ID EPL1_YEAST Reviewed; 832 AA. AC P43572; D6VTK6; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 08-MAR-2011, entry version 77. DE RecName: Full=Enhancer of polycomb-like protein 1; GN Name=EPL1; OrderedLocusNames=YFL024C; 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=95400292; PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., RA Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., RA Yamazaki M., Tashiro H., Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from RT Saccharomyces cerevisiae."; RL Nat. Genet. 10:261-268(1995). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 2-16; 86-96; 101-116; 136-149; 151-178; 227-235; RP 275-280; 283-296; 346-367; 381-407; 471-491; 497-512; 529-569; RP 575-587; 594-600; 605-612; 617-632; 653-698; 711-721; 729-740; 772-794 RP AND 811-821, IDENTIFICATION IN THE NUA4 COMPLEX, AND FUNCTION. RX PubMed=10911987; DOI=10.1016/S1097-2765(00)80258-0; RA Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L., RA Allard S., Savard J., Lane W.S., Stillman D.J., Cote J.; RT "Multiple links between the NuA4 histone acetyltransferase complex and RT epigenetic control of transcription."; RL Mol. Cell 5:927-937(2000). RN [4] RP GENE NAME. RX MEDLINE=98407961; PubMed=9735366; RA Stankunas K., Berger J., Ruse C., Sinclair D.A.R., Randazzo F., RA Brock H.W.; RT "The enhancer of polycomb gene of Drosophila encodes a chromatin RT protein conserved in yeast and mammals."; RL Development 125:4055-4066(1998). RN [5] RP FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY. RX PubMed=12782659; DOI=10.1101/gad.1056603; RA Boudreault A.A., Cronier D., Selleck W., Lacoste N., Utley R.T., RA Allard S., Savard J., Lane W.S., Tan S., Cote J.; RT "Yeast enhancer of polycomb defines global Esa1-dependent acetylation RT of chromatin."; RL Genes Dev. 17:1415-1428(2003). RN [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; 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 [7] 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 [8] RP FUNCTION. RX PubMed=14966276; DOI=10.1128/MCB.24.5.1956-1967.2004; RA Oki M., Valenzuela L., Chiba T., Ito T., Kamakaka R.T.; RT "Barrier proteins remodel and modify chromatin to restrict silenced RT domains."; RL Mol. Cell. Biol. 24:1956-1967(2004). RN [9] RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY. RX PubMed=15485911; DOI=10.1128/MCB.24.21.9424-9436.2004; RA Zhang H., Richardson D.O., Roberts D.N., Utley R.T., RA Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R.; RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for RT proper gene expression, histone H4 acetylation, and Htz1 replacement RT near telomeres."; RL Mol. Cell. Biol. 24:9424-9436(2004). RN [10] RP FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY. RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131; RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., RA Jennings J.L., Link A.J., Madhani H.D., Rine J.; RT "A protein complex containing the conserved Swi2/Snf2-related ATPase RT Swr1p deposits histone variant H2A.Z into euchromatin."; RL PLoS Biol. 2:587-599(2004). RN [11] RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY. RX PubMed=15353583; DOI=10.1073/pnas.0405753101; RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., RA Buratowski S., Hieter P., Greenblatt J.F.; RT "Regulation of chromosome stability by the histone H2A variant Htz1, RT the Swr1 chromatin remodeling complex, and the histone RT acetyltransferase NuA4."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-51, 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). CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex CC which is involved in transcriptional activation of selected genes CC principally by acetylation of nucleosomal histone H4 and H2A. The CC NuA4 complex is also involved in DNA repair. Involved in gene CC silencing by neighboring heterochromatin, blockage of the CC silencing spreading along the chromosome, and required for cell CC cycle progression through G2/M. CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex CC composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, CC EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. CC -!- INTERACTION: CC P38800:-; NbExp=1; IntAct=EBI-22792, EBI-24597; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 1110 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the enhancer of polycomb 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; D50617; BAA09214.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12416.1; -; Genomic_DNA. DR PIR; S56230; S56230. DR ProteinModelPortal; P43572; -. DR DIP; DIP-5904N; -. DR IntAct; P43572; 70. DR MINT; MINT-624154; -. DR STRING; P43572; -. DR PeptideAtlas; P43572; -. DR PRIDE; P43572; -. DR EnsemblFungi; YFL024C; YFL024C; YFL024C. DR GenomeReviews; D50617_GR; YFL024C. DR NMPDR; fig|4932.3.peg.2256; -. DR CYGD; YFL024c; -. DR SGD; S000001870; EPL1. DR eggNOG; fuNOG05193; -. DR GeneTree; EFGT00050000002714; -. DR HOGENOM; HBG398278; -. DR OMA; FRQRKIS; -. DR OrthoDB; EOG45TGWG; -. DR PhylomeDB; P43572; -. DR NextBio; 966251; -. DR ArrayExpress; P43572; -. DR Genevestigator; P43572; -. DR GermOnline; YFL024C; Saccharomyces cerevisiae. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IPI:SGD. DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IDA:SGD. DR GO; GO:0016573; P:histone acetylation; IDA:SGD. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:SGD. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR019542; Enhancer_of_polycomb-like_N. DR Pfam; PF10513; EPL1; 1. PE 1: Evidence at protein level; KW Cell cycle; Complete proteome; Direct protein sequencing; DNA damage; KW DNA repair; Nucleus; Phosphoprotein; Transcription; KW Transcription regulation. FT CHAIN 1 832 Enhancer of polycomb-like protein 1. FT /FTId=PRO_0000214167. FT COMPBIAS 419 428 Poly-Ala. FT COMPBIAS 447 451 Poly-Gln. FT COMPBIAS 454 461 Poly-Gln. FT COMPBIAS 476 481 Poly-Ser. FT COMPBIAS 777 795 Poly-Gln. FT MOD_RES 42 42 Phosphoserine. FT MOD_RES 51 51 Phosphoserine. SQ SEQUENCE 832 AA; 96738 MW; E08689465F84ABA8 CRC64; MPTPSNAIEI NDGSHKSGRS TRRSGSRSAH DDGLDSFSKG DSGAGASAGS SNSRFRHRKI SVKQHLKIYL PNDLKHLDKD ELQQREVVEI ETGVEKNEEK EVHLHRILQM GSGHTKHKDY IPTPDASMTW NEYDKFYTGS FQETTSYIKF SATVEDCCGT NYNMDERDET FLNEQVNKGS SDILTEDEFE ILCSSFEHAI HERQPFLSMD PESILSFEEL KPTLIKSDMA DFNLRNQLNH EINSHKTHFI TQFDPVSQMN TRPLIQLIEK FGSKIYDYWR ERKIEVNGYE IFPQLKFERP GEKEEIDPYV CFRRREVRHP RKTRRIDILN SQRLRALHQE LKNAKDLALL VAKRENVSLN WINDELKIFD QRVKIKNLKR SLNISGEDDD LINHKRKRPT IVTVEQREAE LRKAELKRAA AAAAAAKAKN NKRNNQLEDK SSRLTKQQQQ QLLQQQQQQQ QNALKTENGK QLANASSSST SQPITSHVYV KLPSSKIPDI VLEDVDALLN SKEKNARKFV QEKMEKRKIE DADVFFNLTD DPFNPVFDMS LPKNFSTSNV PFASIASSKF QIDRSFYSSH LPEYLKGISD DIRIYDSNGR SRNKDNYNLD TKRIKKTELY DPFQENLEIH SREYPIKFRK RVGRSNIKYV DRMPNFTTSS TKSACSLMDF VDFDSIEKEQ YSREGSNDTD SINVYDSKYD EFVRLYDKWK YDSPQNEYGI KFSDEPARLN QISNDTQVIR FGTMLGTKSY EQLREATIKY RRDYITRLKQ KHIQHLQQQQ QQQQQQQQQA QQQKQKSQNN NSNSSNSLKK LNDSLINSEA KQNSSITQKN SS //