EPOP_MOUSE
ID EPOP_MOUSE Reviewed; 369 AA.
AC Q7TNS8; Q8BN79; Q99JK6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Elongin BC and Polycomb repressive complex 2-associated protein {ECO:0000303|PubMed:27863225, ECO:0000303|PubMed:27863226};
DE AltName: Full=Embryonic stem cell-specific PRC2 subunit p48 {ECO:0000303|PubMed:21732481};
DE Short=ES cell-specific PRC2 subunit p48 {ECO:0000303|PubMed:21732481};
DE Short=esPRC2p48 {ECO:0000303|PubMed:21732481};
GN Name=Epop {ECO:0000303|PubMed:27863225, ECO:0000303|PubMed:27863226,
GN ECO:0000312|MGI:MGI:2143991}; Synonyms=E13 {ECO:0000303|PubMed:23180766};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 INTERACTION WITH THE PRC2/EZH2 COMPLEX, AND DEVELOPMENTAL STAGE.
RX PubMed=21732481; DOI=10.1002/stem.578;
RA Zhang Z., Jones A., Sun C.W., Li C., Chang C.W., Joo H.Y., Dai Q.,
RA Mysliwiec M.R., Wu L.C., Guo Y., Yang W., Liu K., Pawlik K.M.,
RA Erdjument-Bromage H., Tempst P., Lee Y., Min J., Townes T.M., Wang H.;
RT "PRC2 complexes with JARID2, MTF2, and esPRC2p48 in ES cells to modulate ES
RT cell pluripotency and somatic cell reprogramming.";
RL Stem Cells 29:229-240(2011).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=23180766; DOI=10.1093/nar/gks1136;
RA De Cegli R., Iacobacci S., Flore G., Gambardella G., Mao L., Cutillo L.,
RA Lauria M., Klose J., Illingworth E., Banfi S., di Bernardo D.;
RT "Reverse engineering a mouse embryonic stem cell-specific transcriptional
RT network reveals a new modulator of neuronal differentiation.";
RL Nucleic Acids Res. 41:711-726(2013).
RN [6]
RP INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=27462409; DOI=10.1038/celldisc.2015.8;
RA Liefke R., Shi Y.;
RT "The PRC2-associated factor C17orf96 is a novel CpG island regulator in
RT mouse ES cells.";
RL Cell Discov. 1:15008-15008(2015).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH THE
RP PRC2/EZH2 COMPLEX, INTERACTION WITH THE ELONGIN BC COMPLEX, AND MUTAGENESIS
RP OF LEU-40.
RX PubMed=27863225; DOI=10.1016/j.molcel.2016.10.018;
RA Beringer M., Pisano P., Di Carlo V., Blanco E., Chammas P., Vizan P.,
RA Gutierrez A., Aranda S., Payer B., Wierer M., Di Croce L.;
RT "EPOP functionally links elongin and Polycomb in pluripotent stem cells.";
RL Mol. Cell 64:645-658(2016).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH THE
RP PRC2/EZH2 COMPLEX, INTERACTION WITH THE ELONGIN BC COMPLEX, INTERACTION
RP WITH USP7, AND MUTAGENESIS OF LEU-40.
RX PubMed=27863226; DOI=10.1016/j.molcel.2016.10.019;
RA Liefke R., Karwacki-Neisius V., Shi Y.;
RT "EPOP interacts with elongin BC and USP7 to modulate the chromatin
RT landscape.";
RL Mol. Cell 64:659-672(2016).
CC -!- FUNCTION: Scaffold protein that serves as a bridging partner between
CC the PRC2/EZH2 complex and the elongin BC complex: required to fine-tune
CC the transcriptional status of Polycomb group (PcG) target genes in
CC embryonic stem cells (ESCs) (PubMed:27863225, PubMed:27863226). Plays a
CC key role in genomic regions that display both active and repressive
CC chromatin properties in pluripotent stem cells by sustaining low level
CC expression at PcG target genes: acts by recruiting the elongin BC
CC complex, thereby restricting excessive activity of the PRC2/EZH2
CC complex (PubMed:27863225, PubMed:27863226). Interaction with USP7
CC promotes deubiquitination of H2B at promoter sites (PubMed:27863226).
CC Acts as a regulator of neuronal differentiation (PubMed:23180766).
CC {ECO:0000269|PubMed:23180766, ECO:0000269|PubMed:27863225,
CC ECO:0000269|PubMed:27863226}.
CC -!- SUBUNIT: Associates with the PRC2 complex, which consists of the core
CC components EED, EZH1 or EZH2, SUZ12, and RBBP4, and various
CC combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2
CC and EPOP (PubMed:21732481, PubMed:27462409, PubMed:27863225,
CC PubMed:27863226). Within the complex, interacts with SUZ12 (via C2H2
CC zinc finger domain); competes with JARID2 for SUZ12 binding (By
CC similarity). Associates with the elongin BC complex (PubMed:27863225,
CC PubMed:27863226). Interacts with USP7 (PubMed:27863226).
CC {ECO:0000250|UniProtKB:A6NHQ4, ECO:0000269|PubMed:21732481,
CC ECO:0000269|PubMed:27462409, ECO:0000269|PubMed:27863225,
CC ECO:0000269|PubMed:27863226}.
CC -!- INTERACTION:
CC Q7TNS8; Q921E6: Eed; NbExp=2; IntAct=EBI-16024836, EBI-904301;
CC Q7TNS8; Q9D902: Gtf2e2; NbExp=2; IntAct=EBI-16024836, EBI-309435;
CC Q7TNS8; Q80U70: Suz12; NbExp=2; IntAct=EBI-16024836, EBI-2526494;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27863225}. Chromosome
CC {ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}.
CC Note=Localizes at both PRC2/EZH2 sites (H3K27me3) and broad H3K4me3
CC sites on chromatin of embryonic stem cells (ESCs) (PubMed:27863226).
CC {ECO:0000269|PubMed:27863226}.
CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic stem cells (ESCs)
CC during embryogenesis and in the adult brain (PubMed:23180766).
CC {ECO:0000269|PubMed:23180766}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryonic stem cells (ESCs)
CC during embryogenesis: expression starts from 4-cell stage.
CC {ECO:0000269|PubMed:21732481, ECO:0000269|PubMed:23180766,
CC ECO:0000269|PubMed:27462409, ECO:0000269|PubMed:27863225}.
CC -!- DOMAIN: The BC-box, which mediates binding to the elongin BC complex.
CC {ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK087411; BAC39864.1; -; mRNA.
DR EMBL; AL596123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006054; AAH06054.1; ALT_INIT; mRNA.
DR EMBL; BC055770; AAH55770.1; -; mRNA.
DR CCDS; CCDS25322.1; -.
DR RefSeq; NP_780541.2; NM_175332.3.
DR AlphaFoldDB; Q7TNS8; -.
DR SMR; Q7TNS8; -.
DR BioGRID; 222112; 29.
DR DIP; DIP-59969N; -.
DR IntAct; Q7TNS8; 27.
DR STRING; 10090.ENSMUSP00000051211; -.
DR PhosphoSitePlus; Q7TNS8; -.
DR PaxDb; Q7TNS8; -.
DR PeptideAtlas; Q7TNS8; -.
DR PRIDE; Q7TNS8; -.
DR Antibodypedia; 74279; 22 antibodies from 7 providers.
DR DNASU; 103551; -.
DR Ensembl; ENSMUST00000052281; ENSMUSP00000051211; ENSMUSG00000043439.
DR GeneID; 103551; -.
DR KEGG; mmu:103551; -.
DR UCSC; uc007leg.1; mouse.
DR CTD; 100170841; -.
DR MGI; MGI:2143991; Epop.
DR VEuPathDB; HostDB:ENSMUSG00000043439; -.
DR eggNOG; ENOG502QSWJ; Eukaryota.
DR GeneTree; ENSGT00940000153451; -.
DR HOGENOM; CLU_062153_0_0_1; -.
DR InParanoid; Q7TNS8; -.
DR OMA; WGINLEE; -.
DR OrthoDB; 1145293at2759; -.
DR PhylomeDB; Q7TNS8; -.
DR TreeFam; TF337589; -.
DR BioGRID-ORCS; 103551; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q7TNS8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7TNS8; protein.
DR Bgee; ENSMUSG00000043439; Expressed in ectoplacental cone and 105 other tissues.
DR Genevisible; Q7TNS8; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; IMP:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR InterPro; IPR027971; EPOP.
DR Pfam; PF15223; EPOP; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..369
FT /note="Elongin BC and Polycomb repressive complex 2-
FT associated protein"
FT /id="PRO_0000332155"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..48
FT /note="BC-box"
FT /evidence="ECO:0000269|PubMed:27863225,
FT ECO:0000269|PubMed:27863226"
FT REGION 89..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..349
FT /note="Interaction with SUZ12"
FT /evidence="ECO:0000250|UniProtKB:A6NHQ4"
FT COMPBIAS 9..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NHQ4"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NHQ4"
FT MOD_RES 52
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:A6NHQ4"
FT MUTAGEN 40
FT /note="L->A: Abolishes interaction with the elongin BC
FT complex."
FT /evidence="ECO:0000269|PubMed:27863225,
FT ECO:0000269|PubMed:27863226"
FT CONFLICT 129
FT /note="F -> S (in Ref. 1; BAC39864)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="A -> S (in Ref. 3; AAH06054)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="P -> A (in Ref. 1; BAC39864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 38095 MW; C93AC0213E4E97BF CRC64;
METLCPPPRL AVPASPRGSP CSPTPLKPRR GTPEFSPLCL RALAFCALAK PRPSSLGLGP
GELAPRTPVL LGPPASPCTG GWAADGLKHL GGQAGRPSDV SSPAREDADV AVCPGGGEEE
EGGGGFPHFG AGSCAPPGRC PAPLRPQDSP TNPAWSPPRP ARGLDAASSP PLEPGSPPPS
PPAGLSPEPA PSEQPVPASE APGGGDPAPT APEAPALSPS TADAAPDPPR DLRQEHFNRL
IRRSKLWCYA KGFALDTPSL RRGPERPAAK ARGAAKKRRR PAPPPPSVQP RRPVPTLPTS
STFSLLDCFP CPPALVVEEN GDLGPASSLR LQGDAKPPPA HPLWKWQMGG PAVPEPPGLK
SWWVNLEEL
