databases
Genevestigator	Q05775.
GermOnline	YLR192C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.246.60. 1 hit.
HAMAP	MF_03009. eIF3j.
InterPro	IPR023194. eIF3-like_dom. IPR013906. eIF3_subunit. [Graphical view]
PANTHER	PTHR21681. PTHR21681. 1 hit.
Pfam	PF08597. eIF3_subunit. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967257.

Entry information

Entry name

EIF3J_YEAST

Accession

Primary (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:	April 3, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program