EPL1_YEAST
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 03-AUG-2022, entry version 160.
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; DOI=10.1242/dev.125.20.4055;
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}.
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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 AlphaFoldDB; P43572; -.
DR SMR; P43572; -.
DR BioGRID; 31122; 207.
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; TYIKFSA; -.
DR BioCyc; YEAST:G3O-30436-MON; -.
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:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
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 GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
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
