ID EIF3J_YEAST Reviewed; 265 AA. AC Q05775; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-MAR-2010, entry version 80. DE RecName: Full=Eukaryotic translation initiation factor 3 subunit J; DE Short=eIF3j; DE AltName: Full=Eukaryotic translation initiation factor 3 30 kDa subunit; DE Short=eIF-3 30 kDa; GN Name=HCR1; OrderedLocusNames=YLR192C; ORFNames=L8167.11; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; OC Saccharomycotina; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313267; PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., RA Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [3] RP CHARACTERIZATION. RX MEDLINE=99419035; PubMed=10488093; DOI=10.1074/jbc.274.39.27567; RA Valasek L., Hasek J., Trachsel H., Imre E.M., Ruis H.; RT "The Saccharomyces cerevisiae HCR1 gene encoding a homologue of the RT p35 subunit of human translation initiation factor 3 (eIF3) is a high RT copy suppressor of a temperature-sensitive mutation in the Rpg1p RT subunit of yeast eIF3."; RL J. Biol. Chem. 274:27567-27572(1999). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP INTERACTION WITH PRT1, ASSOCIATION WITH THE 40S RIBOSOME, DISRUPTION RP PHENOTYPE, AND MUTAGENESIS OF ARG-215. RX PubMed=16581774; DOI=10.1128/MCB.26.8.2984-2998.2006; RA Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.; RT "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding RT of eukaryotic initiation factor 3 in yeast."; RL Mol. Cell. Biol. 26:2984-2998(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND MASS RP SPECTROMETRY. RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS RP SPECTROMETRY. RX PubMed=17563356; DOI=10.1073/pnas.0701622104; RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; RT "Proteome-wide identification of in vivo targets of DNA damage RT checkpoint kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; THR-75 AND SER-189, RP AND MASS SPECTROMETRY. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). CC -!- FUNCTION: Probable component of the eukaryotic translation CC initiation factor 3 (eIF-3) complex, which is involved in protein CC synthesis and, together with other initiation factors, stimulates CC binding of mRNA and methionyl-tRNAi to the 40S ribosome. CC -!- SUBUNIT: Probable component of the eukaryotic translation CC initiation factor 3 (eIF-3) complex. Is not part of the eIF-3 core CC complex, with which it is associated in substochiometric amounts. CC -!- INTERACTION: CC P43582:-; NbExp=1; IntAct=EBI-8944, EBI-22766; CC P22696:ESS1; NbExp=1; IntAct=EBI-8944, EBI-6679; CC P33203:PRP40; NbExp=1; IntAct=EBI-8944, EBI-701; CC Q03195:RLI1; NbExp=1; IntAct=EBI-8944, EBI-35146; CC P39940:RSP5; NbExp=1; IntAct=EBI-8944, EBI-16219; CC P46995:SET2; NbExp=1; IntAct=EBI-8944, EBI-16985; CC Q06525:URN1; NbExp=1; IntAct=EBI-8944, EBI-35138; CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- DISRUPTION PHENOTYPE: Marked reduction in binding of the eIF-3 CC core complex to 40S ribosomes. CC -!- MISCELLANEOUS: Present with 17900 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the eIF-3 subunit J family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U14913; AAB67433.1; -; Genomic_DNA. DR EMBL; AY557943; AAS56269.1; -; Genomic_DNA. DR PIR; S48545; S48545. DR RefSeq; NP_013293.1; -. DR SMR; Q05775; 141-210. DR DIP; DIP-4532N; -. DR IntAct; Q05775; 22. DR MINT; MINT-517104; -. DR STRING; Q05775; -. DR PeptideAtlas; Q05775; -. DR Ensembl; YLR192C; YLR192C; YLR192C; Saccharomyces cerevisiae. DR GeneID; 850889; -. DR GenomeReviews; Y13138_GR; YLR192C. DR KEGG; sce:YLR192C; -. DR NMPDR; fig|4932.3.peg.4303; -. DR CYGD; YLR192c; -. DR SGD; S000004182; HCR1. DR eggNOG; fuNOG09875; -. DR HOGENOM; HBG398276; -. DR OMA; MSWDDED; -. DR OrthoDB; EOG9BVT9V; -. DR PhylomeDB; Q05775; -. DR NextBio; 967257; -. DR ArrayExpress; Q05775; -. DR Genevestigator; Q05775; -. DR GermOnline; YLR192C; Saccharomyces cerevisiae. DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 ...; IPI:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019843; F:rRNA binding; IDA:SGD. DR GO; GO:0003743; F:translation initiation factor activity; IPI:SGD. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rR...; IMP:SGD. DR GO; GO:0006412; P:translation; IPI:SGD. DR InterPro; IPR013906; eIF3_subunit. DR PANTHER; PTHR21681; eIF3_subunit; 1. DR Pfam; PF08597; eIF3_subunit; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein; KW Protein biosynthesis. FT CHAIN 1 265 Eukaryotic translation initiation factor FT 3 subunit J. FT /FTId=PRO_0000123509. FT MOD_RES 64 64 Phosphoserine. FT MOD_RES 65 65 Phosphoserine. FT MOD_RES 75 75 Phosphothreonine. FT MOD_RES 189 189 Phosphoserine. FT MUTAGEN 215 215 R->I: Increased association of the eIF-3 FT complex and 40S ribosomes. SQ SEQUENCE 265 AA; 29564 MW; BDDBC5943DD7F9BB CRC64; MSWDDEAING SMGNDDAVLM DSWDAEIGDD EPVMQSWDAE EEEKKPAPKP KKEQPKKVKK GKESSADRAL LDIDTLDEKT RKELIKKAEM ESDLNNAADL FAGLGVAEEH PRARALQKEQ EEQALKRPAF TKDTPIETHP LFNAETKREY QDLRKALTAA ITPMNKKSPL NYSSSLAIDL IRDVAKPMSI ESIRQTVATL NVLIKDKERE ERQARLARVR GGTATGGAGK KKVKGKTNLG GAFKKDQDFD LDGPDDFEFG DDDFM //