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 29-SEP-2021, entry version 157. 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; 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=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT 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., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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; 575-587; RP 594-600; 605-612; 617-632; 653-698; 711-721; 729-740; 772-794 AND 811-821, RP 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., Allard S., RA 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., Brock H.W.; RT "The enhancer of polycomb gene of Drosophila encodes a chromatin protein RT conserved in yeast and mammals."; RL Development 125:4055-4066(1998). RN [5] RP FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12782659; DOI=10.1101/gad.1056603; RA Boudreault A.A., Cronier D., Selleck W., Lacoste N., Utley R.T., Allard S., RA Savard J., Lane W.S., Tan S., Cote J.; RT "Yeast enhancer of polycomb defines global Esa1-dependent acetylation of RT chromatin."; RL Genes Dev. 17:1415-1428(2003). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3; RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M., RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E., RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.; RT "Assigning function to yeast proteins by integration of technologies."; RL Mol. Cell 12:1353-1365(2003). RN [7] 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 [8] 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 [9] 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 [10] 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., Erdjument-Bromage H., RA Tempst P., Cote J., Cairns B.R.; RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for proper RT gene expression, histone H4 acetylation, and Htz1 replacement near RT telomeres."; RL Mol. Cell. Biol. 24:9424-9436(2004). RN [11] RP FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS RP 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 Swr1p RT deposits histone variant H2A.Z into euchromatin."; RL PLoS Biol. 2:587-599(2004). RN [12] 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, the RT Swr1 chromatin remodeling complex, and the histone acetyltransferase RT NuA4."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004). CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which CC is involved in transcriptional activation of selected genes principally CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is CC also involved in DNA repair. Involved in gene silencing by neighboring CC heterochromatin, blockage of the silencing spreading along the CC chromosome, and required for cell cycle progression through G2/M. CC {ECO:0000269|PubMed:10911987, ECO:0000269|PubMed:12782659, CC ECO:0000269|PubMed:14966276, 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, EAF6, CC EAF7, EPL1, ESA1, TRA1 and YNG2. {ECO:0000269|PubMed:10911987, CC ECO:0000269|PubMed:12782659, ECO:0000269|PubMed:15045029, CC ECO:0000269|PubMed:15353583, ECO:0000269|PubMed:15485911}. CC -!- INTERACTION: CC P43572; P38806: YNG2; NbExp=10; IntAct=EBI-22792, EBI-24622; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 1110 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the enhancer of polycomb family. {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 SMR; P43572; -. DR BioGRID; 31122; 206. DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex. DR ComplexPortal; CPX-3185; Piccolo NuA4 histone acetyltransferase complex. DR DIP; DIP-5904N; -. DR IntAct; P43572; 32. DR MINT; P43572; -. DR STRING; 4932.YFL024C; -. DR iPTMnet; P43572; -. DR MaxQB; P43572; -. DR PaxDb; P43572; -. DR PRIDE; P43572; -. DR EnsemblFungi; YFL024C_mRNA; YFL024C; YFL024C. DR GeneID; 850520; -. DR KEGG; sce:YFL024C; -. DR SGD; S000001870; EPL1. DR VEuPathDB; FungiDB:YFL024C; -. DR eggNOG; KOG2261; Eukaryota. DR GeneTree; ENSGT00940000171678; -. DR HOGENOM; CLU_010580_0_0_1; -. DR InParanoid; P43572; -. DR OMA; DPYNPVF; -. DR PRO; PR:P43572; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P43572; protein. 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 by RNA polymerase II; IDA:SGD. 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; Direct protein sequencing; DNA damage; KW DNA repair; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..832 FT /note="Enhancer of polycomb-like protein 1" FT /id="PRO_0000214167" FT REGION 1..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 422..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 776..832 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..37 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 441..483 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:5J9U" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:5J9U" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:5J9U" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 166..174 FT /evidence="ECO:0007829|PDB:5J9T" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 186..203 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 217..226 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 232..241 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 256..260 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 264..285 FT /evidence="ECO:0007829|PDB:5J9T" FT TURN 286..288 FT /evidence="ECO:0007829|PDB:5J9T" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:5J9W" FT STRAND 310..313 FT /evidence="ECO:0007829|PDB:5J9U" FT HELIX 324..382 FT /evidence="ECO:0007829|PDB:5J9T" FT HELIX 388..391 FT /evidence="ECO:0007829|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 //