ID IF31_YEAST Reviewed; 265 AA. AC Q05775; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JUL-2007, entry version 53. DE Probable eukaryotic translation initiation factor 3 30 kDa subunit DE (eIF-3 30 kDa) (eIF3j). GN Name=HCR1; OrderedLocusNames=YLR192C; ORFNames=L8167.11; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; 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 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65. 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). 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 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 P43582:YFL010C; NbExp=1; IntAct=EBI-8944, EBI-22766; CC Q06525:YPR152C; NbExp=1; IntAct=EBI-8944, EBI-35138; CC -!- MISCELLANEOUS: Present with 17900 molecules/cell. CC -!- SIMILARITY: Belongs to the eIF-3 subunit 1 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 DIP; DIP:4532N; -. DR IntAct; Q05775; -. DR PeptideAtlas; Q05775; -. DR Ensembl; YLR192C; Saccharomyces cerevisiae. DR GenomeReviews; Y13138_GR; YLR192C. DR KEGG; sce:YLR192C; -. DR CYGD; YLR192c; -. DR SGD; S000004182; HCR1. DR BioCyc; SCER-S28-01:SCER-S28-01-004076-MONOMER; -. DR LinkHub; 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:0030490; P:processing of 20S pre-rRNA; IMP:SGD. DR GO; GO:0000723; P:telomere maintenance; IMP:SGD. DR GO; GO:0006412; P:translation; IPI:SGD. DR InterPro; IPR013906; eIF3_subunit. DR Pfam; PF08597; eIF3_subunit; 1. PE 1: Evidence at protein level; KW Complete proteome; Initiation factor; Phosphorylation; KW Protein biosynthesis. FT CHAIN 1 265 Probable eukaryotic translation FT initiation factor 3 30 kDa subunit. FT /FTId=PRO_0000123509. FT MOD_RES 65 65 Phosphoserine. FT MOD_RES 75 75 Phosphothreonine. 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 //