EPOP_HUMAN
ID EPOP_HUMAN Reviewed; 379 AA.
AC A6NHQ4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Elongin BC and Polycomb repressive complex 2-associated protein {ECO:0000250|UniProtKB:Q7TNS8};
DE AltName: Full=Proline-rich protein 28 {ECO:0000312|HGNC:HGNC:34493};
GN Name=EPOP {ECO:0000312|HGNC:HGNC:34493};
GN Synonyms=C17orf96 {ECO:0000312|HGNC:HGNC:34493},
GN PRR28 {ECO:0000312|HGNC:HGNC:34493};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-19, AND
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 [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-52, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [5]
RP INTERACTION WITH THE PRC2/EZH2 COMPLEX.
RX PubMed=24550272; DOI=10.1073/pnas.1400648111;
RA Alekseyenko A.A., Gorchakov A.A., Kharchenko P.V., Kuroda M.I.;
RT "Reciprocal interactions of human C10orf12 and C17orf96 with PRC2 revealed
RT by BioTAP-XL cross-linking and affinity purification.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2488-2493(2014).
RN [6] {ECO:0000305}
RP IDENTIFICATION IN THE PRC2 COMPLEX, AND INTERACTION WITH SUZ12.
RX PubMed=29499137; DOI=10.1016/j.molcel.2018.01.039;
RA Chen S., Jiao L., Shubbar M., Yang X., Liu X.;
RT "Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for
RT Chromatin Binding.";
RL Mol. Cell 69:840-852.e5(2018).
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). Plays a key role in genomic regions that
CC display both active and repressive chromatin properties in pluripotent
CC stem cells by sustaining low level expression at PcG target genes: acts
CC by recruiting the elongin BC complex, thereby restricting excessive
CC activity of the PRC2/EZH2 complex. Interaction with USP7 promotes
CC deubiquitination of H2B at promoter sites. Acts as a regulator of
CC neuronal differentiation. {ECO:0000250|UniProtKB:Q7TNS8}.
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:24550272, PubMed:29499137). Within the complex,
CC interacts with SUZ12 (via C2H2 zinc finger domain); competes with
CC JARID2 for SUZ12 binding (PubMed:29499137). Associates with the elongin
CC BC complex (By similarity). Interacts with USP7 (By similarity).
CC {ECO:0000250|UniProtKB:Q7TNS8, ECO:0000269|PubMed:24550272,
CC ECO:0000269|PubMed:29499137}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TNS8}.
CC Chromosome {ECO:0000250|UniProtKB:Q7TNS8}. Note=Localizes at both
CC PRC2/EZH2 sites (H3K27me3) and broad H3K4me3 sites on chromatin of
CC embryonic stem cells (ESCs). {ECO:0000250|UniProtKB:Q7TNS8}.
CC -!- DOMAIN: The BC-box, which mediates binding to the elongin BC complex.
CC {ECO:0000250|UniProtKB:Q7TNS8}.
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DR EMBL; AC006449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60520.1; -; Genomic_DNA.
DR CCDS; CCDS45661.1; -.
DR RefSeq; NP_001124149.1; NM_001130677.1.
DR AlphaFoldDB; A6NHQ4; -.
DR BioGRID; 936860; 28.
DR IntAct; A6NHQ4; 19.
DR MINT; A6NHQ4; -.
DR STRING; 9606.ENSP00000484710; -.
DR iPTMnet; A6NHQ4; -.
DR PhosphoSitePlus; A6NHQ4; -.
DR BioMuta; EPOP; -.
DR jPOST; A6NHQ4; -.
DR MassIVE; A6NHQ4; -.
DR MaxQB; A6NHQ4; -.
DR PaxDb; A6NHQ4; -.
DR PeptideAtlas; A6NHQ4; -.
DR PRIDE; A6NHQ4; -.
DR ProteomicsDB; 1217; -.
DR Antibodypedia; 74279; 22 antibodies from 7 providers.
DR DNASU; 100170841; -.
DR Ensembl; ENST00000613024.2; ENSP00000483859.1; ENSG00000277303.2.
DR Ensembl; ENST00000621654.2; ENSP00000484710.1; ENSG00000273604.2.
DR GeneID; 100170841; -.
DR KEGG; hsa:100170841; -.
DR MANE-Select; ENST00000621654.2; ENSP00000484710.1; NM_001130677.2; NP_001124149.1.
DR UCSC; uc010wdq.3; human.
DR CTD; 100170841; -.
DR GeneCards; EPOP; -.
DR HGNC; HGNC:34493; EPOP.
DR HPA; ENSG00000273604; Tissue enhanced (brain, testis).
DR MIM; 617795; gene.
DR neXtProt; NX_A6NHQ4; -.
DR OpenTargets; ENSG00000273604; -.
DR PharmGKB; PA162378581; -.
DR VEuPathDB; HostDB:ENSG00000273604; -.
DR eggNOG; ENOG502QSWJ; Eukaryota.
DR GeneTree; ENSGT00940000153451; -.
DR HOGENOM; CLU_062153_0_0_1; -.
DR InParanoid; A6NHQ4; -.
DR OMA; WGINLEE; -.
DR OrthoDB; 1145293at2759; -.
DR PhylomeDB; A6NHQ4; -.
DR TreeFam; TF337589; -.
DR PathwayCommons; A6NHQ4; -.
DR SignaLink; A6NHQ4; -.
DR BioGRID-ORCS; 100170841; 204 hits in 1064 CRISPR screens.
DR GenomeRNAi; 100170841; -.
DR Pharos; A6NHQ4; Tdark.
DR PRO; PR:A6NHQ4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; A6NHQ4; protein.
DR Bgee; ENSG00000273604; Expressed in superior frontal gyrus and 91 other tissues.
DR Genevisible; A6NHQ4; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070449; C:elongin complex; IEA:Ensembl.
DR GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; ISS:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR InterPro; IPR027971; EPOP.
DR Pfam; PF15223; EPOP; 1.
PE 1: Evidence at protein level;
KW Chromosome; Methylation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..379
FT /note="Elongin BC and Polycomb repressive complex 2-
FT associated protein"
FT /id="PRO_0000332154"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..48
FT /note="BC-box"
FT /evidence="ECO:0000250|UniProtKB:Q7TNS8"
FT REGION 72..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..359
FT /note="Interaction with SUZ12"
FT /evidence="ECO:0000269|PubMed:29499137"
FT COMPBIAS 159..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 52
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 379 AA; 39322 MW; B79A849C86733102 CRC64;
METLCPAPRL AVPASPRGSP CSPTPRKPCR GTQEFSPLCL RALAFCALAK PRASSLGPGP
GELAARSPVL RGPQAPLRPG GWAPDGLKHL WAPTGRPGVP NTAAGEDADV AACPRRGEEE
EGGGGFPHFG VRSCAPPGRC PAPPHPREST TSFASAPPRP APGLEPQRGP AASPPQEPSS
RPPSPPAGLS TEPAGPGTAP RPFLPGQPAE VDGNPPPAAP EAPAASPSTA SPAPAAPGDL
RQEHFDRLIR RSKLWCYAKG FALDTPSLRR GPERPPAKGP ARGAAKKRRL PAPPPRTAQP
RRPAPTLPTT STFSLLNCFP CPPALVVGED GDLKPASSLR LQGDSKPPPA HPLWRWQMGG
PAVPEPPGLK FWGINMDES
