ID EIF3J_YEAST Reviewed; 265 AA. AC Q05775; D6VYJ5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 02-NOV-2016, entry version 132. DE RecName: Full=Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009}; DE Short=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009}; DE AltName: Full=Eukaryotic translation initiation factor 3 30 kDa subunit; DE Short=eIF-3 30 kDa; GN Name=HCR1 {ECO:0000255|HAMAP-Rule:MF_03009}; GN OrderedLocusNames=YLR192C; ORFNames=L8167.11; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX 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 GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] 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 [4] RP FUNCTION. RX 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 [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX 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 [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75 AND SER-92, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides RT insights into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Component of the eukaryotic translation initiation CC factor 3 (eIF-3) complex, which is involved in protein synthesis CC of a specialized repertoire of mRNAs and, together with other CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi CC to the 40S ribosome. The eIF-3 complex specifically targets and CC initiates translation of a subset of mRNAs involved in cell CC proliferation. {ECO:0000255|HAMAP-Rule:MF_03009, CC ECO:0000269|PubMed:10488093}. 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 Q03195:RLI1; NbExp=4; IntAct=EBI-8944, EBI-35146; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009, CC ECO:0000269|PubMed:14562095}. CC -!- DISRUPTION PHENOTYPE: Marked reduction in binding of the eIF-3 CC core complex to 40S ribosomes. {ECO:0000269|PubMed:16581774}. CC -!- MISCELLANEOUS: Present with 17900 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the eIF-3 subunit J family. CC {ECO:0000255|HAMAP-Rule:MF_03009}. 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 EMBL; BK006945; DAA09511.1; -; Genomic_DNA. DR PIR; S48545; S48545. DR RefSeq; NP_013293.1; NM_001182079.1. DR ProteinModelPortal; Q05775; -. DR BioGrid; 31462; 137. DR DIP; DIP-4532N; -. DR IntAct; Q05775; 24. DR MINT; MINT-517104; -. DR iPTMnet; Q05775; -. DR MaxQB; Q05775; -. DR PRIDE; Q05775; -. DR EnsemblFungi; YLR192C; YLR192C; YLR192C. DR GeneID; 850889; -. DR KEGG; sce:YLR192C; -. DR EuPathDB; FungiDB:YLR192C; -. DR SGD; S000004182; HCR1. DR HOGENOM; HOG000246847; -. DR InParanoid; Q05775; -. DR KO; K03245; -. DR OMA; INAHPRE; -. DR OrthoDB; EOG092C4T6B; -. DR BioCyc; YEAST:G3O-32314-MONOMER; -. DR PRO; PR:Q05775; -. DR Proteomes; UP000002311; Chromosome XII. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD. DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP. DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IPI:SGD. DR GO; GO:0003743; F:translation initiation factor activity; IPI:SGD. DR GO; GO:0002181; P:cytoplasmic translation; IPI:SGD. DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.246.60; -; 1. DR HAMAP; MF_03009; eIF3j; 1. DR InterPro; IPR023194; eIF3-like_dom. DR InterPro; IPR013906; eIF3j. DR Pfam; PF08597; eIF3_subunit; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 265 Eukaryotic translation initiation factor FT 3 subunit J. FT /FTId=PRO_0000123509. FT MOD_RES 75 75 Phosphothreonine. FT {ECO:0000244|PubMed:17330950, FT ECO:0000244|PubMed:18407956, FT ECO:0000244|PubMed:19779198}. FT MOD_RES 92 92 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT MUTAGEN 215 215 R->I: Increased association of the eIF-3 FT complex and 40S ribosomes. FT {ECO:0000269|PubMed:16581774}. 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 //