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 10-MAY-2017, entry version 128. DE RecName: Full=Enhancer of polycomb-like protein 1; GN Name=EPL1; OrderedLocusNames=YFL024C; 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=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; 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 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 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 IDENTIFICATION BY RP 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 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 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 IDENTIFICATION BY MASS RP 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 IDENTIFICATION BY RP 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 IDENTIFICATION BY MASS RP 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). 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. {ECO:0000269|PubMed:10911987, CC ECO:0000269|PubMed:12782659, ECO:0000269|PubMed:14966276, CC ECO:0000269|PubMed:15045029}. 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 {ECO:0000269|PubMed:10911987, ECO:0000269|PubMed:12782659, CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15353583, CC ECO:0000269|PubMed:15485911}. CC -!- INTERACTION: CC P38806:YNG2; NbExp=8; IntAct=EBI-22792, EBI-24622; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 1110 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the enhancer of polycomb family. CC {ECO:0000305}. 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 RefSeq; NP_116629.1; NM_001179942.1. DR PDB; 5J9Q; X-ray; 3.25 A; C/G/N=50-400. DR PDB; 5J9T; X-ray; 2.70 A; C/G/K=121-400. DR PDB; 5J9U; X-ray; 2.95 A; C/G/N=50-400. DR PDB; 5J9W; X-ray; 2.80 A; C/G/K=121-400. DR PDBsum; 5J9Q; -. DR PDBsum; 5J9T; -. DR PDBsum; 5J9U; -. DR PDBsum; 5J9W; -. DR ProteinModelPortal; P43572; -. DR SMR; P43572; -. DR BioGrid; 31122; 198. DR DIP; DIP-5904N; -. DR IntAct; P43572; 32. DR MINT; MINT-624154; -. DR iPTMnet; P43572; -. DR MaxQB; P43572; -. DR PRIDE; P43572; -. DR EnsemblFungi; BAA09214; BAA09214; BAA09214. DR EnsemblFungi; YFL024C; YFL024C; YFL024C. DR GeneID; 850520; -. DR KEGG; sce:YFL024C; -. DR EuPathDB; FungiDB:YFL024C; -. DR SGD; S000001870; EPL1. DR GeneTree; ENSGT00390000013262; -. DR HOGENOM; HOG000094341; -. DR InParanoid; P43572; -. DR KO; K11322; -. DR OMA; NMDERDE; -. DR OrthoDB; EOG092C0XUA; -. DR BioCyc; YEAST:G3O-30436-MONOMER; -. DR PRO; PR:P43572; -. DR Proteomes; UP000002311; Chromosome VI. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD. DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:SGD. 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:0016239; P:positive regulation of macroautophagy; IMP:SGD. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:SGD. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR024943; Enhancer_polycomb. DR InterPro; IPR019542; Enhancer_polycomb-like_N. DR PANTHER; PTHR14898; PTHR14898; 1. DR Pfam; PF10513; EPL1; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Complete proteome; KW Direct protein sequencing; DNA damage; DNA repair; Nucleus; KW Reference proteome; Transcription; 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 STRAND 65 68 {ECO:0000244|PDB:5J9U}. FT STRAND 71 75 {ECO:0000244|PDB:5J9U}. FT STRAND 121 123 {ECO:0000244|PDB:5J9U}. FT HELIX 133 136 {ECO:0000244|PDB:5J9T}. FT HELIX 155 157 {ECO:0000244|PDB:5J9T}. FT HELIX 166 174 {ECO:0000244|PDB:5J9T}. FT STRAND 177 179 {ECO:0000244|PDB:5J9T}. FT HELIX 186 203 {ECO:0000244|PDB:5J9T}. FT HELIX 207 209 {ECO:0000244|PDB:5J9T}. FT HELIX 211 213 {ECO:0000244|PDB:5J9T}. FT HELIX 217 226 {ECO:0000244|PDB:5J9T}. FT HELIX 229 231 {ECO:0000244|PDB:5J9T}. FT HELIX 232 241 {ECO:0000244|PDB:5J9T}. FT HELIX 256 260 {ECO:0000244|PDB:5J9T}. FT HELIX 264 285 {ECO:0000244|PDB:5J9T}. FT TURN 286 288 {ECO:0000244|PDB:5J9T}. FT STRAND 300 302 {ECO:0000244|PDB:5J9W}. FT STRAND 310 313 {ECO:0000244|PDB:5J9U}. FT HELIX 324 382 {ECO:0000244|PDB:5J9T}. FT HELIX 388 391 {ECO:0000244|PDB:5J9W}. 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 //