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Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.43) (ENX-1) (Enhancer of zeste homolog 2) (Lysine N-methyltransferase 6)

 EZH2_HUMAN              Reviewed;         746 AA.
Q15910; B2RAQ1; B3KS30; B7Z1D6; B7Z7L6; Q15755; Q75MG3; Q92857;
Q96FI6;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
30-AUG-2017, entry version 173.
RecName: Full=Histone-lysine N-methyltransferase EZH2 {ECO:0000305};
EC=2.1.1.43 {ECO:0000269|PubMed:22323599};
AltName: Full=ENX-1;
AltName: Full=Enhancer of zeste homolog 2 {ECO:0000303|PubMed:28229514};
AltName: Full=Lysine N-methyltransferase 6;
Name=EZH2 {ECO:0000312|HGNC:HGNC:3527}; Synonyms=KMT6;
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).
TISSUE=Brain;
PubMed=8954776; DOI=10.1006/geno.1996.0588;
Chen H., Rossier C., Antonarakis S.E.;
"Cloning of a human homolog of the Drosophila enhancer of zeste gene
(EZH2) that maps to chromosome 21q22.2.";
Genomics 38:30-37(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9214638; DOI=10.1093/emboj/16.11.3219;
Laible G., Wolf A., Dorn R., Reuter G., Nislow C., Lebersorger A.,
Popkin D., Pillus L., Jenuwein T.;
"Mammalian homologues of the Polycomb-group gene Enhancer of zeste
mediate gene silencing in Drosophila heterochromatin and at S.
cerevisiae telomeres.";
EMBO J. 16:3219-3232(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
TISSUE=Brain, and Testis;
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=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[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=Pancreas;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-746.
PubMed=8649418; DOI=10.1128/MCB.16.6.3066;
Hobert O., Jallal B., Ullrich A.;
"Interaction of Vav with ENX-1, a putative transcriptional regulator
of homeobox gene expression.";
Mol. Cell. Biol. 16:3066-3073(1996).
[8]
INTERACTION WITH ATRX.
PubMed=9499421; DOI=10.1093/hmg/7.4.679;
Cardoso C., Timsit S., Villard L., Khrestchatisky M., Fontes M.,
Colleaux L.;
"Specific interaction between the XNP/ATR-X gene product and the SET
domain of the human EZH2 protein.";
Hum. Mol. Genet. 7:679-684(1998).
[9]
INTERACTION WITH EED, AND SUBCELLULAR LOCATION.
PubMed=9584199; DOI=10.1128/MCB.18.6.3586;
Sewalt R.G.A.B., van der Vlag J., Gunster M.J., Hamer K.M.,
den Blaauwen J.L., Satijn D.P.E., Hendrix T., van Driel R., Otte A.P.;
"Characterization of interactions between the mammalian polycomb-group
proteins Enx1/EZH2 and EED suggests the existence of different
mammalian polycomb-group protein complexes.";
Mol. Cell. Biol. 18:3586-3595(1998).
[10]
INTERACTION WITH EED; HDAC1 AND HDAC2.
PubMed=10581039; DOI=10.1038/70602;
van der Vlag J., Otte A.P.;
"Transcriptional repression mediated by the human polycomb-group
protein EED involves histone deacetylation.";
Nat. Genet. 23:474-478(1999).
[11]
INTERACTION WITH EED.
PubMed=11158321; DOI=10.1128/MCB.21.4.1360-1369.2001;
Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.;
"The polycomb group protein EED interacts with YY1, and both proteins
induce neural tissue in Xenopus embryos.";
Mol. Cell. Biol. 21:1360-1369(2001).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2
COMPLEX WITH EED; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY
OF THE PRC2 COMPLEX, AND MUTAGENESIS OF CYS-588 AND HIS-689.
PubMed=12435631; DOI=10.1101/gad.1035902;
Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P.,
Reinberg D.;
"Histone methyltransferase activity associated with a human
multiprotein complex containing the Enhancer of Zeste protein.";
Genes Dev. 16:2893-2905(2002).
[13]
SUBCELLULAR LOCATION.
PubMed=12101246; DOI=10.1128/MCB.22.15.5539-5553.2002;
Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L.,
Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.;
"Selective interactions between vertebrate polycomb homologs and the
SUV39H1 histone lysine methyltransferase suggest that histone H3-K9
methylation contributes to chromosomal targeting of Polycomb group
proteins.";
Mol. Cell. Biol. 22:5539-5553(2002).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2
COMPLEX WITH EED; RBBP4; RBBP7 AND SUZ12, AND METHYLTRANSFERASE
ACTIVITY OF THE PRC2 COMPLEX.
PubMed=12351676; DOI=10.1126/science.1076997;
Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H3 lysine 27 methylation in Polycomb-group
silencing.";
Science 298:1039-1043(2002).
[15]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=14532106; DOI=10.1093/emboj/cdg542;
Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K.;
"EZH2 is downstream of the pRB-E2F pathway, essential for
proliferation and amplified in cancer.";
EMBO J. 22:5323-5335(2003).
[16]
FUNCTION, INTERACTION WITH EED AND SUZ12, AND METHYLTRANSFERASE
ACTIVITY OF THE PRC2 COMPLEX.
PubMed=15385962; DOI=10.1038/sj.emboj.7600402;
Pasini D., Bracken A.P., Jensen M.R., Lazzerini Denchi E., Helin K.;
"Suz12 is essential for mouse development and for EZH2 histone
methyltransferase activity.";
EMBO J. 23:4061-4071(2004).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15231737; DOI=10.1101/gad.1200204;
Kirmizis A., Bartley S.M., Kuzmichev A., Margueron R., Reinberg D.,
Green R., Farnham P.J.;
"Silencing of human polycomb target genes is associated with
methylation of histone H3 Lys 27.";
Genes Dev. 18:1592-1605(2004).
[18]
CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2;
RBBP4; RBBP7 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND
PRC3 COMPLEXES.
PubMed=15099518; DOI=10.1016/S1097-2765(04)00185-6;
Kuzmichev A., Jenuwein T., Tempst P., Reinberg D.;
"Different EZH2-containing complexes target methylation of histone H1
or nucleosomal histone H3.";
Mol. Cell 14:183-193(2004).
[19]
FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED;
EZH2; RBBP4 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2
COMPLEX.
PubMed=15225548; DOI=10.1016/j.molcel.2004.06.020;
Cao R., Zhang Y.;
"SUZ12 is required for both the histone methyltransferase activity and
the silencing function of the EED-EZH2 complex.";
Mol. Cell 15:57-67(2004).
[20]
DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=15208672; DOI=10.1038/sj.onc.1207706;
Tang X., Milyavsky M., Shats I., Erez N., Goldfinger N., Rotter V.;
"Activated p53 suppresses the histone methyltransferase EZH2 gene.";
Oncogene 23:5759-5769(2004).
[21]
FUNCTION IN RETINOIC ACID SIGNALING, AND INTERACTION WITH PRAME.
PubMed=16179254; DOI=10.1016/j.cell.2005.07.003;
Epping M.T., Wang L., Edel M.J., Carlee L., Hernandez M., Bernards R.;
"The human tumor antigen PRAME is a dominant repressor of retinoic
acid receptor signaling.";
Cell 122:835-847(2005).
[22]
CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4;
RBBP7; SUZ12 AND SIRT1, AND METHYLTRANSFERASE ACTIVITY OF THE PRC4
COMPLEX.
PubMed=15684044; DOI=10.1073/pnas.0409875102;
Kuzmichev A., Margueron R., Vaquero A., Preissner T.S., Scher M.,
Kirmizis A., Ouyang X., Brockdorff N., Abate-Shen C., Farnham P.J.,
Reinberg D.;
"Composition and histone substrates of polycomb repressive group
complexes change during cellular differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005).
[23]
INTERACTION WITH EED AND SUZ12, PHOSPHORYLATION AT SER-21 BY AKT1, AND
MUTAGENESIS OF SER-21.
PubMed=16224021; DOI=10.1126/science.1118947;
Cha T.-L., Zhou B.P., Xia W., Wu Y., Yang C.-C., Chen C.-T., Ping B.,
Otte A.P., Hung M.-C.;
"Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine
27 in histone H3.";
Science 310:306-310(2005).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[25]
FUNCTION.
PubMed=16618801; DOI=10.1101/gad.381706;
Bracken A.P., Dietrich N., Pasini D., Hansen K.H., Helin K.;
"Genome-wide mapping of Polycomb target genes unravels their roles in
cell fate transitions.";
Genes Dev. 20:1123-1136(2006).
[26]
METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
PubMed=16431907; DOI=10.1074/jbc.M513425200;
Martin C., Cao R., Zhang Y.;
"Substrate preferences of the EZH2 histone methyltransferase
complex.";
J. Biol. Chem. 281:8365-8370(2006).
[27]
FUNCTION.
PubMed=16717091; DOI=10.1074/jbc.M603722200;
Etchegaray J.P., Yang X., DeBruyne J.P., Peters A.H., Weaver D.R.,
Jenuwein T., Reppert S.M.;
"The polycomb group protein EZH2 is required for mammalian circadian
clock function.";
J. Biol. Chem. 281:21209-21215(2006).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[29]
FUNCTION, AND INTERACTION OF THE PRC2 COMPLEX WITH DNMT1; DNMT3A AND
DNMT3B.
PubMed=16357870; DOI=10.1038/nature04431;
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
Esteller M., Di Croce L., de Launoit Y., Fuks F.;
"The Polycomb group protein EZH2 directly controls DNA methylation.";
Nature 439:871-874(2006).
[30]
ERRATUM.
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
Esteller M., Di Croce L., de Launoit Y., Fuks F.;
Nature 446:824-824(2006).
[31]
FUNCTION.
PubMed=16936726; DOI=10.1038/nsmb1142;
Kim D.H., Villeneuve L.M., Morris K.V., Rossi J.J.;
"Argonaute-1 directs siRNA-mediated transcriptional gene silencing in
human cells.";
Nat. Struct. Mol. Biol. 13:793-797(2006).
[32]
FUNCTION.
PubMed=17210787; DOI=10.1101/gad.1499407;
Kotake Y., Cao R., Viatour P., Sage J., Zhang Y., Xiong Y.;
"pRB family proteins are required for H3K27 trimethylation and
Polycomb repression complexes binding to and silencing p16INK4alpha
tumor suppressor gene.";
Genes Dev. 21:49-54(2007).
[33]
FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=17344414; DOI=10.1101/gad.415507;
Bracken A.P., Kleine-Kohlbrecher D., Dietrich N., Pasini D.,
Gargiulo G., Beekman C., Theilgaard-Moench K., Minucci S., Porse B.T.,
Marine J.-C., Hansen K.H., Helin K.;
"The Polycomb group proteins bind throughout the INK4A-ARF locus and
are disassociated in senescent cells.";
Genes Dev. 21:525-530(2007).
[34]
DE NOVO DNA METHYLATION OF PRC2 TARGET GENES.
PubMed=17200670; DOI=10.1038/ng1950;
Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M.,
Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E.,
Bergman Y., Simon I., Cedar H.;
"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes
for de novo methylation in cancer.";
Nat. Genet. 39:232-236(2007).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[37]
FUNCTION, AND IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
PubMed=19026781; DOI=10.1016/j.molcel.2008.11.004;
Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L.,
Dynlacht B.D., Reinberg D.;
"Ezh1 and Ezh2 maintain repressive chromatin through different
mechanisms.";
Mol. Cell 32:503-518(2008).
[38]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2
COMPLEX, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
PubMed=18086877; DOI=10.1128/MCB.01589-07;
Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.;
"Role of hPHF1 in H3K27 methylation and Hox gene silencing.";
Mol. Cell. Biol. 28:1862-1872(2008).
[39]
FUNCTION, INTERACTION WITH EED; SUZ12 AND PHF1, METHYLTRANSFERASE
ACTIVITY OF THE PRC2 COMPLEX, AND MUTAGENESIS OF HIS-689.
PubMed=18285464; DOI=10.1128/MCB.02017-07;
Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.;
"Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27
trimethylation in vivo.";
Mol. Cell. Biol. 28:2718-2731(2008).
[40]
SUMOYLATION.
PubMed=18628979; DOI=10.1371/journal.pone.0002704;
Riising E.M., Boggio R., Chiocca S., Helin K., Pasini D.;
"The polycomb repressive complex 2 is a potential target of SUMO
modifications.";
PLoS ONE 3:E2704-E2704(2008).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; THR-367 AND
THR-487, AND 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).
[42]
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).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[44]
FUNCTION, PHOSPHORYLATION AT THR-345 BY CDK1 AND CDK2, AND MUTAGENESIS
OF THR-345.
PubMed=20935635; DOI=10.1038/ncb2116;
Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A.,
Simon J.A., Huang H.;
"Cyclin-dependent kinases regulate epigenetic gene silencing through
phosphorylation of EZH2.";
Nat. Cell Biol. 12:1108-1114(2010).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[46]
INTERACTION WITH CDYL.
PubMed=22009739; DOI=10.1074/jbc.M111.271064;
Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.;
"Corepressor protein CDYL functions as a molecular bridge between
polycomb repressor complex 2 and repressive chromatin mark
trimethylated histone lysine 27.";
J. Biol. Chem. 286:42414-42425(2011).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[48]
FUNCTION.
PubMed=23063525; DOI=10.1016/j.molcel.2012.09.004;
Lee J.M., Lee J.S., Kim H., Kim K., Park H., Kim J.Y., Lee S.H.,
Kim I.S., Kim J., Lee M., Chung C.H., Seo S.B., Yoon J.B., Ko E.,
Noh D.Y., Kim K.I., Kim K.K., Baek S.H.;
"EZH2 generates a methyl degron that is recognized by the
DCAF1/DDB1/CUL4 E3 ubiquitin ligase complex.";
Mol. Cell 48:572-586(2012).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; THR-339; SER-363;
THR-367 AND THR-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[50]
GLYCOSYLATION AT SER-75, MUTAGENESIS OF SER-75, AND FUNCTION.
PubMed=24474760; DOI=10.1073/pnas.1323226111;
Chu C.S., Lo P.W., Yeh Y.H., Hsu P.H., Peng S.H., Teng Y.C.,
Kang M.L., Wong C.H., Juan L.J.;
"O-GlcNAcylation regulates EZH2 protein stability and function.";
Proc. Natl. Acad. Sci. U.S.A. 111:1355-1360(2014).
[51]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-634, 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).
[52]
VARIANTS PHE-641; SER-641; ASN-641; HIS-641 AND CYS-641.
PubMed=20081860; DOI=10.1038/ng.518;
Morin R.D., Johnson N.A., Severson T.M., Mungall A.J., An J., Goya R.,
Paul J.E., Boyle M., Woolcock B.W., Kuchenbauer F., Yap D.,
Humphries R.K., Griffith O.L., Shah S., Zhu H., Kimbara M.,
Shashkin P., Charlot J.F., Tcherpakov M., Corbett R., Tam A.,
Varhol R., Smailus D., Moksa M., Zhao Y., Delaney A., Qian H.,
Birol I., Schein J., Moore R., Holt R., Horsman D.E., Connors J.M.,
Jones S., Aparicio S., Hirst M., Gascoyne R.D., Marra M.A.;
"Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse
large B-cell lymphomas of germinal-center origin.";
Nat. Genet. 42:181-185(2010).
[53]
VARIANTS TRP-571; CYS-641; CYS-685 AND ASP-726, AND CHARACTERIZATION
OF VARIANTS TRP-571; CYS-641; CYS-685 AND ASP-726.
PubMed=20601953; DOI=10.1038/ng.621;
Ernst T., Chase A.J., Score J., Hidalgo-Curtis C.E., Bryant C.,
Jones A.V., Waghorn K., Zoi K., Ross F.M., Reiter A., Hochhaus A.,
Drexler H.G., Duncombe A., Cervantes F., Oscier D., Boultwood J.,
Grand F.H., Cross N.C.;
"Inactivating mutations of the histone methyltransferase gene EZH2 in
myeloid disorders.";
Nat. Genet. 42:722-726(2010).
[54]
CHARACTERIZATION OF VARIANTS PHE-641 AND ASN-641.
PubMed=21190999; DOI=10.1182/blood-2010-11-321208;
Yap D.B., Chu J., Berg T., Schapira M., Cheng S.W., Moradian A.,
Morin R.D., Mungall A.J., Meissner B., Boyle M., Marquez V.E.,
Marra M.A., Gascoyne R.D., Humphries R.K., Arrowsmith C.H.,
Morin G.B., Aparicio S.A.;
"Somatic mutations at EZH2 Y641 act dominantly through a mechanism of
selectively altered PRC2 catalytic activity, to increase H3K27
trimethylation.";
Blood 117:2451-2459(2011).
[55]
VARIANT HIS-685.
PubMed=21828135; DOI=10.1182/blood-2010-10-311019;
Jankowska A.M., Makishima H., Tiu R.V., Szpurka H., Huang Y.,
Traina F., Visconte V., Sugimoto Y., Prince C., O'Keefe C., Hsi E.D.,
List A., Sekeres M.A., Rao A., McDevitt M.A., Maciejewski J.P.;
"Mutational spectrum analysis of chronic myelomonocytic leukemia
includes genes associated with epigenetic regulation: UTX, EZH2, and
DNMT3A.";
Blood 118:3932-3941(2011).
[56]
VARIANTS WVS THR-134; GLU-156; ARG-279; MET-621; ASN-658; THR-677;
CYS-679; LEU-690; 728-TYR--PRO-746 DEL AND CYS-736.
PubMed=22190405; DOI=10.18632/oncotarget.385;
Childhood Overgrowth Collaboration;
Tatton-Brown K., Hanks S., Ruark E., Zachariou A., Duarte S.V.,
Ramsay E., Snape K., Murray A., Perdeaux E.R., Seal S., Loveday C.,
Banka S., Clericuzio C., Flinter F., Magee A., McConnell V.,
Patton M., Raith W., Rankin J., Splitt M., Strenger V., Taylor C.,
Wheeler P., Temple K.I., Cole T., Douglas J., Rahman N.;
"Germline mutations in the oncogene EZH2 cause Weaver syndrome and
increased human height.";
Oncotarget 2:1127-1133(2011).
[57]
VARIANTS WVS SER-132; TYR-153 DEL AND TYR-689.
PubMed=22177091; DOI=10.1016/j.ajhg.2011.11.018;
Gibson W.T., Hood R.L., Zhan S.H., Bulman D.E., Fejes A.P., Moore R.,
Mungall A.J., Eydoux P., Babul-Hirji R., An J., Marra M.A.,
Chitayat D., Boycott K.M., Weaver D.D., Jones S.J.;
"Mutations in EZH2 cause Weaver syndrome.";
Am. J. Hum. Genet. 90:110-118(2012).
[58]
VARIANT GLY-677, CHARACTERIZATION OF VARIANTS ASN-641; CYS-641;
HIS-641; PHE-641 AND GLY-677, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=22323599; DOI=10.1073/pnas.1116418109;
McCabe M.T., Graves A.P., Ganji G., Diaz E., Halsey W.S., Jiang Y.,
Smitheman K.N., Ott H.M., Pappalardi M.B., Allen K.E., Chen S.B.,
Della Pietra A. III, Dul E., Hughes A.M., Gilbert S.A., Thrall S.H.,
Tummino P.J., Kruger R.G., Brandt M., Schwartz B., Creasy C.L.;
"Mutation of A677 in histone methyltransferase EZH2 in human B-cell
lymphoma promotes hypertrimethylation of histone H3 on lysine 27
(H3K27).";
Proc. Natl. Acad. Sci. U.S.A. 109:2989-2994(2012).
[59]
VARIANT WVS LYS-740.
PubMed=23239504; DOI=10.1002/ajmg.a.35660;
Al-Salem A., Alshammari M.J., Hassan H., Alazami A.M., Alkuraya F.S.;
"Weaver syndrome and defective cortical development: a rare
association.";
Am. J. Med. Genet. A 161A:225-227(2013).
[60]
VARIANTS WVS CYS-133 AND CYS-679, CHARACTERIZATION OF VARIANTS WVS
SER-132; CYS-133; TYR-153 DEL; CYS-679 AND TYR-689, VARIANT HIS-185,
CHARACTERIZATION OF VARIANT HIS-185, AND MUTAGENESIS OF PHE-667.
PubMed=26694085; DOI=10.1002/humu.22946;
Cohen A.S., Yap D.B., Lewis M.E., Chijiwa C., Ramos-Arroyo M.A.,
Tkachenko N., Milano V., Fradin M., McKinnon M.L., Townsend K.N.,
Xu J., Van Allen M.I., Ross C.J., Dobyns W.B., Weaver D.D.,
Gibson W.T.;
"Weaver Syndrome-Associated EZH2 Protein Variants Show Impaired
Histone Methyltransferase Function In Vitro.";
Hum. Mutat. 37:301-307(2016).
[61]
INVOLVEMENT IN WVS.
PubMed=28229514; DOI=10.1002/humu.23200;
Imagawa E., Higashimoto K., Sakai Y., Numakura C., Okamoto N.,
Matsunaga S., Ryo A., Sato Y., Sanefuji M., Ihara K., Takada Y.,
Nishimura G., Saitsu H., Mizuguchi T., Miyatake S., Nakashima M.,
Miyake N., Soejima H., Matsumoto N.;
"Mutations in genes encoding polycomb repressive complex 2 subunits
cause Weaver syndrome.";
Hum. Mutat. 38:637-648(2017).
-!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-
27' (H3K27me) of histone H3, leading to transcriptional repression
of the affected target gene. Able to mono-, di- and trimethylate
'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3,
respectively. Displays a preference for substrates with less
methylation, loses activity when progressively more methyl groups
are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2
(PubMed:22323599). Compared to EZH1-containing complexes, it is
more abundant in embryonic stem cells and plays a major role in
forming H3K27me3, which is required for embryonic stem cell
identity and proper differentiation. The PRC2/EED-EZH2 complex may
also serve as a recruiting platform for DNA methyltransferases,
thereby linking two epigenetic repression systems. Genes repressed
by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A
and retinoic acid target genes. EZH2 can also methylate non-
histone proteins such as the transcription factor GATA4 and the
nuclear receptor RORA. Regulates the circadian clock via histone
methylation at the promoter of the circadian genes. Essential for
the CRY1/2-mediated repression of the transcriptional activation
of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di
and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters
which is necessary for the CRY1/2 proteins to inhibit
transcription. {ECO:0000269|PubMed:14532106,
ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737,
ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16179254,
ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:16618801,
ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:16936726,
ECO:0000269|PubMed:17210787, ECO:0000269|PubMed:17344414,
ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:19026781,
ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:22323599,
ECO:0000269|PubMed:23063525, ECO:0000269|PubMed:24474760}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:22323599}.
-!- SUBUNIT: Binds ATRX via the SET domain (Probable). Component of
the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4
and RBBP7 and possibly AEBP2. The minimum components required for
methyltransferase activity of the PRC2/EED-EZH2 complex are EED,
EZH2 and SUZ12. The PRC2 complex may also interact with DNMT1,
DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via
the SUZ12 subunit. Interacts with HDAC1 and HDAC2. Interacts with
PRAME. Interacts with CDYL. Interacts with CLOCK, ARNTL/BMAL1 and
CRY1 (By similarity). Interacts with DNMT3L; the interaction is
direct (By similarity). {ECO:0000250|UniProtKB:Q61188,
ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:11158321,
ECO:0000269|PubMed:12351676, ECO:0000269|PubMed:12435631,
ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16179254,
ECO:0000269|PubMed:16224021, ECO:0000269|PubMed:16357870,
ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464,
ECO:0000269|PubMed:19026781, ECO:0000269|PubMed:22009739,
ECO:0000269|PubMed:9499421, ECO:0000269|PubMed:9584199,
ECO:0000305}.
-!- INTERACTION:
Q8IXJ9:ASXL1; NbExp=6; IntAct=EBI-530054, EBI-1646500;
P46100:ATRX; NbExp=2; IntAct=EBI-530054, EBI-396461;
Q96MT8:CEP63; NbExp=3; IntAct=EBI-530054, EBI-741977;
P26358:DNMT1; NbExp=8; IntAct=EBI-530054, EBI-719459;
Q9Y6K1:DNMT3A; NbExp=6; IntAct=EBI-530054, EBI-923653;
Q9UBC3:DNMT3B; NbExp=14; IntAct=EBI-530054, EBI-80125;
Q9CWR8:Dnmt3l (xeno); NbExp=2; IntAct=EBI-530054, EBI-3043871;
O75530:EED; NbExp=11; IntAct=EBI-530054, EBI-923794;
P60411:KRTAP10-9; NbExp=4; IntAct=EBI-10699473, EBI-10172052;
Q9Y4K0:LOXL2; NbExp=2; IntAct=EBI-530054, EBI-7172227;
O43189:PHF1; NbExp=4; IntAct=EBI-530054, EBI-530034;
Q15156:PML-RAR; NbExp=8; IntAct=EBI-530054, EBI-867256;
P10276:RARA; NbExp=2; IntAct=EBI-530054, EBI-413374;
P40763:STAT3; NbExp=5; IntAct=EBI-530054, EBI-518675;
O43463:SUV39H1; NbExp=2; IntAct=EBI-530054, EBI-349968;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12101246,
ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15231737,
ECO:0000269|PubMed:9584199}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q15910-1; Sequence=Displayed;
Name=2;
IsoId=Q15910-2; Sequence=VSP_038815;
Name=3;
IsoId=Q15910-3; Sequence=VSP_038814;
Name=4;
IsoId=Q15910-4; Sequence=VSP_038813;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q15910-5; Sequence=VSP_038813, VSP_038816;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in many tissues. Overexpressed in
numerous tumor types including carcinomas of the breast, colon,
larynx, lymphoma and testis. {ECO:0000269|PubMed:14532106}.
-!- DEVELOPMENTAL STAGE: Expression decreases during senescence of
embryonic fibroblasts (HEFs). Expression peaks at the G1/S phase
boundary. {ECO:0000269|PubMed:14532106,
ECO:0000269|PubMed:15208672, ECO:0000269|PubMed:17344414}.
-!- INDUCTION: Expression is induced by E2F1, E2F2 and E2F3.
Expression is reduced in cells subject to numerous types of stress
including UV-, IR- and bleomycin-induced DNA damage and by
activation of p53/TP53. {ECO:0000269|PubMed:14532106,
ECO:0000269|PubMed:15208672, ECO:0000269|PubMed:17344414}.
-!- PTM: Phosphorylated by AKT1. Phosphorylation by AKT1 reduces
methyltransferase activity. Phosphorylation at Thr-345 by CDK1 and
CDK2 promotes maintenance of H3K27me3 levels at EZH2-target loci,
thus leading to epigenetic gene silencing.
{ECO:0000269|PubMed:16224021, ECO:0000269|PubMed:20935635}.
-!- PTM: Sumoylated. {ECO:0000269|PubMed:18628979}.
-!- PTM: Glycosylated: O-GlcNAcylation at Ser-75 by OGT increases
stability of EZH2 and facilitates the formation of H3K27me3 by the
PRC2/EED-EZH2 complex. {ECO:0000269|PubMed:24474760}.
-!- DISEASE: Weaver syndrome (WVS) [MIM:277590]: A syndrome of
accelerated growth and osseous maturation, unusual craniofacial
appearance, hoarse and low-pitched cry, and hypertonia with
camptodactyly. Distinguishing features of Weaver syndrome include
broad forehead and face, ocular hypertelorism, prominent wide
philtrum, micrognathia, deep horizontal chin groove, and deep-set
nails. In addition, carpal bone development is advanced over the
rest of the hand. {ECO:0000269|PubMed:22177091,
ECO:0000269|PubMed:22190405, ECO:0000269|PubMed:23239504,
ECO:0000269|PubMed:26694085, ECO:0000269|PubMed:28229514}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. EZ subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- CAUTION: Two variants of the PRC2 complex have been described,
termed PRC3 and PRC4. Each of the three complexes may include a
different complement of EED isoforms, although the precise
sequences of the isoforms in each complex have not been
determined. The PRC2 and PRC4 complexes may also methylate 'Lys-
26' of histone H1 in addition to 'Lys-27' of histone H3
(PubMed:15099518 and PubMed:15684044), although other studies have
demonstrated no methylation of 'Lys-26' of histone H1 by PRC2
(PubMed:16431907). {ECO:0000305|PubMed:16431907}.
-!- SEQUENCE CAUTION:
Sequence=AAS07448.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X95653; CAA64955.1; -; mRNA.
EMBL; U61145; AAC51520.1; -; mRNA.
EMBL; AK302216; BAH13652.1; -; mRNA.
EMBL; AK092676; BAG52592.1; -; mRNA.
EMBL; AK293239; BAH11472.1; -; mRNA.
EMBL; AK314291; BAG36948.1; -; mRNA.
EMBL; AC006323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073140; AAS07448.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471146; EAW80067.1; -; Genomic_DNA.
EMBL; CH471146; EAW80070.1; -; Genomic_DNA.
EMBL; BC010858; AAH10858.1; -; mRNA.
EMBL; U52965; AAC50591.1; -; Genomic_DNA.
CCDS; CCDS56516.1; -. [Q15910-1]
CCDS; CCDS56517.1; -. [Q15910-5]
CCDS; CCDS56518.1; -. [Q15910-4]
CCDS; CCDS5891.1; -. [Q15910-2]
CCDS; CCDS5892.1; -. [Q15910-3]
PIR; G02838; G02838.
RefSeq; NP_001190176.1; NM_001203247.1. [Q15910-1]
RefSeq; NP_001190177.1; NM_001203248.1. [Q15910-4]
RefSeq; NP_001190178.1; NM_001203249.1. [Q15910-5]
RefSeq; NP_004447.2; NM_004456.4. [Q15910-2]
RefSeq; NP_694543.1; NM_152998.2. [Q15910-3]
RefSeq; XP_011514186.1; XM_011515884.2. [Q15910-2]
UniGene; Hs.444082; -.
UniGene; Hs.732308; -.
PDB; 2C6V; Model; -; A=508-734.
PDB; 4MI0; X-ray; 2.00 A; A=520-746.
PDB; 4MI5; X-ray; 2.00 A; A=521-746.
PDB; 5GSA; X-ray; 2.49 A; C/D=40-68.
PDB; 5H14; X-ray; 1.90 A; C/D=40-68.
PDB; 5H15; X-ray; 2.27 A; C/D=40-68.
PDB; 5H17; X-ray; 2.30 A; B=40-68.
PDB; 5H19; X-ray; 1.90 A; B=40-68.
PDB; 5H24; X-ray; 2.50 A; C/D=40-68.
PDB; 5H25; X-ray; 2.88 A; C/D=40-68.
PDB; 5HYN; X-ray; 2.95 A; A/F/K/Q=1-746.
PDB; 5IJ7; X-ray; 2.62 A; A/B=429-487, A/B=511-746.
PDB; 5IJ8; X-ray; 2.99 A; A/B=429-487, A/B=511-531, A/B=533-746.
PDB; 5LS6; X-ray; 3.47 A; A/D/G/J=1-385, A/D/G/J=421-746.
PDB; 5U5T; X-ray; 1.60 A; C/D=39-68.
PDB; 5U62; X-ray; 1.90 A; C/D=39-68.
PDB; 5WUK; X-ray; 2.03 A; B=41-68.
PDBsum; 2C6V; -.
PDBsum; 4MI0; -.
PDBsum; 4MI5; -.
PDBsum; 5GSA; -.
PDBsum; 5H14; -.
PDBsum; 5H15; -.
PDBsum; 5H17; -.
PDBsum; 5H19; -.
PDBsum; 5H24; -.
PDBsum; 5H25; -.
PDBsum; 5HYN; -.
PDBsum; 5IJ7; -.
PDBsum; 5IJ8; -.
PDBsum; 5LS6; -.
PDBsum; 5U5T; -.
PDBsum; 5U62; -.
PDBsum; 5WUK; -.
ProteinModelPortal; Q15910; -.
SMR; Q15910; -.
BioGrid; 108446; 280.
DIP; DIP-34002N; -.
IntAct; Q15910; 108.
MINT; MINT-1371596; -.
STRING; 9606.ENSP00000320147; -.
BindingDB; Q15910; -.
ChEMBL; CHEMBL2189110; -.
GuidetoPHARMACOLOGY; 2654; -.
iPTMnet; Q15910; -.
PhosphoSitePlus; Q15910; -.
BioMuta; EZH2; -.
DMDM; 3334180; -.
EPD; Q15910; -.
MaxQB; Q15910; -.
PaxDb; Q15910; -.
PeptideAtlas; Q15910; -.
PRIDE; Q15910; -.
DNASU; 2146; -.
Ensembl; ENST00000320356; ENSP00000320147; ENSG00000106462. [Q15910-2]
Ensembl; ENST00000350995; ENSP00000223193; ENSG00000106462. [Q15910-3]
Ensembl; ENST00000460911; ENSP00000419711; ENSG00000106462. [Q15910-1]
Ensembl; ENST00000476773; ENSP00000419050; ENSG00000106462. [Q15910-5]
Ensembl; ENST00000478654; ENSP00000417062; ENSG00000106462. [Q15910-5]
Ensembl; ENST00000483967; ENSP00000419856; ENSG00000106462. [Q15910-4]
GeneID; 2146; -.
KEGG; hsa:2146; -.
UCSC; uc003wfb.3; human. [Q15910-1]
CTD; 2146; -.
DisGeNET; 2146; -.
GeneCards; EZH2; -.
GeneReviews; EZH2; -.
HGNC; HGNC:3527; EZH2.
HPA; CAB009589; -.
HPA; HPA029131; -.
MalaCards; EZH2; -.
MIM; 277590; phenotype.
MIM; 601573; gene.
neXtProt; NX_Q15910; -.
OpenTargets; ENSG00000106462; -.
Orphanet; 3447; Weaver syndrome.
PharmGKB; PA27939; -.
eggNOG; KOG1079; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOVERGEN; HBG002453; -.
InParanoid; Q15910; -.
KO; K11430; -.
OMA; VYNYTPC; -.
PhylomeDB; Q15910; -.
TreeFam; TF314509; -.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLink; Q15910; -.
SIGNOR; Q15910; -.
ChiTaRS; EZH2; human.
GeneWiki; EZH2; -.
GenomeRNAi; 2146; -.
PRO; PR:Q15910; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106462; -.
CleanEx; HS_EZH2; -.
ExpressionAtlas; Q15910; baseline and differential.
Genevisible; Q15910; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0045120; C:pronucleus; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:MGI.
GO; GO:0070878; F:primary miRNA binding; IEA:Ensembl.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0035984; P:cellular response to trichostatin A; IEA:Ensembl.
GO; GO:0021695; P:cerebellar cortex development; IEA:Ensembl.
GO; GO:0006325; P:chromatin organization; TAS:ProtInc.
GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
GO; GO:0070314; P:G1 to G0 transition; IEA:Ensembl.
GO; GO:0036333; P:hepatocyte homeostasis; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0070734; P:histone H3-K27 methylation; IDA:UniProtKB.
GO; GO:0098532; P:histone H3-K27 trimethylation; IEA:Ensembl.
GO; GO:0016571; P:histone methylation; IMP:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0045605; P:negative regulation of epidermal cell differentiation; IEA:Ensembl.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:UniProtKB.
GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IMP:UniProtKB.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0051154; P:negative regulation of striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0014013; P:regulation of gliogenesis; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:1904772; P:response to tetrachloromethane; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR026489; CXC_dom.
InterPro; IPR021654; EZH1/EZH2.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR001214; SET_dom.
InterPro; IPR033467; Tesmin/TSO1-like_CXC.
Pfam; PF11616; EZH2_WD-Binding; 1.
Pfam; PF00856; SET; 1.
SMART; SM01114; CXC; 1.
SMART; SM00717; SANT; 2.
SMART; SM00317; SET; 1.
PROSITE; PS51633; CXC; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Biological rhythms;
Chromatin regulator; Complete proteome; Disease mutation;
Glycoprotein; Isopeptide bond; Methyltransferase; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repressor;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Ubl conjugation.
CHAIN 1 746 Histone-lysine N-methyltransferase EZH2.
/FTId=PRO_0000213992.
DOMAIN 503 605 CXC. {ECO:0000255|PROSITE-
ProRule:PRU00970}.
DOMAIN 612 727 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
REGION 1 340 Interaction with DNMT1, DNMT3A and
DNMT3B.
REGION 39 68 Interaction with EED. {ECO:0000250}.
REGION 329 522 Interaction with CDYL.
{ECO:0000269|PubMed:22009739}.
COMPBIAS 523 605 Cys-rich.
MOD_RES 21 21 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:16224021}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 339 339 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 345 345 Phosphothreonine; by CDK1 and CDK2.
{ECO:0000269|PubMed:20935635}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 367 367 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 487 487 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CARBOHYD 75 75 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:24474760}.
CROSSLNK 634 634 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 74 82 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038813.
VAR_SEQ 83 121 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038814.
VAR_SEQ 297 298 HP -> HRKCNYS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038815.
VAR_SEQ 511 553 DGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSS
EC -> G (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038816.
VARIANT 132 132 P -> S (in WVS; decreased histone
methyltransferase activity;
dbSNP:rs193921148).
{ECO:0000269|PubMed:22177091,
ECO:0000269|PubMed:26694085}.
/FTId=VAR_067595.
VARIANT 133 133 Y -> C (in WVS; decreased histone
methyltransferase activity).
{ECO:0000269|PubMed:26694085}.
/FTId=VAR_078320.
VARIANT 134 134 M -> T (in WVS).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078321.
VARIANT 153 153 Missing (in WVS; decreased histone
methyltransferase activity).
{ECO:0000269|PubMed:22177091,
ECO:0000269|PubMed:26694085}.
/FTId=VAR_067596.
VARIANT 156 156 K -> E (in WVS).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078322.
VARIANT 185 185 D -> H (polymorhism; decreased histone
methyltransferase activity;
dbSNP:rs2302427).
{ECO:0000269|PubMed:26694085}.
/FTId=VAR_055795.
VARIANT 279 279 H -> R (in WVS).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078323.
VARIANT 571 571 C -> W (found in a patient with
myelodysplastic syndrome and
myelodysplastic-myeloproliferative
neoplasms; somatic mutation; loss of
histone methyltransferase activity).
{ECO:0000269|PubMed:20601953}.
/FTId=VAR_078324.
VARIANT 621 621 V -> M (in WVS; unknown pathological
significance; dbSNP:rs587783625).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078325.
VARIANT 641 641 Y -> C (in a patient with diffuse large
B-cell lymphoma; somatic mutation;
changed substrate preferences; prefers
substrates with greater methylation
H3K27me0 {ECO:0000269|PubMed:20081860,
ECO:0000269|PubMed:20601953,
ECO:0000269|PubMed:22323599}.
/FTId=VAR_067228.
VARIANT 641 641 Y -> F (found in a patient with
follicular lymphoma; also in diffuse
large B-cell lymphoma; somatic mutation;
changed substrate preferences; prefers
substrates with greater methylation
H3K27me0 {ECO:0000269|PubMed:20081860,
ECO:0000269|PubMed:22323599}.
/FTId=VAR_067229.
VARIANT 641 641 Y -> H (found in patients with follicular
lymphoma; also in diffuse large B-cell
lymphoma; somatic mutation; changed
substrate preferences; prefers substrates
with greater methylation
H3K27me0 {ECO:0000269|PubMed:20081860,
ECO:0000269|PubMed:22323599}.
/FTId=VAR_067230.
VARIANT 641 641 Y -> N (found in patients with follicular
lymphoma; also in diffuse large B-cell
lymphoma; somatic mutation; changed
substrate preferences; prefers substrates
with greater methylation
H3K27me0 {ECO:0000269|PubMed:20081860,
ECO:0000269|PubMed:22323599}.
/FTId=VAR_067231.
VARIANT 641 641 Y -> S (found in patients with follicular
lymphoma; also in diffuse large B-cell
lymphoma; somatic mutation).
{ECO:0000269|PubMed:20081860}.
/FTId=VAR_067232.
VARIANT 658 658 Y -> N (in WVS).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078326.
VARIANT 677 677 A -> G (found in a patient with B-cell
lymphoma; increased hypertrimethylation
of H3K27; changed substrate preferences;
confers biochemical activity independent
of H3K27 methylation state).
{ECO:0000269|PubMed:22323599}.
/FTId=VAR_078327.
VARIANT 677 677 A -> T (in WVS; dbSNP:rs397515547).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078328.
VARIANT 679 679 R -> C (in WVS; decreased histone
methyltransferase activity;
dbSNP:rs587783626).
{ECO:0000269|PubMed:22190405,
ECO:0000269|PubMed:26694085}.
/FTId=VAR_078329.
VARIANT 685 685 R -> C (found in a patient with myeloid
disorders; somatic mutation; loss of
histone methyltransferase activity).
{ECO:0000269|PubMed:20601953}.
/FTId=VAR_078330.
VARIANT 685 685 R -> H (in a patient with chronic
myelomonocytic leukemia).
{ECO:0000269|PubMed:21828135}.
/FTId=VAR_067233.
VARIANT 689 689 H -> Y (in WVS; decreased histone
methyltransferase activity;
dbSNP:rs193921147).
{ECO:0000269|PubMed:22177091,
ECO:0000269|PubMed:26694085}.
/FTId=VAR_067597.
VARIANT 690 690 S -> L (in WVS).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078331.
VARIANT 726 726 Y -> D (found in a patient with chronic
myelomonocytic leukemia; somatic
mutation; loss of histone
methyltransferase activity).
{ECO:0000269|PubMed:20601953}.
/FTId=VAR_078332.
VARIANT 728 746 Missing (in WVS).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078333.
VARIANT 736 736 Y -> C (in WVS).
{ECO:0000269|PubMed:22190405}.
/FTId=VAR_078334.
VARIANT 740 740 E -> K (in WVS; unknown pathological
significance; dbSNP:rs397515548).
{ECO:0000269|PubMed:23239504}.
/FTId=VAR_078335.
MUTAGEN 21 21 S->A: Enhances methyltransferase activity
towards 'Lys-27' of histone H3 and
abrogates phosphorylation by PKB/AKT1.
{ECO:0000269|PubMed:16224021}.
MUTAGEN 21 21 S->D: Reduces methyltransferase activity
towards 'Lys-27' of histone H3 and
abrogates phosphorylation by PKB/AKT1.
{ECO:0000269|PubMed:16224021}.
MUTAGEN 75 75 S->A: Reduced protein stability.
{ECO:0000269|PubMed:24474760}.
MUTAGEN 345 345 T->A: Impaired CDK1- and CDK-2 mediated
phosphorylation and subsequent gene
silencing. Altered EZH2-mediated cell
proliferation and migration.
{ECO:0000269|PubMed:20935635}.
MUTAGEN 588 588 C->Y: Strongly impairs methyltransferase
activity towards 'Lys-27' of histone H3.
{ECO:0000269|PubMed:12435631}.
MUTAGEN 667 667 F->I: Strongly decreases histone
methyltransferase activity.
{ECO:0000269|PubMed:26694085}.
MUTAGEN 689 689 H->A: Abrogates methyltransferase
activity. {ECO:0000269|PubMed:12435631,
ECO:0000269|PubMed:18285464}.
CONFLICT 39 39 K -> N (in Ref. 3; BAG52592).
{ECO:0000305}.
CONFLICT 224 224 F -> L (in Ref. 1; CAA64955).
{ECO:0000305}.
CONFLICT 724 724 F -> V (in Ref. 1; CAA64955).
{ECO:0000305}.
HELIX 44 62 {ECO:0000244|PDB:5U5T}.
STRAND 82 87 {ECO:0000244|PDB:5HYN}.
STRAND 94 97 {ECO:0000244|PDB:5HYN}.
STRAND 99 101 {ECO:0000244|PDB:5HYN}.
STRAND 126 129 {ECO:0000244|PDB:5HYN}.
HELIX 135 138 {ECO:0000244|PDB:5HYN}.
TURN 139 143 {ECO:0000244|PDB:5HYN}.
HELIX 144 152 {ECO:0000244|PDB:5HYN}.
TURN 153 155 {ECO:0000244|PDB:5HYN}.
STRAND 161 163 {ECO:0000244|PDB:5LS6}.
HELIX 168 181 {ECO:0000244|PDB:5HYN}.
HELIX 221 230 {ECO:0000244|PDB:5HYN}.
TURN 232 234 {ECO:0000244|PDB:5HYN}.
HELIX 237 248 {ECO:0000244|PDB:5HYN}.
STRAND 264 266 {ECO:0000244|PDB:5LS6}.
HELIX 274 284 {ECO:0000244|PDB:5HYN}.
TURN 287 289 {ECO:0000244|PDB:5HYN}.
STRAND 291 293 {ECO:0000244|PDB:5HYN}.
TURN 304 306 {ECO:0000244|PDB:5HYN}.
HELIX 332 343 {ECO:0000244|PDB:5HYN}.
HELIX 434 443 {ECO:0000244|PDB:5IJ7}.
TURN 444 446 {ECO:0000244|PDB:5IJ7}.
HELIX 451 458 {ECO:0000244|PDB:5IJ7}.
STRAND 459 461 {ECO:0000244|PDB:5IJ7}.
HELIX 463 471 {ECO:0000244|PDB:5IJ7}.
STRAND 526 528 {ECO:0000244|PDB:5HYN}.
HELIX 535 538 {ECO:0000244|PDB:4MI0}.
STRAND 563 565 {ECO:0000244|PDB:4MI0}.
HELIX 572 575 {ECO:0000244|PDB:4MI0}.
TURN 582 584 {ECO:0000244|PDB:4MI0}.
STRAND 587 589 {ECO:0000244|PDB:4MI0}.
STRAND 590 592 {ECO:0000244|PDB:5LS6}.
STRAND 594 596 {ECO:0000244|PDB:5HYN}.
STRAND 600 603 {ECO:0000244|PDB:4MI0}.
HELIX 605 608 {ECO:0000244|PDB:4MI0}.
STRAND 614 618 {ECO:0000244|PDB:4MI0}.
STRAND 620 630 {ECO:0000244|PDB:4MI0}.
STRAND 637 640 {ECO:0000244|PDB:4MI0}.
STRAND 643 647 {ECO:0000244|PDB:4MI0}.
HELIX 648 656 {ECO:0000244|PDB:4MI0}.
STRAND 666 668 {ECO:0000244|PDB:4MI0}.
STRAND 670 676 {ECO:0000244|PDB:4MI0}.
TURN 678 680 {ECO:0000244|PDB:4MI0}.
HELIX 683 686 {ECO:0000244|PDB:4MI0}.
STRAND 687 689 {ECO:0000244|PDB:4MI0}.
STRAND 694 702 {ECO:0000244|PDB:4MI0}.
STRAND 705 714 {ECO:0000244|PDB:4MI0}.
STRAND 721 723 {ECO:0000244|PDB:5LS6}.
HELIX 726 730 {ECO:0000244|PDB:5IJ7}.
SEQUENCE 746 AA; 85363 MW; 1B5029EB9D509BE5 CRC64;
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL ERTEILNQEW
KQRRIQPVHI LTSVSSLRGT RECSVTSDLD FPTQVIPLKT LNAVASVPIM YSWSPLQQNF
MVEDETVLHN IPYMGDEVLD QDGTFIEELI KNYDGKVHGD RECGFINDEI FVELVNALGQ
YNDDDDDDDG DDPEEREEKQ KDLEDHRDDK ESRPPRKFPS DKIFEAISSM FPDKGTAEEL
KEKYKELTEQ QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH
ATPNTYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP GGRRRGRLPN
NSSRPSTPTI NVLESKDTDS DREAGTETGG ENNDKEEEEK KDETSSSSEA NSRCQTPIKM
KPNIEPPENV EWSGAEASMF RVLIGTYYDN FCAIARLIGT KTCRQVYEFR VKESSIIAPA
PAEDVDTPPR KKKRKHRLWA AHCRKIQLKK DGSSNHVYNY QPCDHPRQPC DSSCPCVIAQ
NFCEKFCQCS SECQNRFPGC RCKAQCNTKQ CPCYLAVREC DPDLCLTCGA ADHWDSKNVS
CKNCSIQRGS KKHLLLAPSD VAGWGIFIKD PVQKNEFISE YCGEIISQDE ADRRGKVYDK
YMCSFLFNLN NDFVVDATRK GNKIRFANHS VNPNCYAKVM MVNGDHRIGI FAKRAIQTGE
ELFFDYRYSQ ADALKYVGIE REMEIP


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CSB-EL007913MO Mouse Histone-lysine N-methyltransferase EZH2(EZH2) ELISA kit SpeciesMouse 96T
CSB-EL007913HU Human Histone-lysine N-methyltransferase EZH2(EZH2) ELISA kit 96T
CSB-EL007913MO Mouse Histone-lysine N-methyltransferase EZH2(EZH2) ELISA kit 96T


 

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