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Enhancer of polycomb homolog 1

 EPC1_HUMAN              Reviewed;         836 AA.
Q9H2F5; B4DSC3; D3DRX7; Q5VW54; Q5VW56; Q5VW58; Q8NAQ4; Q8NE21;
Q96LF4; Q96RR6; Q9H7T7;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
13-FEB-2019, entry version 151.
RecName: Full=Enhancer of polycomb homolog 1;
Name=EPC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
INTERACTION WITH TRIM27.
PubMed=10976108; DOI=10.1074/jbc.M006585200;
Shimono Y., Murakami H., Hasegawa Y., Takahashi M.;
"RET finger protein is a transcriptional repressor and interacts with
enhancer of polycomb that has dual transcriptional functions.";
J. Biol. Chem. 275:39411-39419(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Nunes D.N., Dias-Neto E., Brentani R.R., Camargo A.A.;
"Cloning and characterization of two human homologs of the enhancer of
polycomb gene (EPC1) from Drosophila.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 58-68 AND 802-813, IDENTIFICATION IN NUA4 COMPLEX,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12963728; DOI=10.1074/jbc.C300389200;
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
Conaway R.C., Conaway J.W.;
"Identification of new subunits of the multiprotein mammalian
TRRAP/TIP60-containing histone acetyltransferase complex.";
J. Biol. Chem. 278:42733-42736(2003).
[8]
REVIEW ON NUA4 COMPLEX.
PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
Doyon Y., Cote J.;
"The highly conserved and multifunctional NuA4 HAT complex.";
Curr. Opin. Genet. Dev. 14:147-154(2004).
[9]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
COMPLEX, AND IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING
COMPLEX.
PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
"Structural and functional conservation of the NuA4 histone
acetyltransferase complex from yeast to humans.";
Mol. Cell. Biol. 24:1884-1896(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-319 AND LYS-673, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[14]
VARIANT LEU-123.
PubMed=25787250; DOI=10.1073/pnas.1503696112;
Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D.,
Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T.,
Bjoerklund P., Lifton R.P.;
"Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
insulin-producing adenomas.";
Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
-!- FUNCTION: Component of the NuA4 histone acetyltransferase (HAT)
complex which is involved in transcriptional activation of select
genes principally by acetylation of nucleosomal histones H4 and
H2A. This modification may both alter nucleosome - DNA
interactions and promote interaction of the modified histones with
other proteins which positively regulate transcription. This
complex may be required for the activation of transcriptional
programs associated with oncogene and proto-oncogene mediated
growth induction, tumor suppressor mediated growth arrest and
replicative senescence, apoptosis, and DNA repair. NuA4 may also
play a direct role in DNA repair when directly recruited to sites
of DNA damage. {ECO:0000269|PubMed:14966270}.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
which contains the catalytic subunit KAT5/TIP60 and the subunits
EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX,
MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. HTATTIP/TIP60, EPC1, and
ING3 together constitute a minimal HAT complex termed Piccolo
NuA4. Component of a NuA4-related complex which contains EP400,
TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. The NuA4
complex interacts with MYC and the adenovirus E1A protein. EPC1
interacts with TRIM27. {ECO:0000269|PubMed:10976108,
ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14966270}.
-!- INTERACTION:
P19012:KRT15; NbExp=3; IntAct=EBI-769270, EBI-739566;
Q6NUQ1:RINT1; NbExp=4; IntAct=EBI-769270, EBI-726876;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10976108}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H2F5-1; Sequence=Displayed;
Name=2;
IsoId=Q9H2F5-2; Sequence=VSP_012877;
Name=3;
IsoId=Q9H2F5-3; Sequence=VSP_012875, VSP_012877;
-!- SIMILARITY: Belongs to the enhancer of polycomb family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB14888.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC03857.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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EMBL; AF277374; AAG41402.1; -; mRNA.
EMBL; AF286905; AAK60501.1; -; mRNA.
EMBL; AK024329; BAB14888.1; ALT_INIT; mRNA.
EMBL; AK092304; BAC03857.1; ALT_SEQ; mRNA.
EMBL; AK299676; BAG61585.1; -; mRNA.
EMBL; AL158834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL391839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471072; EAW85972.1; -; Genomic_DNA.
EMBL; CH471072; EAW85973.1; -; Genomic_DNA.
EMBL; BC036529; AAH36529.1; -; mRNA.
CCDS; CCDS60511.1; -. [Q9H2F5-2]
CCDS; CCDS7172.1; -. [Q9H2F5-1]
CCDS; CCDS73083.1; -. [Q9H2F5-3]
RefSeq; NP_001258933.1; NM_001272004.1. [Q9H2F5-2]
RefSeq; NP_001258948.1; NM_001272019.2.
RefSeq; NP_001269320.1; NM_001282391.1. [Q9H2F5-3]
RefSeq; NP_079485.1; NM_025209.3. [Q9H2F5-1]
UniGene; Hs.167805; -.
ProteinModelPortal; Q9H2F5; -.
BioGrid; 123227; 40.
ComplexPortal; CPX-709; Piccolo NuA4 histone acetyltransferase complex.
ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
CORUM; Q9H2F5; -.
IntAct; Q9H2F5; 17.
MINT; Q9H2F5; -.
STRING; 9606.ENSP00000263062; -.
iPTMnet; Q9H2F5; -.
PhosphoSitePlus; Q9H2F5; -.
SwissPalm; Q9H2F5; -.
BioMuta; EPC1; -.
DMDM; 59797889; -.
EPD; Q9H2F5; -.
jPOST; Q9H2F5; -.
MaxQB; Q9H2F5; -.
PaxDb; Q9H2F5; -.
PeptideAtlas; Q9H2F5; -.
PRIDE; Q9H2F5; -.
ProteomicsDB; 80540; -.
ProteomicsDB; 80541; -. [Q9H2F5-2]
ProteomicsDB; 80542; -. [Q9H2F5-3]
Ensembl; ENST00000263062; ENSP00000263062; ENSG00000120616. [Q9H2F5-1]
Ensembl; ENST00000319778; ENSP00000318559; ENSG00000120616. [Q9H2F5-2]
Ensembl; ENST00000375110; ENSP00000364251; ENSG00000120616. [Q9H2F5-3]
GeneID; 80314; -.
KEGG; hsa:80314; -.
UCSC; uc001iwg.3; human. [Q9H2F5-1]
CTD; 80314; -.
DisGeNET; 80314; -.
EuPathDB; HostDB:ENSG00000120616.15; -.
GeneCards; EPC1; -.
HGNC; HGNC:19876; EPC1.
MIM; 610999; gene.
neXtProt; NX_Q9H2F5; -.
OpenTargets; ENSG00000120616; -.
PharmGKB; PA134981141; -.
eggNOG; KOG2261; Eukaryota.
eggNOG; ENOG410XSSX; LUCA.
GeneTree; ENSGT00940000155003; -.
HOVERGEN; HBG051489; -.
InParanoid; Q9H2F5; -.
KO; K11322; -.
OMA; DYDSMFR; -.
OrthoDB; 957492at2759; -.
PhylomeDB; Q9H2F5; -.
TreeFam; TF106438; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
ChiTaRS; EPC1; human.
GeneWiki; EPC1; -.
GenomeRNAi; 80314; -.
PRO; PR:Q9H2F5; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000120616; Expressed in 207 organ(s), highest expression level in secondary oocyte.
Genevisible; Q9H2F5; HS.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0035886; P:vascular smooth muscle cell differentiation; IEA:Ensembl.
InterPro; IPR024943; Enhancer_polycomb.
InterPro; IPR019542; Enhancer_polycomb-like_N.
InterPro; IPR009607; Enhancer_polycomb_C.
PANTHER; PTHR14898; PTHR14898; 1.
Pfam; PF06752; E_Pc_C; 1.
Pfam; PF10513; EPL1; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Chromatin regulator;
Complete proteome; Direct protein sequencing; Growth regulation;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 836 Enhancer of polycomb homolog 1.
/FTId=PRO_0000214153.
MOD_RES 539 539 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 319 319 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 673 673 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 51 MSKLSFRARALDASKPLPVFRCEDLPDLHEYASINRAVPQM
PTGMEKEEES -> M (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_012875.
VAR_SEQ 621 643 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_012877.
VARIANT 123 123 V -> L. {ECO:0000269|PubMed:25787250}.
/FTId=VAR_074181.
CONFLICT 156 156 S -> G (in Ref. 2; AAK60501).
{ECO:0000305}.
CONFLICT 256 256 K -> R (in Ref. 2; AAK60501).
{ECO:0000305}.
CONFLICT 783 783 A -> V (in Ref. 6; AAH36529).
{ECO:0000305}.
CONFLICT 825 825 N -> S (in Ref. 3; BAC03857).
{ECO:0000305}.
SEQUENCE 836 AA; 93463 MW; E9E89699E73336B5 CRC64;
MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS
AQQVYGEKRD NMVIPVPEAE SNIAYYESIY PGEFKMPKQL IHIQPFSLDA EQPDYDLDSE
DEVFVNKLKK KMDICPLQFE EMIDRLEKGS GQQPVSLQEA KLLLKEDDEL IREVYEYWIK
KRKNCRGPSL IPSVKQEKRD GSSTNDPYVA FRRRTEKMQT RKNRKNDEAS YEKMLKLRRD
LSRAVTILEM IKRREKSKRE LLHLTLEIME KRYNLGDYNG EIMSEVMAQR QPMKPTYAIP
IIPITNSSQF KHQEAMDVKE FKVNKQDKAD LIRPKRKYEK KPKVLPSSAA ATPQQTSPAA
LPVFNAKDLN QYDFPSSDEE PLSQVLSGSS EAEEDNDPDG PFAFRRKAGC QYYAPHLDQT
GNWPWTSPKD GGLGDVRYRY CLTTLTVPQR CIGFARRRVG RGGRVLLDRA HSDYDSVFHH
LDLEMLSSPQ HSPVNQFANT SETNTSDKSF SKDLSQILVN IKSCRWRHFR PRTPSLHDSD
NDELSCRKLY RSINRTGTAQ PGTQTCSTST QSKSSSGSAH FAFTAEQYQQ HQQQLALMQK
QQLAQIQQQQ ANSNSSTNTS QNLASNQQKS GFRLNIQGLE RTLQGFVSKT LDSASAQFAA
SALVTSEQLM GFKMKDDVVL GIGVNGVLPA SGVYKGLHLS STTPTALVHT SPSTAGSALL
QPSNITQTSS SHSALSHQVT AANSATTQVL IGNNIRLTVP SSVATVNSIA PINARHIPRT
LSAVPSSALK LAAAANCQVS KVPSSSSVDS VPRENHESEK PALNNIADNT VAMEVT


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EIAAB13060 Enhancer of polycomb homolog 1,EPC1,Homo sapiens,Human
CSB-EL007715MO Mouse Enhancer of polycomb homolog 1(EPC1) ELISA kit SpeciesMouse 96T
CSB-EL007716HU Human Enhancer of polycomb homolog 2(EPC2) ELISA kit SpeciesHuman 96T
EIAAB13062 Enhancer of polycomb homolog 2,EPC2,EPC-like,Homo sapiens,Human
EPC1_MOUSE ELISA Kit FOR Enhancer of polycomb homolog 1; organism: Mouse; gene name: Epc1 96T
EPC2_MOUSE ELISA Kit FOR Enhancer of polycomb homolog 2; organism: Mouse; gene name: Epc2 96T
CSB-EL007715MO Mouse enhancer of polycomb homolog 1 (Drosophila) (EPC1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL007716HU Human enhancer of polycomb homolog 2 (Drosophila) (EPC2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL007715HU Human enhancer of polycomb homolog 1 (Drosophila) (EPC1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL007716MO Mouse enhancer of polycomb homolog 2 (Drosophila) (EPC2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
18-003-42562 Chromobox protein homolog 8 - Polycomb 3 homolog; Pc3; hPc3; Rectachrome 1 Polyclonal 0.05 mg Aff Pur

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP100: Glutathione metabolism
WP1016: Wnt Signaling Pathway
WP1039: Glutathione metabolism
WP104: Alanine and aspartate metabolism
WP1056: Complement and Coagulation Cascades
WP106: Alanine and aspartate metabolism
WP1126: Tryptophan metabolism
WP1135: Wnt Signaling Pathway
WP1172: Complement and Coagulation Cascades
WP1313: Insulin Signaling
WP1315: IL-5 Signaling Pathway
WP1318: Eicosanoid Synthesis
WP1321: Myometrial Relaxation and Contraction Pathways
WP1323: EGFR1 Signaling Pathway
WP1330: estrogen signalling
WP1331: Adipogenesis
WP1333: Hypothetical Network for Drug Addiction
WP1337: MAPK signaling pathway
WP1338: Peptide GPCRs
WP1339: Electron Transport Chain
WP1345: T Cell Receptor Signaling Pathway
WP1347: Triacylglyceride Synthesis
WP1349: Wnt Signaling Pathway
WP1350: Type II interferon signaling (IFNG)
WP1351: Apoptosis

Related Genes :
[EPC1] Enhancer of polycomb homolog 1
[EZH2 KMT6] Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.43) (ENX-1) (Enhancer of zeste homolog 2) (Lysine N-methyltransferase 6)
[Ezh2 Enx1h] Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.43) (ENX-1) (Enhancer of zeste homolog 2)
[pho CG17743] Polycomb protein PHO (Protein pleiohomeotic) (Transcription factor YY1 homolog)
[TLE1] Transducin-like enhancer protein 1 (E(Sp1) homolog) (Enhancer of split groucho-like protein 1) (ESG1)
[CBX8 PC3 RC1] Chromobox protein homolog 8 (Polycomb 3 homolog) (Pc3) (hPc3) (Rectachrome 1)
[EZH1 KIAA0388] Histone-lysine N-methyltransferase EZH1 (EC 2.1.1.43) (ENX-2) (Enhancer of zeste homolog 1)
[Epc1] Enhancer of polycomb homolog 1
[CBX4] E3 SUMO-protein ligase CBX4 (EC 2.3.2.-) (Chromobox protein homolog 4) (Polycomb 2 homolog) (Pc2) (hPc2)
[SUZ12 CHET9 JJAZ1 KIAA0160] Polycomb protein SUZ12 (Chromatin precipitated E2F target 9 protein) (ChET 9 protein) (Joined to JAZF1 protein) (Suppressor of zeste 12 protein homolog)
[Ezh1 Enx2] Histone-lysine N-methyltransferase EZH1 (EC 2.1.1.43) (ENX-2) (Enhancer of zeste homolog 1)
[Cbx4 Pc2] E3 SUMO-protein ligase CBX4 (EC 2.3.2.-) (Chromobox protein homolog 4) (E3 SUMO-protein transferase CBX4) (Polycomb 2 homolog) (Pc2) (mPc2)
[EED] Polycomb protein EED (hEED) (Embryonic ectoderm development protein) (WD protein associating with integrin cytoplasmic tails 1) (WAIT-1)
[Cbx8 Pc3] Chromobox protein homolog 8 (Polycomb 3 homolog) (Pc3) (mPc3)
[CNKSR1 CNK1] Connector enhancer of kinase suppressor of ras 1 (Connector enhancer of KSR 1) (CNK homolog protein 1) (CNK1) (hCNK1) (Connector enhancer of KSR-like)
[EPL1 YFL024C] Enhancer of polycomb-like protein 1
[CNKSR2 CNK2 KIAA0902 KSR2] Connector enhancer of kinase suppressor of ras 2 (Connector enhancer of KSR 2) (CNK homolog protein 2) (CNK2)
[ERH] Enhancer of rudimentary homolog
[E(z) KMT6 CG6502] Histone-lysine N-methyltransferase E(z) (EC 2.1.1.43) (Lysine N-methyltransferase 6) (Protein enhancer of zeste)
[HEY2 BHLHB32 CHF1 GRL HERP HERP1 HRT2] Hairy/enhancer-of-split related with YRPW motif protein 2 (Cardiovascular helix-loop-helix factor 1) (hCHF1) (Class B basic helix-loop-helix protein 32) (bHLHb32) (HES-related repressor protein 2) (Hairy and enhancer of split-related protein 2) (HESR-2) (Hairy-related transcription factor 2) (HRT-2) (hHRT2) (Protein gridlock homolog)
[PCOLCE PCPE1] Procollagen C-endopeptidase enhancer 1 (Procollagen COOH-terminal proteinase enhancer 1) (PCPE-1) (Procollagen C-proteinase enhancer 1) (Type 1 procollagen C-proteinase enhancer protein) (Type I procollagen COOH-terminal proteinase enhancer)
[ETV4 E1AF PEA3] ETS translocation variant 4 (Adenovirus E1A enhancer-binding protein) (E1A-F) (Polyomavirus enhancer activator 3 homolog) (Protein PEA3)
[Ezh2 LOC312299 rCG_28121] Enhancer of zeste 2 polycomb repressive complex 2 subunit (Ezh2 protein) (Similar to Enhancer of zeste homolog 2 (ENX-1), isoform CRA_b)
[Hey2 Chf1 Herp Herp1 Hesr2 Hrt2] Hairy/enhancer-of-split related with YRPW motif protein 2 (HES-related repressor protein 2) (Hairy and enhancer of split-related protein 2) (HESR-2) (Hairy-related transcription factor 2) (HRT-2) (mHRT2) (Protein gridlock homolog)
[mef2a sl2] Myocyte-specific enhancer factor 2A homolog (XMEF2A1) (xMEF2A) (Serum response factor-like protein 2) (SL-2)
[Atf4] Cyclic AMP-dependent transcription factor ATF-4 (cAMP-dependent transcription factor ATF-4) (Activating transcription factor 4) (C/EBP-related ATF) (C/ATF) (Tax-responsive enhancer element-binding protein 67 homolog) (TaxREB67 homolog)
[Hivep3 KBP1 Kiaa1555 Krc Rc shn3 Zas3] Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3 homolog) (KB-binding and recognition component) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Recombinant component) (Schnurri-3) (Zinc finger protein ZAS3)
[Scmh1] Polycomb protein SCMH1 (Sex comb on midleg homolog 1)
[AES GRG GRG5] Amino-terminal enhancer of split (Amino enhancer of split) (Gp130-associated protein GAM) (Grg-5) (Groucho-related protein 5) (Protein ESP1) (Protein GRG)
[PCGF1 NSPC1 RNF68] Polycomb group RING finger protein 1 (Nervous system Polycomb-1) (NSPc1) (RING finger protein 68)

Bibliography :
[30885343] Highly expressed EZH2 in combination with BAP1 and MTAP loss, as detected by immunohistochemistry, is useful for differentiating malignant pleural mesothelioma from reactive mesothelial hyperplasia.
[30788509] Long noncoding RNA MALAT1 releases epigenetic silencing of HIV-1 replication by displacing the polycomb repressive complex 2 from binding to the LTR promoter.
[30736855] Coordination between TGF-β cellular signaling and epigenetic regulation during epithelial to mesenchymal transition.
[30692537] Maintenance of epigenetic landscape requires CIZ1 and is corrupted in differentiated fibroblasts in long-term culture.
[30683859] The functional synergism of microRNA clustering provides therapeutically relevant epigenetic interference in glioblastoma.
[30677064] The ezh2(sa1199) mutant zebrafish display no distinct phenotype.
[30655550] CBX6 is negatively regulated by EZH2 and plays a potential tumor suppressor role in breast cancer.
[30626493] Epigenetic modulation enhances immunotherapy for hepatocellular carcinoma.
[30608448] Novel EZH2 mutation in a patient with secondary B-cell acute lymphocytic leukemia after deletion 5q myelodysplastic syndrome treated with lenalidomide: A case report.
[30606231] Specific functions of TET1 and TET2 in regulating mesenchymal cell lineage determination.
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