EPC2_MOUSE
ID EPC2_MOUSE Reviewed; 808 AA.
AC Q8C0I4; A2AQU9; Q3URX9; Q80Y70; Q8BXC5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Enhancer of polycomb homolog 2;
DE AltName: Full=EPC-like;
GN Name=Epc2;
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=Cerebellum, Head, and 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 [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] OF 82-808.
RC STRAIN=FVB/N; TISSUE=Colon;
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).
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=BAC33197.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK031025; BAC27218.1; -; mRNA.
DR EMBL; AK047947; BAC33197.1; ALT_INIT; mRNA.
DR EMBL; AK141073; BAE24558.1; -; mRNA.
DR EMBL; AL845163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048785; AAH48785.1; -; mRNA.
DR CCDS; CCDS16023.1; -.
DR RefSeq; NP_766251.3; NM_172663.4.
DR AlphaFoldDB; Q8C0I4; -.
DR BioGRID; 230690; 2.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q8C0I4; 4.
DR MINT; Q8C0I4; -.
DR STRING; 10090.ENSMUSP00000089758; -.
DR iPTMnet; Q8C0I4; -.
DR PhosphoSitePlus; Q8C0I4; -.
DR EPD; Q8C0I4; -.
DR MaxQB; Q8C0I4; -.
DR PaxDb; Q8C0I4; -.
DR PeptideAtlas; Q8C0I4; -.
DR PRIDE; Q8C0I4; -.
DR ProteomicsDB; 275527; -.
DR Antibodypedia; 51789; 58 antibodies from 12 providers.
DR DNASU; 227867; -.
DR Ensembl; ENSMUST00000092123; ENSMUSP00000089758; ENSMUSG00000069495.
DR GeneID; 227867; -.
DR KEGG; mmu:227867; -.
DR UCSC; uc008jpw.2; mouse.
DR CTD; 26122; -.
DR MGI; MGI:1278321; Epc2.
DR VEuPathDB; HostDB:ENSMUSG00000069495; -.
DR eggNOG; KOG2261; Eukaryota.
DR GeneTree; ENSGT00940000158526; -.
DR HOGENOM; CLU_012781_0_0_1; -.
DR InParanoid; Q8C0I4; -.
DR OMA; SNKRCEN; -.
DR OrthoDB; 957492at2759; -.
DR PhylomeDB; Q8C0I4; -.
DR TreeFam; TF106438; -.
DR BioGRID-ORCS; 227867; 18 hits in 114 CRISPR screens.
DR PRO; PR:Q8C0I4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C0I4; protein.
DR Bgee; ENSMUSG00000069495; Expressed in manus and 221 other tissues.
DR ExpressionAtlas; Q8C0I4; baseline and differential.
DR Genevisible; Q8C0I4; MM.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO: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: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 2: Evidence at transcript level;
KW Chromatin regulator; DNA damage; DNA repair; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..808
FT /note="Enhancer of polycomb homolog 2"
FT /id="PRO_0000239296"
FT REGION 337..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LR7"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q52LR7"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q52LR7"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q52LR7"
FT CROSSLNK 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q52LR7"
FT CONFLICT 5
FT /note="S -> A (in Ref. 1; BAC33197)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="E -> K (in Ref. 1; BAE24558)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="L -> P (in Ref. 3; AAH48785)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="A -> V (in Ref. 1; BAC27218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 90960 MW; F1DAAC73786B349B 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 EILNEVKVNR SEKELYASPA
TLHNGNHHKV QECKTKHPHH LSLKEEASDV VRQKKKYPKK PKAEAGIAPQ QPTPETLPVI
NKSDIKQYDF QSSDEDEFPQ VLSPASEAEE ENDPDGSCAF RRRAGCQYYA PRLDQANNHM
CENSELADLD KLRYKHCLTT LTVPRRCIGF ARRRIGRGGR VIMDRISTEH DPVLKQIDPE
MLNGFSSSSQ TIDFSSNFSR TNASSKPCEN RLSLSEILSN IRSCRLQCFQ PRLLNVQDID
SEECTSRKPG QTVSSKRVSA ASVALLNTSK NGISVTGGIT EEQFQTHQQQ LVQMQRQQLA
QLHQKQQSQH SSQQTHPKAQ GSSTSDCMSK TLDSASAHFA ASAVVSAPVP SRSEGSKEQN
TGHNNMNGVV QPSGPSKTLY STNMALSSSP GISAVQLVRT VGHTTTNHLI PALCTSSPQT
LPMNNSCLTN AVHLNNVSVV SPVNVHINTR TSAPSPTALK LATVAASMDR VPKVTPSSAI
SSIARENHEP ERLGLNGLAE TTVAMEVT
