EPC1_HUMAN
ID EPC1_HUMAN Reviewed; 836 AA.
AC Q9H2F5; B4DSC3; D3DRX7; Q5VW54; Q5VW56; Q5VW58; Q8NAQ4; Q8NE21; Q96LF4;
AC Q96RR6; Q9H7T7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Enhancer of polycomb homolog 1 {ECO:0000305};
GN Name=EPC1 {ECO:0000303|PubMed:10976108, ECO:0000312|HGNC:HGNC:19876};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH TRIM27.
RX PubMed=10976108; DOI=10.1074/jbc.m006585200;
RA Shimono Y., Murakami H., Hasegawa Y., Takahashi M.;
RT "RET finger protein is a transcriptional repressor and interacts with
RT enhancer of polycomb that has dual transcriptional functions.";
RL J. Biol. Chem. 275:39411-39419(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Nunes D.N., Dias-Neto E., Brentani R.R., Camargo A.A.;
RT "Cloning and characterization of two human homologs of the enhancer of
RT polycomb gene (EPC1) from Drosophila.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 58-68 AND 802-813, IDENTIFICATION IN NUA4 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12963728; DOI=10.1074/jbc.c300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-
RT containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [8]
RP REVIEW ON NUA4 COMPLEX.
RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
RA Doyon Y., Cote J.;
RT "The highly conserved and multifunctional NuA4 HAT complex.";
RL Curr. Opin. Genet. Dev. 14:147-154(2004).
RN [9]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
RP COMPLEX, AND IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION IN NUA4 COMPLEX.
RX PubMed=27153538; DOI=10.1016/j.molcel.2016.03.031;
RA Jacquet K., Fradet-Turcotte A., Avvakumov N., Lambert J.P., Roques C.,
RA Pandita R.K., Paquet E., Herst P., Gingras A.C., Pandita T.K., Legube G.,
RA Doyon Y., Durocher D., Cote J.;
RT "The TIP60 complex regulates bivalent chromatin recognition by 53BP1
RT through direct H4K20me binding and H2AK15 acetylation.";
RL Mol. Cell 62:409-421(2016).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-319 AND LYS-673, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15] {ECO:0007744|PDB:6NFX}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 644-671 IN COMPLEX WITH MBTD1,
RP FUNCTION, IDENTIFICATION IN NUA4 COMPLEX, INTERACTION WITH MBTD1, AND
RP MUTAGENESIS OF LEU-651 AND 659-ALA--LEU-663.
RX PubMed=32209463; DOI=10.1016/j.celrep.2020.03.003;
RA Zhang H., Devoucoux M., Song X., Li L., Ayaz G., Cheng H., Tempel W.,
RA Dong C., Loppnau P., Cote J., Min J.;
RT "Structural basis for EPC1-mediated recruitment of MBTD1 into the
RT NuA4/TIP60 acetyltransferase complex.";
RL Cell Rep. 30:3996-4002(2020).
RN [16]
RP VARIANT LEU-123.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase (HAT)
CC complex, a multiprotein complex involved in transcriptional activation
CC of select genes principally by acetylation of nucleosomal histones H4
CC and H2A (PubMed:14966270). The NuA4 complex plays a direct role in
CC repair of DNA double-strand breaks (DSBs) by promoting homologous
CC recombination (HR) (PubMed:27153538). The NuA4 complex is also required
CC for spermatid development by promoting acetylation of histones: histone
CC acetylation is required for histone replacement during the transition
CC from round to elongating spermatids (By similarity). In the NuA4
CC complex, EPC1 is required to recruit MBTD1 into the complex
CC (PubMed:32209463). {ECO:0000250|UniProtKB:Q8C9X6,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:27153538,
CC ECO:0000269|PubMed:32209463}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41, VPS72/YL1 and MEAF6 (PubMed:12963728, PubMed:14966270,
CC PubMed:27153538, PubMed:32209463). KAT5/TIP60, EPC1, and ING3 together
CC constitute a minimal HAT complex termed Piccolo NuA4 (PubMed:14966270).
CC Component of a NuA4-related complex which contains EP400, TRRAP/PAF400,
CC SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin,
CC ACTL6A/BAF53A, VPS72 and YEATS4/GAS41 (PubMed:14966270). Interacts with
CC TRIM27 (PubMed:10976108). Interacts with MBTD1; interaction is direct
CC and promotes recruitment of MBTD1 into the NuA4 histone
CC acetyltransferase complex (PubMed:32209463).
CC {ECO:0000269|PubMed:10976108, ECO:0000269|PubMed:12963728,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:27153538,
CC ECO:0000269|PubMed:32209463}.
CC -!- INTERACTION:
CC Q9H2F5; Q9H0E9: BRD8; NbExp=5; IntAct=EBI-769270, EBI-769266;
CC Q9H2F5; P19012: KRT15; NbExp=3; IntAct=EBI-769270, EBI-739566;
CC Q9H2F5; Q05BQ5: MBTD1; NbExp=6; IntAct=EBI-769270, EBI-5666902;
CC Q9H2F5; Q6NUQ1: RINT1; NbExp=5; IntAct=EBI-769270, EBI-726876;
CC Q9H2F5-2; Q92993: KAT5; NbExp=3; IntAct=EBI-11023729, EBI-399080;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10976108}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8C9X6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H2F5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2F5-2; Sequence=VSP_012877;
CC Name=3;
CC IsoId=Q9H2F5-3; Sequence=VSP_012875, VSP_012877;
CC -!- SIMILARITY: Belongs to the enhancer of polycomb family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14888.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC03857.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; AF277374; AAG41402.1; -; mRNA.
DR EMBL; AF286905; AAK60501.1; -; mRNA.
DR EMBL; AK024329; BAB14888.1; ALT_INIT; mRNA.
DR EMBL; AK092304; BAC03857.1; ALT_SEQ; mRNA.
DR EMBL; AK299676; BAG61585.1; -; mRNA.
DR EMBL; AL158834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW85972.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85973.1; -; Genomic_DNA.
DR EMBL; BC036529; AAH36529.1; -; mRNA.
DR CCDS; CCDS60511.1; -. [Q9H2F5-2]
DR CCDS; CCDS7172.1; -. [Q9H2F5-1]
DR CCDS; CCDS73083.1; -. [Q9H2F5-3]
DR RefSeq; NP_001258933.1; NM_001272004.1. [Q9H2F5-2]
DR RefSeq; NP_001258948.1; NM_001272019.2.
DR RefSeq; NP_001269320.1; NM_001282391.1. [Q9H2F5-3]
DR RefSeq; NP_079485.1; NM_025209.3. [Q9H2F5-1]
DR PDB; 6NFX; X-ray; 1.95 A; A=644-671.
DR PDBsum; 6NFX; -.
DR AlphaFoldDB; Q9H2F5; -.
DR SMR; Q9H2F5; -.
DR BioGRID; 123227; 74.
DR ComplexPortal; CPX-709; Piccolo NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q9H2F5; -.
DR IntAct; Q9H2F5; 51.
DR MINT; Q9H2F5; -.
DR STRING; 9606.ENSP00000263062; -.
DR GlyGen; Q9H2F5; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9H2F5; -.
DR PhosphoSitePlus; Q9H2F5; -.
DR SwissPalm; Q9H2F5; -.
DR BioMuta; EPC1; -.
DR DMDM; 59797889; -.
DR EPD; Q9H2F5; -.
DR jPOST; Q9H2F5; -.
DR MassIVE; Q9H2F5; -.
DR MaxQB; Q9H2F5; -.
DR PaxDb; Q9H2F5; -.
DR PeptideAtlas; Q9H2F5; -.
DR PRIDE; Q9H2F5; -.
DR ProteomicsDB; 80540; -. [Q9H2F5-1]
DR ProteomicsDB; 80541; -. [Q9H2F5-2]
DR ProteomicsDB; 80542; -. [Q9H2F5-3]
DR Antibodypedia; 26401; 91 antibodies from 20 providers.
DR DNASU; 80314; -.
DR Ensembl; ENST00000263062.8; ENSP00000263062.8; ENSG00000120616.16. [Q9H2F5-1]
DR Ensembl; ENST00000319778.11; ENSP00000318559.6; ENSG00000120616.16. [Q9H2F5-2]
DR Ensembl; ENST00000375110.6; ENSP00000364251.2; ENSG00000120616.16. [Q9H2F5-3]
DR GeneID; 80314; -.
DR KEGG; hsa:80314; -.
DR MANE-Select; ENST00000319778.11; ENSP00000318559.6; NM_001272004.3; NP_001258933.1. [Q9H2F5-2]
DR UCSC; uc001iwg.3; human. [Q9H2F5-1]
DR CTD; 80314; -.
DR DisGeNET; 80314; -.
DR GeneCards; EPC1; -.
DR HGNC; HGNC:19876; EPC1.
DR HPA; ENSG00000120616; Tissue enriched (bone).
DR MIM; 610999; gene.
DR neXtProt; NX_Q9H2F5; -.
DR OpenTargets; ENSG00000120616; -.
DR PharmGKB; PA134981141; -.
DR VEuPathDB; HostDB:ENSG00000120616; -.
DR eggNOG; KOG2261; Eukaryota.
DR GeneTree; ENSGT00940000155003; -.
DR HOGENOM; CLU_012781_0_0_1; -.
DR InParanoid; Q9H2F5; -.
DR OMA; MMEREDA; -.
DR OrthoDB; 957492at2759; -.
DR PhylomeDB; Q9H2F5; -.
DR TreeFam; TF106438; -.
DR PathwayCommons; Q9H2F5; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q9H2F5; -.
DR BioGRID-ORCS; 80314; 74 hits in 1083 CRISPR screens.
DR ChiTaRS; EPC1; human.
DR GeneWiki; EPC1; -.
DR GenomeRNAi; 80314; -.
DR Pharos; Q9H2F5; Tbio.
DR PRO; PR:Q9H2F5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H2F5; protein.
DR Bgee; ENSG00000120616; Expressed in colonic epithelium and 197 other tissues.
DR ExpressionAtlas; Q9H2F5; baseline and differential.
DR Genevisible; Q9H2F5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0140463; F:chromatin-protein adaptor; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; TAS:UniProtKB.
DR InterPro; IPR024943; Enhancer_polycomb.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR009607; Enhancer_polycomb_C.
DR PANTHER; PTHR14898; PTHR14898; 1.
DR Pfam; PF06752; E_Pc_C; 1.
DR Pfam; PF10513; EPL1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Differentiation; Direct protein sequencing; Growth regulation;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..836
FT /note="Enhancer of polycomb homolog 1"
FT /id="PRO_0000214153"
FT REGION 335..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 319
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 673
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..51
FT /note="MSKLSFRARALDASKPLPVFRCEDLPDLHEYASINRAVPQMPTGMEKEEES
FT -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_012875"
FT VAR_SEQ 621..643
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_012877"
FT VARIANT 123
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:25787250"
FT /id="VAR_074181"
FT MUTAGEN 651
FT /note="L->D: Abolished interaction with MBTD1; when
FT associated with D-660--663-D."
FT /evidence="ECO:0000269|PubMed:32209463"
FT MUTAGEN 659..663
FT /note="AASAL->DASAD: Abolished interaction with MBTD1; when
FT associated with D-651."
FT /evidence="ECO:0000269|PubMed:32209463"
FT CONFLICT 156
FT /note="S -> G (in Ref. 2; AAK60501)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="K -> R (in Ref. 2; AAK60501)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="A -> V (in Ref. 6; AAH36529)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="N -> S (in Ref. 3; BAC03857)"
FT /evidence="ECO:0000305"
FT HELIX 653..660
FT /evidence="ECO:0007829|PDB:6NFX"
SQ SEQUENCE 836 AA; 93463 MW; E9E89699E73336B5 CRC64;
MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS
AQQVYGEKRD NMVIPVPEAE SNIAYYESIY PGEFKMPKQL IHIQPFSLDA EQPDYDLDSE
DEVFVNKLKK KMDICPLQFE EMIDRLEKGS GQQPVSLQEA KLLLKEDDEL IREVYEYWIK
KRKNCRGPSL IPSVKQEKRD GSSTNDPYVA FRRRTEKMQT RKNRKNDEAS YEKMLKLRRD
LSRAVTILEM IKRREKSKRE LLHLTLEIME KRYNLGDYNG EIMSEVMAQR QPMKPTYAIP
IIPITNSSQF KHQEAMDVKE FKVNKQDKAD LIRPKRKYEK KPKVLPSSAA ATPQQTSPAA
LPVFNAKDLN QYDFPSSDEE PLSQVLSGSS EAEEDNDPDG PFAFRRKAGC QYYAPHLDQT
GNWPWTSPKD GGLGDVRYRY CLTTLTVPQR CIGFARRRVG RGGRVLLDRA HSDYDSVFHH
LDLEMLSSPQ HSPVNQFANT SETNTSDKSF SKDLSQILVN IKSCRWRHFR PRTPSLHDSD
NDELSCRKLY RSINRTGTAQ PGTQTCSTST QSKSSSGSAH FAFTAEQYQQ HQQQLALMQK
QQLAQIQQQQ ANSNSSTNTS QNLASNQQKS GFRLNIQGLE RTLQGFVSKT LDSASAQFAA
SALVTSEQLM GFKMKDDVVL GIGVNGVLPA SGVYKGLHLS STTPTALVHT SPSTAGSALL
QPSNITQTSS SHSALSHQVT AANSATTQVL IGNNIRLTVP SSVATVNSIA PINARHIPRT
LSAVPSSALK LAAAANCQVS KVPSSSSVDS VPRENHESEK PALNNIADNT VAMEVT
