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 13-SEP-2023, entry version 174. 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; DE AltName: Full=High-copy suppressor of Rpg1 protein 1 {ECO:0000303|PubMed:10488093}; GN Name=HCR1 {ECO:0000255|HAMAP-Rule:MF_03009, ECO:0000303|PubMed:10488093}; GN OrderedLocusNames=YLR192C; ORFNames=L8167.11; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC 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., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., 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., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT 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 p35 RT subunit of human translation initiation factor 3 (eIF3) is a high copy RT suppressor of a temperature-sensitive mutation in the Rpg1p subunit of RT 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., Dephoure N., RA 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 of RT 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 BY RP 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 BY RP 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 phosphoproteome RT 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 insights RT into evolution."; RL Science 325:1682-1686(2009). RN [11] RP METHYLATION AT ARG-220, AND PHOSPHORYLATION AT SER-65 AND THR-75. RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927; RA Hamey J.J., Nguyen A., Wilkins M.R.; RT "Discovery of arginine methylation, phosphorylation, and their co- RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae."; RL J. Proteome Res. 20:2420-2434(2021). RN [12] {ECO:0007744|PDB:6ZCE, ECO:0007744|PDB:7A1G} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS). RX PubMed=33289941; DOI=10.15252/embj.2020105179; RA Kratzat H., Mackens-Kiani T., Ameismeier M., Potocnjak M., Cheng J., RA Dacheux E., Namane A., Berninghausen O., Herzog F., Fromont-Racine M., RA Becker T., Beckmann R.; RT "A structural inventory of native ribosomal ABCE1-43S pre-initiation RT complexes."; RL EMBO J. 40:e105179-e105179(2021). CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3 CC (eIF-3) complex, which is involved in protein synthesis of a CC specialized repertoire of mRNAs and, together with other initiation CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S CC ribosome. The eIF-3 complex specifically targets and initiates CC translation of a subset of mRNAs involved in cell proliferation. CC {ECO:0000255|HAMAP-Rule:MF_03009, ECO:0000269|PubMed:10488093}. CC -!- SUBUNIT: Probable component of the eukaryotic translation initiation CC factor 3 (eIF-3) complex. Is not part of the eIF-3 core complex, with CC which it is associated in substochiometric amounts. CC -!- INTERACTION: CC Q05775; 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 core CC 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. {ECO:0000255|HAMAP- CC 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 PDB; 6ZCE; EM; 5.30 A; s/t=1-265. DR PDB; 7A1G; EM; 3.00 A; y/z=1-265. DR PDBsum; 6ZCE; -. DR PDBsum; 7A1G; -. DR AlphaFoldDB; Q05775; -. DR SMR; Q05775; -. DR BioGRID; 31462; 376. DR DIP; DIP-4532N; -. DR IntAct; Q05775; 24. DR MINT; Q05775; -. DR STRING; 4932.YLR192C; -. DR iPTMnet; Q05775; -. DR MaxQB; Q05775; -. DR PaxDb; Q05775; -. DR PeptideAtlas; Q05775; -. DR EnsemblFungi; YLR192C_mRNA; YLR192C; YLR192C. DR GeneID; 850889; -. DR KEGG; sce:YLR192C; -. DR AGR; SGD:S000004182; -. DR SGD; S000004182; HCR1. DR VEuPathDB; FungiDB:YLR192C; -. DR eggNOG; KOG4813; Eukaryota. DR HOGENOM; CLU_085412_0_0_1; -. DR InParanoid; Q05775; -. DR OMA; MESWDAE; -. DR OrthoDB; 2053540at2759; -. DR BioCyc; YEAST:G3O-32314-MONOMER; -. DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-SCE-72649; Translation initiation complex formation. DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex. DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition. DR BioGRID-ORCS; 850889; 0 hits in 10 CRISPR screens. DR PRO; PR:Q05775; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; Q05775; Protein. DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD. DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule. DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule. 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:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR Gene3D; 1.10.246.60; Eukaryotic translation initiation factor 3 like domains; 1. DR HAMAP; MF_03009; eIF3j; 1. DR InterPro; IPR023194; eIF3-like_dom_sf. DR InterPro; IPR013906; eIF3j. DR PANTHER; PTHR21681; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT J; 1. DR PANTHER; PTHR21681:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT J; 1. DR Pfam; PF08597; eIF3_subunit; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Initiation factor; Methylation; Phosphoprotein; KW Protein biosynthesis; Reference proteome. FT CHAIN 1..265 FT /note="Eukaryotic translation initiation factor 3 subunit FT J" FT /id="PRO_0000123509" FT REGION 1..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 219..265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 22..37 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 57..71 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 65 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 75 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:33856219, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 220 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:33856219" FT MUTAGEN 215 FT /note="R->I: Increased association of the eIF-3 complex and FT 40S ribosomes." FT /evidence="ECO:0000269|PubMed:16581774" FT HELIX 147..161 FT /evidence="ECO:0007829|PDB:7A1G" FT HELIX 162..165 FT /evidence="ECO:0007829|PDB:7A1G" FT HELIX 169..175 FT /evidence="ECO:0007829|PDB:7A1G" FT HELIX 177..185 FT /evidence="ECO:0007829|PDB:7A1G" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:7A1G" FT HELIX 190..218 FT /evidence="ECO:0007829|PDB:7A1G" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:7A1G" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:7A1G" 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 //