[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1006/geno.1996.0588; PubMed=8954776 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1093/emboj/16.11.3219; PubMed=9214638 [NCBI, ExPASy, EBI, Israel, Japan] 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 GENOMIC DNA]. DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-746. PubMed=8649418 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	INTERACTION WITH ATRX. DOI=10.1093/hmg/7.4.679; PubMed=9499421 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	INTERACTION WITH EED, AND SUBCELLULAR LOCATION. PubMed=9584199 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	INTERACTION WITH EED; HDAC1 AND HDAC2. DOI=10.1038/70602; PubMed=10581039 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	INTERACTION WITH EED. DOI=10.1128/MCB.21.4.1360-1369.2001; PubMed=11158321 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	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. DOI=10.1101/gad.1035902; PubMed=12435631 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[10]	SUBCELLULAR LOCATION. DOI=10.1128/MCB.22.15.5539-5553.2002; PubMed=12101246 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EED; RBBP4; RBBP7 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX. DOI=10.1126/science.1076997; PubMed=12351676 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, AND TISSUE SPECIFICITY. DOI=10.1093/emboj/cdg542; PubMed=14532106 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	FUNCTION, INTERACTION WITH EED AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX. DOI=10.1038/sj.emboj.7600402; PubMed=15385962 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[14]	FUNCTION, AND SUBCELLULAR LOCATION. DOI=10.1101/gad.1200204; PubMed=15231737 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2; RBBP4; RBBP7 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND PRC3 COMPLEXES. DOI=10.1016/S1097-2765(04)00185-6; PubMed=15099518 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED; EZH2; RBBP4 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX. DOI=10.1016/j.molcel.2004.06.020; PubMed=15225548 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	DEVELOPMENTAL STAGE, AND INDUCTION. DOI=10.1038/sj.onc.1207706; PubMed=15208672 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[19]	CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4; RBBP7; SUZ12 AND SIRT1, AND METHYLTRANSFERASE ACTIVITY OF THE PRC4 COMPLEX. DOI=10.1073/pnas.0409875102; PubMed=15684044 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	INTERACTION WITH EED AND SUZ12, PHOSPHORYLATION BY AKT1, AND MUTAGENESIS OF SER-21. DOI=10.1126/science.1118947; PubMed=16224021 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	FUNCTION. DOI=10.1101/gad.381706; PubMed=16618801 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX. DOI=10.1074/jbc.M513425200; PubMed=16431907 [NCBI, ExPASy, EBI, Israel, Japan] Martin C., Cao R., Zhang Y.; "Substrate preferences of the EZH2 histone methyltransferase complex."; J. Biol. Chem. 281:8365-8370(2006).
[24]	FUNCTION, AND INTERACTION OF THE PRC2 COMPLEX WITH DNMT1; DNMT3A AND DNMT3B. DOI=10.1038/nature04431; PubMed=16357870 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[25]	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).
[26]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[27]	FUNCTION. DOI=10.1038/nsmb1142; PubMed=16936726 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[28]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan] Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; "Phosphoproteome analysis of the human mitotic spindle."; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[29]	FUNCTION. DOI=10.1101/gad.1499407; PubMed=17210787 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[30]	FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION. DOI=10.1101/gad.415507; PubMed=17344414 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[31]	DE NOVO DNA METHYLATION OF PRC2 TARGET GENES. DOI=10.1038/ng1950; PubMed=17200670 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[32]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[33]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[34]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[35]	FUNCTION, AND IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX. DOI=10.1016/j.molcel.2008.11.004; PubMed=19026781 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[36]	IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX. DOI=10.1128/MCB.01589-07; PubMed=18086877 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[37]	FUNCTION, INTERACTION WITH EED; SUZ12 AND PHF1, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, AND MUTAGENESIS OF HIS-689. DOI=10.1128/MCB.02017-07; PubMed=18285464 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[38]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-339; SER-366; THR-367 AND THR-487, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' 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. Compared to EZH2-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 and CDKN2A.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N⁶-methyl-L-lysine.
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.
INTERACTION:
P26358:DNMT1; NbExp=3; IntAct=EBI-530054, EBI-719459;
Q9Y6K1:DNMT3A; NbExp=3; IntAct=EBI-530054, EBI-923653;
Q9UBC3:DNMT3B; NbExp=3; IntAct=EBI-530054, EBI-80125;
P10276:RARA; NbExp=2; IntAct=EBI-530054, EBI-413374;
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Expressed in many tissues. Overexpressed in numerous tumor types including carcinomas of the breast, colon, larynx, lymphoma and testis.
DEVELOPMENTAL STAGE: Expression decreases during senescence of embryonic fibroblasts (HEFs). Expression peaks at the G1/S phase boundary.
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 TP53/p53.
PTM: Phosphorylated by AKT1. Phosphorylation by AKT1 reduces methyltransferase activity.
SIMILARITY: Belongs to the histone-lysine methyltransferase family. EZ subfamily.
SIMILARITY: Contains 1 SET domain.
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).

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X95653; CAA64955.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U61145; AAC51520.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006323; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC073140; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
U52965; AAC50591.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00376787; -.

G02838; G02838.

3D structure databases

PDB

2C6V; Model; -; A=508-734.

[ExPASy / RCSB / EBI]

PDBsum

2C6V; -.

ModBase

Q15910.

Protein-protein interaction databases

IntAct

Q15910; 20.

PTM databases

PhosphoSite

Q15910; -.

Organism-specific databases

GC07M148135; -.

HGNC:3527; EZH2.

CAB009589; -.

601573; gene. [NCBI / EBI]

PharmGKB

PA27939; -.

Gene expression databases

Q15910; -.

Q15910; -.

HS_EZH2; -.

ENSG00000106462; Homo sapiens.

Ontologies

GO:0035098;	Cellular component: ESC/E(Z) complex (inferred from direct assay from MGI).
GO:0003677;	Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0018024;	Molecular function: histone-lysine N-methyltransferase activity (inferred from electronic annotation from EC).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0016568;	Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (traceable author statement from ProtInc).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001005; SANT_DNA-bd.
IPR001214; SET.
Graphical view of domain structure.

Pfam

PF00856; SET; 1.
Pfam graphical view of domain structure.

SMART

SM00717; SANT; 2.
SM00317; SET; 1.
SMART graphical view of domain structure.

PROSITE

PS50280; SET; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q15910; -.

Genome annotation databases

Ensembl

ENSG00000106462; Homo sapiens. [Contig view]

Phylogenomic databases

HOVERGEN

Q15910; -.

Other

EZH2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chromatin regulator; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; Repressor; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 746`	`746`	`Histone-lysine N-methyltransferase EZH2.`	`PRO_0000213992`
`DOMAIN`	`611 731`	`121`	`SET.`
`REGION`	`1 340`	`340`	`Interaction with DNMT1, DNMT3A and DNMT3B.`
`REGION`	`39 68`	`30`	`Interaction with EED (By similarity).`
`COMPBIAS`	`523 605`	`83`	`Cys-rich.`
`MOD_RES`	`21 21`		`Phosphoserine; by PKB/AKT1.`
`MOD_RES`	`339 339`		`Phosphothreonine.`
`MOD_RES`	`366 366`		`Phosphoserine.`
`MOD_RES`	`367 367`		`Phosphothreonine.`
`MOD_RES`	`380 380`		`Phosphoserine.`
`MOD_RES`	`487 487`		`Phosphothreonine.`
`VARIANT`	`185 185`	`1`	`D -> H (in dbSNP:rs2302427 [NCBI]).`	`VAR_055795`
`MUTAGEN`	`21 21`		`S->A: Enhances methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1.`
`MUTAGEN`	`21 21`		`S->D: Reduces methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1.`
`MUTAGEN`	`588 588`		`C->Y: Strongly impairs methyltransferase activity towards 'Lys-27' of histone H3.`
`MUTAGEN`	`689 689`		`H->A: Abrogates methyltransferase activity.`
`CONFLICT`	`224 224`		`F -> L (in Ref. 1; CAA64955).`
`CONFLICT`	`724 724`		`F -> V (in Ref. 1; CAA64955).`

Sequence information

Length: 746 AA [This is the length of the unprocessed precursor]

Molecular weight: 85363 Da [This is the MW of the unprocessed precursor]

CRC64: 1B5029EB9D509BE5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL ERTEILNQEW 

        70         80         90        100        110        120 
KQRRIQPVHI LTSVSSLRGT RECSVTSDLD FPTQVIPLKT LNAVASVPIM YSWSPLQQNF 

       130        140        150        160        170        180 
MVEDETVLHN IPYMGDEVLD QDGTFIEELI KNYDGKVHGD RECGFINDEI FVELVNALGQ 

       190        200        210        220        230        240 
YNDDDDDDDG DDPEEREEKQ KDLEDHRDDK ESRPPRKFPS DKIFEAISSM FPDKGTAEEL 

       250        260        270        280        290        300 
KEKYKELTEQ QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH 

       310        320        330        340        350        360 
ATPNTYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP GGRRRGRLPN 

       370        380        390        400        410        420 
NSSRPSTPTI NVLESKDTDS DREAGTETGG ENNDKEEEEK KDETSSSSEA NSRCQTPIKM 

       430        440        450        460        470        480 
KPNIEPPENV EWSGAEASMF RVLIGTYYDN FCAIARLIGT KTCRQVYEFR VKESSIIAPA 

       490        500        510        520        530        540 
PAEDVDTPPR KKKRKHRLWA AHCRKIQLKK DGSSNHVYNY QPCDHPRQPC DSSCPCVIAQ 

       550        560        570        580        590        600 
NFCEKFCQCS SECQNRFPGC RCKAQCNTKQ CPCYLAVREC DPDLCLTCGA ADHWDSKNVS 

       610        620        630        640        650        660 
CKNCSIQRGS KKHLLLAPSD VAGWGIFIKD PVQKNEFISE YCGEIISQDE ADRRGKVYDK 

       670        680        690        700        710        720 
YMCSFLFNLN NDFVVDATRK GNKIRFANHS VNPNCYAKVM MVNGDHRIGI FAKRAIQTGE 

       730        740 
ELFFDYRYSQ ADALKYVGIE REMEIP

Q15910 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools