EPC1_MOUSE
ID EPC1_MOUSE Reviewed; 813 AA.
AC Q8C9X6; B2RRY2; Q9Z299;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Enhancer of polycomb homolog 1 {ECO:0000305};
GN Name=Epc1 {ECO:0000303|PubMed:9735366, ECO:0000312|MGI:MGI:1278322};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=28694333; DOI=10.1128/mcb.00082-17;
RA Dong Y., Isono K.I., Ohbo K., Endo T.A., Ohara O., Maekawa M., Toyama Y.,
RA Ito C., Toshimori K., Helin K., Ogonuki N., Inoue K., Ogura A.,
RA Yamagata K., Kitabayashi I., Koseki H.;
RT "EPC1/TIP60-mediated histone acetylation facilitates spermiogenesis in
RT mice.";
RL Mol. Cell. Biol. 37:0-0(2017).
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:28694333). The NuA4 complex plays a direct role in
CC repair of DNA double-strand breaks (DSBs) by promoting homologous
CC recombination (HR) (By similarity). 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 (PubMed:28694333). In the NuA4
CC complex, EPC1 is required to recruit MBTD1 into the complex (By
CC similarity). {ECO:0000250|UniProtKB:Q9H2F5,
CC ECO:0000269|PubMed:28694333}.
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 (By similarity). KAT5/TIP60, EPC1,
CC and ING3 together constitute a minimal HAT complex termed Piccolo NuA4
CC (By similarity). Component of a NuA4-related complex which contains
CC EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41 (By
CC similarity). Interacts with TRIM27 (By similarity). Interacts with
CC MBTD1; interaction is direct and promotes recruitment of MBTD1 into the
CC NuA4 histone acetyltransferase complex (By similarity).
CC {ECO:0000250|UniProtKB:Q9H2F5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28694333}. Cytoplasm
CC {ECO:0000269|PubMed:28694333}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C9X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C9X6-2; Sequence=VSP_012878;
CC -!- TISSUE SPECIFICITY: Expressed in adult brain, heart, kidney, liver,
CC lung, skeletal muscle and testis (PubMed:9735366). Expressed in male
CC germ cells, present in round spermatids of steps 1 to 4
CC (PubMed:28694333). {ECO:0000269|PubMed:28694333,
CC ECO:0000269|PubMed:9735366}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but display growth retardation,
CC homeotic transformations of the axis and sterility in both males and
CC females (PubMed:28694333). Male sterility is caused by defects in
CC generation of elongating spermatids (PubMed:28694333).
CC {ECO:0000269|PubMed:28694333}.
CC -!- SIMILARITY: Belongs to the enhancer of polycomb family. {ECO:0000305}.
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DR EMBL; AF079765; AAC64272.1; -; mRNA.
DR EMBL; AK040254; BAC30552.1; -; mRNA.
DR EMBL; BC138622; AAI38623.1; -; mRNA.
DR EMBL; BC138623; AAI38624.1; -; mRNA.
DR CCDS; CCDS29041.1; -. [Q8C9X6-1]
DR CCDS; CCDS37726.1; -. [Q8C9X6-2]
DR RefSeq; NP_001263279.1; NM_001276350.1.
DR RefSeq; NP_031961.1; NM_007935.2. [Q8C9X6-2]
DR RefSeq; NP_081773.1; NM_027497.3. [Q8C9X6-1]
DR AlphaFoldDB; Q8C9X6; -.
DR BioGRID; 199466; 11.
DR ComplexPortal; CPX-747; Piccolo NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q8C9X6; 5.
DR MINT; Q8C9X6; -.
DR STRING; 10090.ENSMUSP00000028100; -.
DR iPTMnet; Q8C9X6; -.
DR PhosphoSitePlus; Q8C9X6; -.
DR EPD; Q8C9X6; -.
DR jPOST; Q8C9X6; -.
DR MaxQB; Q8C9X6; -.
DR PaxDb; Q8C9X6; -.
DR PRIDE; Q8C9X6; -.
DR ProteomicsDB; 275930; -. [Q8C9X6-1]
DR ProteomicsDB; 275931; -. [Q8C9X6-2]
DR Antibodypedia; 26401; 91 antibodies from 20 providers.
DR DNASU; 13831; -.
DR Ensembl; ENSMUST00000028100; ENSMUSP00000028100; ENSMUSG00000024240. [Q8C9X6-1]
DR Ensembl; ENSMUST00000115870; ENSMUSP00000111536; ENSMUSG00000024240. [Q8C9X6-2]
DR GeneID; 13831; -.
DR KEGG; mmu:13831; -.
DR UCSC; uc008dzi.2; mouse. [Q8C9X6-1]
DR UCSC; uc008dzj.2; mouse. [Q8C9X6-2]
DR CTD; 80314; -.
DR MGI; MGI:1278322; Epc1.
DR VEuPathDB; HostDB:ENSMUSG00000024240; -.
DR eggNOG; KOG2261; Eukaryota.
DR GeneTree; ENSGT00940000155003; -.
DR HOGENOM; CLU_012781_0_0_1; -.
DR InParanoid; Q8C9X6; -.
DR OMA; XENHESE; -.
DR OrthoDB; 957492at2759; -.
DR PhylomeDB; Q8C9X6; -.
DR TreeFam; TF106438; -.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 13831; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Epc1; mouse.
DR PRO; PR:Q8C9X6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8C9X6; protein.
DR Bgee; ENSMUSG00000024240; Expressed in metanephric mesenchyme and 258 other tissues.
DR ExpressionAtlas; Q8C9X6; baseline and differential.
DR Genevisible; Q8C9X6; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0140463; F:chromatin-protein adaptor; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; ISO:MGI.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; ISA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:1902275; P:regulation of chromatin organization; IC: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 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 Activator; Alternative splicing; Chromatin regulator; Cytoplasm;
KW Differentiation; Growth regulation; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..813
FT /note="Enhancer of polycomb homolog 1"
FT /id="PRO_0000214154"
FT REGION 310..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2F5"
FT CROSSLNK 319
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2F5"
FT CROSSLNK 650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2F5"
FT VAR_SEQ 1..51
FT /note="MSKLSFRARALDASKPLPVFRCEDLPDLHEYASINRAVPQMPTGMEKEEES
FT -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9735366"
FT /id="VSP_012878"
SQ SEQUENCE 813 AA; 90411 MW; E6F3CD987FC55905 CRC64;
MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS
AQQVYGEKRD NMVIPVPEAE SNIAYYESIY PGEFRMPKQL IHIQPFSLDA EQPDYDLDSE
DEVFVNKLKK KMDICPLQFE EMIDRLEKGS GQQPVSLQEA KLLLKEDDEL IREVYEYWIK
KRKTCRGSSL IPLVKQEKRD GSSTNDPYVA FRRRTEKMQT RKNRKNDEAS YEKMLKLRRD
LSRAVTILEM IKRREKSKRE LLHLTLEIME KRYNLGDYSG EIMSEVMAQR QPVKPTYAIP
IIPITNSSQF KHQDATDSKE FKVNKQDKAD LIRPKRKYEK KPKVLPPSAA APQQQSPAAL
PGFSAKDLNQ YDFPSSDEEP LSQVLSGSSE AEEENDPDGP FAFRRKAGCQ YYAPHLDQTG
NWPWTSPKDG GLGDVRYRYC LTTLTVPQRC LGFARRRVGR GGRVVLDRAH SDYDSMFHHL
DLDMLSSPQP SPVNQFANTS EPNTSDRSSS KDLSQILVDI KSCRWRHFRP RTPSLPDSDS
GELSSRKLHR SISRAGAAQP GAHTCSTSTQ NRSSSGSAHC AFTAEQYQQH QQQLALMQQQ
QLAQTQQQQQ ANSSSSAAAQ QGFVSKTLDS ASAQFAASAL MTSEQLLGFK VKDDVVLGLG
VNGVLPASGV YKGLHLSSTT PTALVHTSPS TAGSTLLQPS NITQTSGSHS SLSHQVTAAS
SATTQVLFGN NIRLTVPSSV PTVNSVTPIN ARHIPRTLSA VPPSALKLAA AANCQVSKVP
SSSSVDSVPR ENHESEKPAL NNIADNTVAM EVT
