EPC2_HUMAN
ID EPC2_HUMAN Reviewed; 807 AA.
AC Q52LR7; B3KWT7; D3DP89; Q7L9J1; Q96RR7; Q9NUT8; Q9NVR1; Q9UFM9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Enhancer of polycomb homolog 2;
DE AltName: Full=EPC-like;
GN Name=EPC2;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, Teratocarcinoma, and Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-807.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 661-807.
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-754, AND
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-324, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-195; LYS-324 AND
RP LYS-362, AND 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).
CC -!- FUNCTION: May play a role in transcription or DNA repair.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the enhancer of polycomb family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH93818.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH93820.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK60500.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91688.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA92032.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF286904; AAK60500.1; ALT_INIT; mRNA.
DR EMBL; AK002010; BAA92032.1; ALT_INIT; mRNA.
DR EMBL; AK001433; BAA91688.1; ALT_INIT; mRNA.
DR EMBL; AK125789; BAG54249.1; -; mRNA.
DR EMBL; CH471058; EAX11547.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11548.1; -; Genomic_DNA.
DR EMBL; BC093818; AAH93818.1; ALT_INIT; mRNA.
DR EMBL; BC093820; AAH93820.1; ALT_INIT; mRNA.
DR EMBL; AL117558; CAB55993.1; -; mRNA.
DR CCDS; CCDS46422.1; -.
DR PIR; T17303; T17303.
DR RefSeq; NP_056445.3; NM_015630.3.
DR AlphaFoldDB; Q52LR7; -.
DR SMR; Q52LR7; -.
DR BioGRID; 117564; 57.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q52LR7; -.
DR IntAct; Q52LR7; 36.
DR MINT; Q52LR7; -.
DR STRING; 9606.ENSP00000258484; -.
DR CarbonylDB; Q52LR7; -.
DR GlyGen; Q52LR7; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q52LR7; -.
DR PhosphoSitePlus; Q52LR7; -.
DR BioMuta; EPC2; -.
DR DMDM; 108935980; -.
DR EPD; Q52LR7; -.
DR jPOST; Q52LR7; -.
DR MassIVE; Q52LR7; -.
DR MaxQB; Q52LR7; -.
DR PaxDb; Q52LR7; -.
DR PeptideAtlas; Q52LR7; -.
DR PRIDE; Q52LR7; -.
DR ProteomicsDB; 62425; -.
DR Antibodypedia; 51789; 58 antibodies from 12 providers.
DR DNASU; 26122; -.
DR Ensembl; ENST00000258484.11; ENSP00000258484.6; ENSG00000135999.12.
DR GeneID; 26122; -.
DR KEGG; hsa:26122; -.
DR MANE-Select; ENST00000258484.11; ENSP00000258484.6; NM_015630.4; NP_056445.3.
DR UCSC; uc010zbt.3; human.
DR CTD; 26122; -.
DR DisGeNET; 26122; -.
DR GeneCards; EPC2; -.
DR HGNC; HGNC:24543; EPC2.
DR HPA; ENSG00000135999; Low tissue specificity.
DR MalaCards; EPC2; -.
DR MIM; 611000; gene.
DR neXtProt; NX_Q52LR7; -.
DR OpenTargets; ENSG00000135999; -.
DR PharmGKB; PA134875170; -.
DR VEuPathDB; HostDB:ENSG00000135999; -.
DR eggNOG; KOG2261; Eukaryota.
DR GeneTree; ENSGT00940000158526; -.
DR HOGENOM; CLU_012781_0_0_1; -.
DR InParanoid; Q52LR7; -.
DR OMA; SNKRCEN; -.
DR OrthoDB; 957492at2759; -.
DR PhylomeDB; Q52LR7; -.
DR TreeFam; TF106438; -.
DR PathwayCommons; Q52LR7; -.
DR SignaLink; Q52LR7; -.
DR BioGRID-ORCS; 26122; 200 hits in 1083 CRISPR screens.
DR ChiTaRS; EPC2; human.
DR GenomeRNAi; 26122; -.
DR Pharos; Q52LR7; Tbio.
DR PRO; PR:Q52LR7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q52LR7; protein.
DR Bgee; ENSG00000135999; Expressed in germinal epithelium of ovary and 190 other tissues.
DR ExpressionAtlas; Q52LR7; baseline and differential.
DR Genevisible; Q52LR7; HS.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:ComplexPortal.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:ComplexPortal.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:ComplexPortal.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
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; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 Chromatin regulator; DNA damage; DNA repair; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..807
FT /note="Enhancer of polycomb homolog 2"
FT /id="PRO_0000239295"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 723
FT /note="N -> D (in Ref. 5; CAB55993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 807 AA; 91095 MW; 855433050972CA7C CRC64;
MSKLSFRARA LDAAKPLPIY RGKDMPDLND CVSINRAVPQ MPTGMEKEEE SEHHLQRAIS
AQQVFREKKE SMVIPVPEAE SNVNYYNRLY KGEFKQPKQF IHIQPFNLDN EQPDYDMDSE
DETLLNRLNR KMEIKPLQFE IMIDRLEKAS SNQLVTLQEA KLLLNEDDYL IKAVYDYWVR
KRKNCRGPSL IPQIKQEKRD GSTNNDPYVA FRRRTEKMQT RKNRKNDEAS YEKMLKLRRE
FSRAITILEM IKRREKTKRE LLHLTLEVVE KRYHLGDYGG EILNEVKISR SEKELYATPA
TLHNGNHHKV QECKTKHPHH LSLKEEASDV VRQKKKYPKK PKAEALITSQ QPTPETLPVI
NKSDIKQYDF HSSDEDEFPQ VLSPVSEPEE ENDPDGPCAF RRRAGCQYYA PRLDQANHSC
ENSELADLDK LRYRHCLTTL TVPRRCIGFA RRRIGRGGRV IMDRISTEHD PVLKQIDPEM
LNSFSSSSQT IDFSSNFSRT NASSKHCENR LSLSEILSNI RSCRLQCFQP RLLNLQDSDS
EECTSRKPGQ TVNNKRVSAA SVALLNTSKN GISVTGGITE EQFQTHQQQL VQMQRQQLAQ
LQQKQQSQHS SQQTHPKAQG SSTSDCMSKT LDSASAHFAA SAVVSAPVPS RSEVAKEQNT
GHNNINGVVQ PSGTSKTLYS TNMALSSSPG ISAVQLVRTV GHTTTNHLIP ALCTSSPQTL
PMNNSCLTNA VHLNNVSVVS PVNVHINTRT SAPSPTALKL ATVAASMDRV PKVTPSSAIS
SIARENHEPE RLGLNGIAET TVAMEVT
