Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 EZH2_MOUSE              Reviewed;         746 AA.
Q61188; Q99L74; Q9R090;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 163.
RecName: Full=Histone-lysine N-methyltransferase EZH2 {ECO:0000305};
EC=2.1.1.43;
AltName: Full=ENX-1;
AltName: Full=Enhancer of zeste homolog 2;
Name=Ezh2 {ECO:0000312|MGI:MGI:107940}; Synonyms=Enx1h;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8861097; DOI=10.1016/0925-4773(96)00499-6;
Hobert O., Sures I., Ciossek T., Fuchs M., Ullrich A.;
"Isolation and developmental expression analysis of Enx-1, a novel
mouse Polycomb group gene.";
Mech. Dev. 55:171-184(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary tumor;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-497.
STRAIN=129/Sv;
PubMed=10051331; DOI=10.1007/s003359900993;
Laible G., Haynes A.R., Lebersorger A., O'Carroll D., Mattei M.-G.,
Denny P., Brown S.D.M., Jenuwein T.;
"The murine polycomb-group genes ezh1 and ezh2 map close to hox gene
clusters on mouse chromosomes 11 and 6.";
Mamm. Genome 10:311-314(1999).
[5]
INTERACTION WITH EED.
PubMed=9742080; DOI=10.1128/MCB.18.10.5634;
Denisenko O.N., Shnyreva M., Suzuki H., Bomsztyk K.;
"Point mutations in the WD40 domain of Eed block its interaction with
Ezh2.";
Mol. Cell. Biol. 18:5634-5642(1998).
[6]
DISRUPTION PHENOTYPE.
PubMed=11390661; DOI=10.1128/MCB.21.13.4330-4336.2001;
O'Carroll D., Erhardt S., Pagani M., Barton S.C., Surani M.A.,
Jenuwein T.;
"The polycomb-group gene Ezh2 is required for early mouse
development.";
Mol. Cell. Biol. 21:4330-4336(2001).
[7]
SUBCELLULAR LOCATION.
PubMed=12123576; DOI=10.1016/S0960-9822(02)00892-8;
Mak W., Baxter J., Silva J., Newall A.E., Otte A.P., Brockdorff N.;
"Mitotically stable association of polycomb group proteins Eed and
Enx1 with the inactive X chromosome in trophoblast stem cells.";
Curr. Biol. 12:1016-1020(2002).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=12689588; DOI=10.1016/S1534-5807(03)00068-6;
Silva J., Mak W., Zvetkova I., Appanah R., Nesterova T.B., Webster Z.,
Peters A.H.F.M., Jenuwein T., Otte A.P., Brockdorff N.;
"Establishment of histone H3 methylation on the inactive X chromosome
requires transient recruitment of Eed-Enx1 polycomb group complexes.";
Dev. Cell 4:481-495(2003).
[9]
SUBCELLULAR LOCATION.
PubMed=12649488; DOI=10.1126/science.1084274;
Plath K., Fang J., Mlynarczyk-Evans S.K., Cao R., Worringer K.A.,
Wang H., de la Cruz C.C., Otte A.P., Panning B., Zhang Y.;
"Role of histone H3 lysine 27 methylation in X inactivation.";
Science 300:131-135(2003).
[10]
FUNCTION.
PubMed=15520282; DOI=10.1101/gad.1241904;
Caretti G., Di Padova M., Micales B., Lyons G.E., Sartorelli V.;
"The Polycomb Ezh2 methyltransferase regulates muscle gene expression
and skeletal muscle differentiation.";
Genes Dev. 18:2627-2638(2004).
[11]
ERRATUM.
Caretti G., Di Padova M., Micales B., Lyons G.E., Sartorelli V.;
Genes Dev. 19:768-768(2005).
[12]
FUNCTION.
PubMed=15516932; DOI=10.1038/ng1467;
Umlauf D., Goto Y., Cao R., Cerqueira F., Wagschal A., Zhang Y.,
Feil R.;
"Imprinting along the Kcnq1 domain on mouse chromosome 7 involves
repressive histone methylation and recruitment of Polycomb group
complexes.";
Nat. Genet. 36:1296-1300(2004).
[13]
SUBCELLULAR LOCATION.
PubMed=14752160; DOI=10.1126/science.1092674;
Mak W., Nesterova T.B., de Napoles M., Appanah R., Yamanaka S.,
Otte A.P., Brockdorff N.;
"Reactivation of the paternal X chromosome in early mouse embryos.";
Science 303:666-669(2004).
[14]
DEVELOPMENTAL STAGE.
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).
[15]
FUNCTION, AND INTERACTION WITH CLOCK; ARNTL AND CRY1.
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).
[16]
SUBCELLULAR LOCATION.
PubMed=16415857; DOI=10.1038/ncb1351;
Kalantry S., Mills K.C., Yee D., Otte A.P., Panning B., Magnuson T.;
"The Polycomb group protein Eed protects the inactive X-chromosome
from differentiation-induced reactivation.";
Nat. Cell Biol. 8:195-202(2006).
[17]
DEVELOPMENTAL STAGE.
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).
[18]
INTERACTION WITH EED.
PubMed=17259173; DOI=10.1074/jbc.M608722200;
Kim S.Y., Levenson J.M., Korsmeyer S., Sweatt J.D., Schumacher A.;
"Developmental regulation of Eed complex composition governs a switch
in global histone modification in brain.";
J. Biol. Chem. 282:9962-9972(2007).
[19]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=18281287; DOI=10.1074/jbc.M709614200;
Wong C.F., Tellam R.L.;
"MicroRNA-26a targets the histone methyltransferase Enhancer of Zeste
homolog 2 during myogenesis.";
J. Biol. Chem. 283:9836-9843(2008).
[20]
FUNCTION, AND IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
PubMed=19026780; DOI=10.1016/j.molcel.2008.10.016;
Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C.,
Orkin S.H.;
"EZH1 mediates methylation on histone H3 lysine 27 and complements
EZH2 in maintaining stem cell identity and executing pluripotency.";
Mol. Cell 32:491-502(2008).
[21]
TISSUE SPECIFICITY.
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).
[22]
FUNCTION.
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363; SER-366; THR-367
AND THR-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[24]
IDENTIFICATION IN THE PRC2 COMPLEX.
PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K.,
Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.;
"Polycomb-like 2 associates with PRC2 and regulates transcriptional
networks during mouse embryonic stem cell self-renewal and
differentiation.";
Cell Stem Cell 6:153-166(2010).
[25]
INTERACTION WITH DNMT3L.
PubMed=24074865; DOI=10.1016/j.cell.2013.08.056;
Neri F., Krepelova A., Incarnato D., Maldotti M., Parlato C.,
Galvagni F., Matarese F., Stunnenberg H.G., Oliviero S.;
"Dnmt3L antagonizes DNA methylation at bivalent promoters and favors
DNA methylation at gene bodies in ESCs.";
Cell 155:121-134(2013).
[26]
INTERACTION WITH ARNTL/BMAL1.
PubMed=23970558; DOI=10.1126/science.1240636;
Nguyen K.D., Fentress S.J., Qiu Y., Yun K., Cox J.S., Chawla A.;
"Circadian gene Bmal1 regulates diurnal oscillations of Ly6C(hi)
inflammatory monocytes.";
Science 341:1483-1488(2013).
[27]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 39-68 IN COMPLEX WITH EED,
INTERACTION WITH EED, AND MUTAGENESIS OF PHE-42; ASN-45; ILE-49;
LEU-56; PRO-67 AND VAL-68.
PubMed=17937919; DOI=10.1016/j.str.2007.08.007;
Han Z., Xing X., Hu M., Zhang Y., Liu P., Chai J.;
"Structural basis of EZH2 recognition by EED.";
Structure 15:1306-1315(2007).
-!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
PRC2/EED-EZH2 complex, which methylates (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.
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 HOXA7, HOXB6 and HOXC8. 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:0000250|UniProtKB:Q15910,
ECO:0000269|PubMed:12689588, ECO:0000269|PubMed:15516932,
ECO:0000269|PubMed:15520282, ECO:0000269|PubMed:16717091,
ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:19026780}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBUNIT: Component of the PRC2/EED-EZH2 complex, which includes
EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2 (By
similarity). The minimum components required for methyltransferase
activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12 (By
similarity). The PRC2 complex may also interact with DNMT1,
DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via
the SUZ12 subunit (By similarity). Interacts with HDAC1 and HDAC2
(By similarity). Binds ATRX via the SET domain (By similarity).
Interacts with PRAME (By similarity). Interacts with CDYL (By
similarity). Interacts with EED. Interacts with ARNTL/BMAL1.
Interacts with CLOCK and CRY1. Interacts with DNMT3L; the
interaction is direct (PubMed:24074865).
{ECO:0000250|UniProtKB:Q15910, ECO:0000269|PubMed:16717091,
ECO:0000269|PubMed:17259173, ECO:0000269|PubMed:17937919,
ECO:0000269|PubMed:19026780, ECO:0000269|PubMed:20144788,
ECO:0000269|PubMed:23970558, ECO:0000269|PubMed:24074865,
ECO:0000269|PubMed:9742080}.
-!- INTERACTION:
P38398:BRCA1 (xeno); NbExp=5; IntAct=EBI-904311, EBI-349905;
Q9CWR8:Dnmt3l; NbExp=10; IntAct=EBI-904311, EBI-3043871;
Q921E6:Eed; NbExp=9; IntAct=EBI-904311, EBI-904301;
Q62315:Jarid2; NbExp=15; IntAct=EBI-904311, EBI-493592;
Q02395:Mtf2; NbExp=4; IntAct=EBI-904311, EBI-2531578;
Q80U70:Suz12; NbExp=10; IntAct=EBI-904311, EBI-2526494;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to the
inactive X chromosome in trophoblast stem cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=ENX-1A;
IsoId=Q61188-1; Sequence=Displayed;
Name=ENX-1B;
IsoId=Q61188-2; Sequence=VSP_001501;
-!- TISSUE SPECIFICITY: Present in actively dividing cells. Widely
expressed in early embryos. In later embryogenesis, expression
restricted to central and peripheral nervous system, liver and
thymus. In adult, highest expression in spleen, testis and
placenta. Lower levels in intestine and muscle and very low levels
in brain and liver. No expression in heart, thyroid gland, lung
and kidney. {ECO:0000269|PubMed:19026781}.
-!- DEVELOPMENTAL STAGE: Expressed in both adult and embryo with
highest levels in early embryogenesis. Expressed in the fertilized
oocyte. Expression decreases during differentiation of ES cells
and during senescence of MEFs. Expression increases in prostate
during prostate tumor development. {ECO:0000269|PubMed:12689588,
ECO:0000269|PubMed:15684044, ECO:0000269|PubMed:17344414}.
-!- INDUCTION: Repressed by the microRNA (miRNA) miR-26a.
{ECO:0000269|PubMed:18281287}.
-!- PTM: Phosphorylated by AKT1 (By similarity). 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 (By
similarity). {ECO:0000250}.
-!- PTM: Sumoylated. {ECO:0000250}.
-!- 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:0000250}.
-!- DISRUPTION PHENOTYPE: Death early in development. Embryos cease
development following implantation or initiate but fail to
complete gastrulation. {ECO:0000269|PubMed:11390661}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. EZ subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAD54020.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U52951; AAC52655.1; -; mRNA.
EMBL; CH466533; EDL13435.1; -; Genomic_DNA.
EMBL; BC003772; AAH03772.1; -; mRNA.
EMBL; BC016391; AAH16391.1; -; mRNA.
EMBL; AF104359; AAD54020.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS20096.1; -. [Q61188-1]
RefSeq; NP_031997.2; NM_007971.2. [Q61188-1]
UniGene; Mm.246688; -.
PDB; 2QXV; X-ray; 1.82 A; B=39-68.
PDBsum; 2QXV; -.
ProteinModelPortal; Q61188; -.
SMR; Q61188; -.
BioGrid; 199564; 37.
DIP; DIP-29524N; -.
IntAct; Q61188; 26.
MINT; MINT-4124083; -.
STRING; 10090.ENSMUSP00000080419; -.
iPTMnet; Q61188; -.
PhosphoSitePlus; Q61188; -.
EPD; Q61188; -.
PaxDb; Q61188; -.
PeptideAtlas; Q61188; -.
PRIDE; Q61188; -.
Ensembl; ENSMUST00000081721; ENSMUSP00000080419; ENSMUSG00000029687. [Q61188-1]
Ensembl; ENSMUST00000092648; ENSMUSP00000090318; ENSMUSG00000029687. [Q61188-2]
GeneID; 14056; -.
KEGG; mmu:14056; -.
UCSC; uc009btb.2; mouse. [Q61188-1]
CTD; 2146; -.
MGI; MGI:107940; Ezh2.
eggNOG; KOG1079; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOGENOM; HOG000008176; -.
HOVERGEN; HBG002453; -.
InParanoid; Q61188; -.
KO; K11430; -.
OMA; VYNYTPC; -.
OrthoDB; EOG091G09L0; -.
TreeFam; TF314509; -.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
ChiTaRS; Ezh2; mouse.
EvolutionaryTrace; Q61188; -.
PRO; PR:Q61188; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029687; -.
CleanEx; MM_EZH2; -.
ExpressionAtlas; Q61188; baseline and differential.
Genevisible; Q61188; MM.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0045120; C:pronucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0001047; F:core promoter binding; IDA:MGI.
GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); ISO:MGI.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:MGI.
GO; GO:0070878; F:primary miRNA binding; IDA:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:MGI.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI.
GO; GO:0035984; P:cellular response to trichostatin A; IMP:MGI.
GO; GO:0021695; P:cerebellar cortex development; IMP:MGI.
GO; GO:0006306; P:DNA methylation; IMP:MGI.
GO; GO:0070314; P:G1 to G0 transition; IMP:MGI.
GO; GO:0036333; P:hepatocyte homeostasis; IGI:MGI.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0070734; P:histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0098532; P:histone H3-K27 trimethylation; IGI:MGI.
GO; GO:0016571; P:histone methylation; IDA:MGI.
GO; GO:0097421; P:liver regeneration; IGI:MGI.
GO; GO:0045605; P:negative regulation of epidermal cell differentiation; IMP:MGI.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IGI:MGI.
GO; GO:0051154; P:negative regulation of striated muscle cell differentiation; IDA:MGI.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0071168; P:protein localization to chromatin; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0014013; P:regulation of gliogenesis; IMP:MGI.
GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:1904772; P:response to tetrachloromethane; IGI:MGI.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IMP:MGI.
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; Chromosome; Complete proteome; Glycoprotein;
Isopeptide bond; Methyltransferase; Nucleus; Phosphoprotein;
Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 746 Histone-lysine N-methyltransferase EZH2.
/FTId=PRO_0000213993.
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. {ECO:0000250}.
REGION 39 68 Interaction with EED.
REGION 329 522 Interaction with CDYL. {ECO:0000250}.
COMPBIAS 523 605 Cys-rich.
MOD_RES 21 21 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 339 339 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 345 345 Phosphothreonine; by CDK1 and CDK2.
{ECO:0000250|UniProtKB:Q15910}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 367 367 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 487 487 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 75 75 O-linked (GlcNAc) serine. {ECO:0000250}.
CROSSLNK 634 634 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15910}.
VAR_SEQ 511 553 DGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSS
EC -> G (in isoform ENX-1B).
{ECO:0000305}.
/FTId=VSP_001501.
MUTAGEN 42 42 F->D: Abrogates interaction with EED.
{ECO:0000269|PubMed:17937919}.
MUTAGEN 45 45 N->A: Abrogates interaction with EED.
{ECO:0000269|PubMed:17937919}.
MUTAGEN 49 49 I->E: Abrogates interaction with EED.
{ECO:0000269|PubMed:17937919}.
MUTAGEN 56 56 L->E: Abrogates interaction with EED.
{ECO:0000269|PubMed:17937919}.
MUTAGEN 67 67 P->D: Abrogates interaction with EED.
{ECO:0000269|PubMed:17937919}.
MUTAGEN 68 68 V->E: Abrogates interaction with EED.
{ECO:0000269|PubMed:17937919}.
CONFLICT 159 161 Missing (in Ref. 4; AAD54020).
{ECO:0000305}.
CONFLICT 651 651 A -> D (in Ref. 1; AAC52655).
{ECO:0000305}.
HELIX 41 62 {ECO:0000244|PDB:2QXV}.
SEQUENCE 746 AA; 85292 MW; 7442C751E13EA24B CRC64;
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKT MFSSNRQKIL ERTETLNQEW
KQRRIQPVHI MTSVSSLRGT RECSVTSDLD FPAQVIPLKT LNAVASVPIM YSWSPLQQNF
MVEDETVLHN IPYMGDEVLD QDGTFIEELI KNYDGKVHGD RECGFINDEI FVELVNALGQ
YNDDDDDDDG DDPDEREEKQ KDLEDNRDDK ETCPPRKFPA DKIFEAISSM FPDKGTAEEL
KEKYKELTEQ QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH
ATPNTYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP GGRRRGRLPN
NSSRPSTPTI SVLESKDTDS DREAGTETGG ENNDKEEEEK KDETSSSSEA NSRCQTPIKM
KPNIEPPENV EWSGAEASMF RVLIGTYYDN FCAIARLIGT KTCRQVYEFR VKESSIIAPV
PTEDVDTPPR 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


Related products :

Catalog number Product name Quantity
EIAAB13541 Enhancer of zeste homolog 2,ENX-1,EZH2,Histone-lysine N-methyltransferase EZH2,Homo sapiens,Human,KMT6,Lysine N-methyltransferase 6
EIAAB13540 Enhancer of zeste homolog 2,ENX-1,Enx1h,Ezh2,Histone-lysine N-methyltransferase EZH2,Mouse,Mus musculus
EIAAB13537 Bos taurus,Bovine,Enhancer of zeste homolog 1,EZH1,Histone-lysine N-methyltransferase EZH1
EIAAB13538 Enhancer of zeste homolog 1,Enx2,ENX-2,Ezh1,Histone-lysine N-methyltransferase EZH1,Mouse,Mus musculus
EIAAB13539 Enhancer of zeste homolog 1,ENX-2,EZH1,Histone-lysine N-methyltransferase EZH1,Homo sapiens,Human,KIAA0388
DL-EZH2-Hu Human Enhancer Of Zeste Homolog 2 (EZH2) ELISA Kit 96T
EIAAB40615 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Homo sapiens,Human,KMT1A,Lysine N-methyltransferase 1A,Position-effect variegation 3-9 homolog,Su(var)3-9 ho
EIAAB40618 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Homo sapiens,Human,KMT1B,Lysine N-methyltransferase 1B,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 ho
F10 EZH2 Gene enhancer of zeste homolog 2 (Drosophila)
E99073Hu ELISA Kit for Enhancer Of Zeste Homolog 2 (EZH2) 96T/Kit
CSB-EL007913HU Human Histone-lysine N-methyltransferase EZH2(EZH2) ELISA kit SpeciesHuman 96T
CSB-EL007913MO Mouse Histone-lysine N-methyltransferase EZH2(EZH2) ELISA kit SpeciesMouse 96T
CSB-EL007913MO Mouse Histone-lysine N-methyltransferase EZH2(EZH2) ELISA kit 96T
CSB-EL007913HU Human Histone-lysine N-methyltransferase EZH2(EZH2) ELISA kit 96T
EZH2_MOUSE ELISA Kit FOR Histone-lysine N-methyltransferase EZH2; organism: Mouse; gene name: Ezh2 96T
YHB1090Hu Human Enhancer Of Zeste Homolog 2 (EZH2)ELISA Kit 96T
UB-E04466 Human Enhancer Of Zeste Homolog 2(EZH2)ELISA Kit 96T
QY-E04466 Human Enhancer Of Zeste Homolog 2(EZH2)ELISA Kit 96T
201-12-2672 Human Enhancer Of Zeste Homolog 2 (EZH2)ELISA Kit 48T
201-12-2672 Human Enhancer Of Zeste Homolog 2(EZH2)ELISA Kit 96T
201-12-2672 Human Enhancer Of Zeste Homolog 2 (EZH2)ELISA Kit 96T
UT-E04466 Human Enhancer Of Zeste Homolog 2 (EZH2) ELISA Kit 96T
E2671Hu Human Enhancer Of Zeste Homolog 2 (EZH2)ELISA Kit 96T
YHB1090Hu Human Enhancer Of Zeste Homolog 2 (EZH2)ELISA Kit 48T
E2671Hu Human Enhancer Of Zeste Homolog 2 (EZH2)ELISA Kit 48T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur