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Q61188

- EZH2_MOUSE

UniProt

Q61188 - EZH2_MOUSE

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Protein

Histone-lysine N-methyltransferase EZH2

Gene

Ezh2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. 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 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.6 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. chromatin DNA binding Source: Ensembl
  3. core promoter binding Source: UniProtKB
  4. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  5. histone methyltransferase activity Source: MGI
  6. RNA binding Source: MGI
  7. sequence-specific DNA binding Source: MGI

GO - Biological processi

  1. cellular response to hydrogen peroxide Source: MGI
  2. cerebellar cortex development Source: MGI
  3. DNA methylation Source: MGI
  4. G1 to G0 transition Source: MGI
  5. histone H3-K27 methylation Source: UniProtKB
  6. histone methylation Source: MGI
  7. negative regulation of epidermal cell differentiation Source: MGI
  8. negative regulation of G1/S transition of mitotic cell cycle Source: MGI
  9. negative regulation of gene expression, epigenetic Source: UniProtKB
  10. negative regulation of retinoic acid receptor signaling pathway Source: UniProtKB
  11. negative regulation of striated muscle cell differentiation Source: MGI
  12. negative regulation of transcription, DNA-templated Source: UniProtKB
  13. negative regulation of transcription elongation from RNA polymerase II promoter Source: MGI
  14. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  15. positive regulation of epithelial to mesenchymal transition Source: UniProtKB
  16. positive regulation of MAP kinase activity Source: UniProtKB
  17. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  18. positive regulation of Ras GTPase activity Source: UniProtKB
  19. protein localization to chromatin Source: MGI
  20. regulation of cell proliferation Source: MGI
  21. regulation of circadian rhythm Source: UniProtKB
  22. regulation of gene expression Source: MGI
  23. regulation of gliogenesis Source: MGI
  24. regulation of neurogenesis Source: MGI
  25. regulation of protein phosphorylation Source: MGI
  26. regulation of transcription from RNA polymerase II promoter Source: MGI
  27. skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration Source: MGI
  28. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
REACT_222475. PRC2 methylates histones and DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase EZH2 (EC:2.1.1.43)
Alternative name(s):
ENX-1
Enhancer of zeste homolog 2
Gene namesi
Name:Ezh2
Synonyms:Enx1h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:107940. Ezh2.

Subcellular locationi

Nucleus. Chromosome
Note: Localizes to the inactive X chromosome in trophoblast stem cells.

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. ESC/E(Z) complex Source: UniProtKB
  3. nuclear chromatin Source: Ensembl
  4. nucleus Source: MGI
  5. pronucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Death early in development. Embryos cease development following implantation or initiate but fail to complete gastrulation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421F → D: Abrogates interaction with EED. 1 Publication
Mutagenesisi45 – 451N → A: Abrogates interaction with EED. 1 Publication
Mutagenesisi49 – 491I → E: Abrogates interaction with EED. 1 Publication
Mutagenesisi56 – 561L → E: Abrogates interaction with EED. 1 Publication
Mutagenesisi67 – 671P → D: Abrogates interaction with EED. 1 Publication
Mutagenesisi68 – 681V → E: Abrogates interaction with EED. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 746746Histone-lysine N-methyltransferase EZH2PRO_0000213993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine; by PKB/AKT1By similarity
Glycosylationi75 – 751O-linked (GlcNAc)By similarity
Modified residuei345 – 3451Phosphothreonine; by CDK1 and CDK2By similarity
Modified residuei366 – 3661PhosphoserineBy similarity
Modified residuei367 – 3671PhosphothreonineBy similarity
Modified residuei487 – 4871PhosphothreonineBy similarity

Post-translational modificationi

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).By similarity
Sumoylated.By similarity
Glycosylated: O-GlcNAcylation at Ser-75 by OGT increases stability of EZH2 and facilitates the formation of H3K27me3 by the PRC2/EED-EZH2 complex.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ61188.
PaxDbiQ61188.
PRIDEiQ61188.

PTM databases

PhosphoSiteiQ61188.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.3 Publications

Inductioni

Repressed by the microRNA (miRNA) miR-26a.1 Publication

Gene expression databases

BgeeiQ61188.
CleanExiMM_EZH2.
ExpressionAtlasiQ61188. baseline and differential.
GenevestigatoriQ61188.

Interactioni

Subunit structurei

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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P383985EBI-904311,EBI-349905From a different organism.
Dnmt3lQ9CWR810EBI-904311,EBI-3043871
EedQ921E69EBI-904311,EBI-904301
Jarid2Q6231515EBI-904311,EBI-493592
Mtf2Q023954EBI-904311,EBI-2531578
Suz12Q80U7010EBI-904311,EBI-2526494

Protein-protein interaction databases

BioGridi199564. 33 interactions.
DIPiDIP-29524N.
IntActiQ61188. 25 interactions.
MINTiMINT-4124083.

Structurei

Secondary structure

1
746
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 6222

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QXVX-ray1.82B39-68[»]
ProteinModelPortaliQ61188.
SMRiQ61188. Positions 40-68, 520-729.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61188.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 605103CXCPROSITE-ProRule annotationAdd
BLAST
Domaini612 – 727116SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 340340Interaction with DNMT1, DNMT3A and DNMT3BBy similarityAdd
BLAST
Regioni39 – 6830Interaction with EEDAdd
BLAST
Regioni329 – 522194Interaction with CDYLBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi523 – 60583Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.PROSITE-ProRule annotation
Contains 1 CXC domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000118855.
HOGENOMiHOG000008176.
HOVERGENiHBG002453.
InParanoidiQ61188.
KOiK11430.
OMAiNRDDKES.
OrthoDBiEOG7VB2DR.
TreeFamiTF314509.

Family and domain databases

InterProiIPR026489. CXC_dom.
IPR021654. EZH2_WD-Binding.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view]
PfamiPF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform ENX-1A (identifier: Q61188-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKT MFSSNRQKIL
60 70 80 90 100
ERTETLNQEW KQRRIQPVHI MTSVSSLRGT RECSVTSDLD FPAQVIPLKT
110 120 130 140 150
LNAVASVPIM YSWSPLQQNF MVEDETVLHN IPYMGDEVLD QDGTFIEELI
160 170 180 190 200
KNYDGKVHGD RECGFINDEI FVELVNALGQ YNDDDDDDDG DDPDEREEKQ
210 220 230 240 250
KDLEDNRDDK ETCPPRKFPA DKIFEAISSM FPDKGTAEEL KEKYKELTEQ
260 270 280 290 300
QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH
310 320 330 340 350
ATPNTYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP
360 370 380 390 400
GGRRRGRLPN NSSRPSTPTI SVLESKDTDS DREAGTETGG ENNDKEEEEK
410 420 430 440 450
KDETSSSSEA NSRCQTPIKM KPNIEPPENV EWSGAEASMF RVLIGTYYDN
460 470 480 490 500
FCAIARLIGT KTCRQVYEFR VKESSIIAPV PTEDVDTPPR KKKRKHRLWA
510 520 530 540 550
AHCRKIQLKK DGSSNHVYNY QPCDHPRQPC DSSCPCVIAQ NFCEKFCQCS
560 570 580 590 600
SECQNRFPGC RCKAQCNTKQ CPCYLAVREC DPDLCLTCGA ADHWDSKNVS
610 620 630 640 650
CKNCSIQRGS KKHLLLAPSD VAGWGIFIKD PVQKNEFISE YCGEIISQDE
660 670 680 690 700
ADRRGKVYDK YMCSFLFNLN NDFVVDATRK GNKIRFANHS VNPNCYAKVM
710 720 730 740
MVNGDHRIGI FAKRAIQTGE ELFFDYRYSQ ADALKYVGIE REMEIP
Length:746
Mass (Da):85,292
Last modified:July 27, 2011 - v2
Checksum:i7442C751E13EA24B
GO
Isoform ENX-1B (identifier: Q61188-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     511-553: DGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSEC → G

Show »
Length:704
Mass (Da):80,536
Checksum:iFDB869B96F929D75
GO

Sequence cautioni

The sequence AAD54020.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1613Missing in AAD54020. (PubMed:10051331)Curated
Sequence conflicti651 – 6511A → D in AAC52655. (PubMed:8861097)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei511 – 55343DGSSN…CSSEC → G in isoform ENX-1B. CuratedVSP_001501Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52951 mRNA. Translation: AAC52655.1.
CH466533 Genomic DNA. Translation: EDL13435.1.
BC003772 mRNA. Translation: AAH03772.1.
BC016391 mRNA. Translation: AAH16391.1.
AF104359 Genomic DNA. Translation: AAD54020.1. Sequence problems.
CCDSiCCDS20096.1. [Q61188-1]
RefSeqiNP_031997.2. NM_007971.2. [Q61188-1]
UniGeneiMm.246688.

Genome annotation databases

EnsembliENSMUST00000081721; ENSMUSP00000080419; ENSMUSG00000029687. [Q61188-1]
ENSMUST00000092648; ENSMUSP00000090318; ENSMUSG00000029687. [Q61188-2]
GeneIDi14056.
KEGGimmu:14056.
UCSCiuc009btb.2. mouse. [Q61188-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52951 mRNA. Translation: AAC52655.1 .
CH466533 Genomic DNA. Translation: EDL13435.1 .
BC003772 mRNA. Translation: AAH03772.1 .
BC016391 mRNA. Translation: AAH16391.1 .
AF104359 Genomic DNA. Translation: AAD54020.1 . Sequence problems.
CCDSi CCDS20096.1. [Q61188-1 ]
RefSeqi NP_031997.2. NM_007971.2. [Q61188-1 ]
UniGenei Mm.246688.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QXV X-ray 1.82 B 39-68 [» ]
ProteinModelPortali Q61188.
SMRi Q61188. Positions 40-68, 520-729.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199564. 33 interactions.
DIPi DIP-29524N.
IntActi Q61188. 25 interactions.
MINTi MINT-4124083.

PTM databases

PhosphoSitei Q61188.

Proteomic databases

MaxQBi Q61188.
PaxDbi Q61188.
PRIDEi Q61188.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081721 ; ENSMUSP00000080419 ; ENSMUSG00000029687 . [Q61188-1 ]
ENSMUST00000092648 ; ENSMUSP00000090318 ; ENSMUSG00000029687 . [Q61188-2 ]
GeneIDi 14056.
KEGGi mmu:14056.
UCSCi uc009btb.2. mouse. [Q61188-1 ]

Organism-specific databases

CTDi 2146.
MGIi MGI:107940. Ezh2.

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000118855.
HOGENOMi HOG000008176.
HOVERGENi HBG002453.
InParanoidi Q61188.
KOi K11430.
OMAi NRDDKES.
OrthoDBi EOG7VB2DR.
TreeFami TF314509.

Enzyme and pathway databases

Reactomei REACT_188970. Oxidative Stress Induced Senescence.
REACT_222475. PRC2 methylates histones and DNA.

Miscellaneous databases

ChiTaRSi EZH2. mouse.
EvolutionaryTracei Q61188.
NextBioi 285012.
PROi Q61188.
SOURCEi Search...

Gene expression databases

Bgeei Q61188.
CleanExi MM_EZH2.
ExpressionAtlasi Q61188. baseline and differential.
Genevestigatori Q61188.

Family and domain databases

InterProi IPR026489. CXC_dom.
IPR021654. EZH2_WD-Binding.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view ]
PROSITEi PS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and developmental expression analysis of Enx-1, a novel mouse Polycomb group gene."
    Hobert O., Sures I., Ciossek T., Fuchs M., Ullrich A.
    Mech. Dev. 55:171-184(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. "The murine polycomb-group genes ezh1 and ezh2 map close to hox gene clusters on mouse chromosomes 11 and 6."
    Laible G., Haynes A.R., Lebersorger A., O'Carroll D., Mattei M.-G., Denny P., Brown S.D.M., Jenuwein T.
    Mamm. Genome 10:311-314(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-497.
    Strain: 129/Sv.
  5. "Point mutations in the WD40 domain of Eed block its interaction with Ezh2."
    Denisenko O.N., Shnyreva M., Suzuki H., Bomsztyk K.
    Mol. Cell. Biol. 18:5634-5642(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EED.
  6. "The polycomb-group gene Ezh2 is required for early mouse development."
    O'Carroll D., Erhardt S., Pagani M., Barton S.C., Surani M.A., Jenuwein T.
    Mol. Cell. Biol. 21:4330-4336(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "Mitotically stable association of polycomb group proteins Eed and Enx1 with the inactive X chromosome in trophoblast stem cells."
    Mak W., Baxter J., Silva J., Newall A.E., Otte A.P., Brockdorff N.
    Curr. Biol. 12:1016-1020(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Establishment of histone H3 methylation on the inactive X chromosome requires transient recruitment of Eed-Enx1 polycomb group complexes."
    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.
    Dev. Cell 4:481-495(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  9. Cited for: SUBCELLULAR LOCATION.
  10. "The Polycomb Ezh2 methyltransferase regulates muscle gene expression and skeletal muscle differentiation."
    Caretti G., Di Padova M., Micales B., Lyons G.E., Sartorelli V.
    Genes Dev. 18:2627-2638(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Erratum
    Caretti G., Di Padova M., Micales B., Lyons G.E., Sartorelli V.
    Genes Dev. 19:768-768(2005)
  12. "Imprinting along the Kcnq1 domain on mouse chromosome 7 involves repressive histone methylation and recruitment of Polycomb group complexes."
    Umlauf D., Goto Y., Cao R., Cerqueira F., Wagschal A., Zhang Y., Feil R.
    Nat. Genet. 36:1296-1300(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Reactivation of the paternal X chromosome in early mouse embryos."
    Mak W., Nesterova T.B., de Napoles M., Appanah R., Yamanaka S., Otte A.P., Brockdorff N.
    Science 303:666-669(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  15. "The polycomb group protein EZH2 is required for mammalian circadian clock function."
    Etchegaray J.P., Yang X., DeBruyne J.P., Peters A.H., Weaver D.R., Jenuwein T., Reppert S.M.
    J. Biol. Chem. 281:21209-21215(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLOCK; ARNTL AND CRY1.
  16. "The Polycomb group protein Eed protects the inactive X-chromosome from differentiation-induced reactivation."
    Kalantry S., Mills K.C., Yee D., Otte A.P., Panning B., Magnuson T.
    Nat. Cell Biol. 8:195-202(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells."
    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.
    Genes Dev. 21:525-530(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  18. "Developmental regulation of Eed complex composition governs a switch in global histone modification in brain."
    Kim S.Y., Levenson J.M., Korsmeyer S., Sweatt J.D., Schumacher A.
    J. Biol. Chem. 282:9962-9972(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EED.
  19. "MicroRNA-26a targets the histone methyltransferase Enhancer of Zeste homolog 2 during myogenesis."
    Wong C.F., Tellam R.L.
    J. Biol. Chem. 283:9836-9843(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION.
  20. "EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency."
    Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C., Orkin S.H.
    Mol. Cell 32:491-502(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
  21. "Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms."
    Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L., Dynlacht B.D., Reinberg D.
    Mol. Cell 32:503-518(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  22. "Role of hPHF1 in H3K27 methylation and Hox gene silencing."
    Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.
    Mol. Cell. Biol. 28:1862-1872(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Polycomb-like 2 associates with PRC2 and regulates transcriptional networks during mouse embryonic stem cell self-renewal and differentiation."
    Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.
    Cell Stem Cell 6:153-166(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PRC2 COMPLEX.
  24. "Circadian gene Bmal1 regulates diurnal oscillations of Ly6C(hi) inflammatory monocytes."
    Nguyen K.D., Fentress S.J., Qiu Y., Yun K., Cox J.S., Chawla A.
    Science 341:1483-1488(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARNTL/BMAL1.
  25. "Structural basis of EZH2 recognition by EED."
    Han Z., Xing X., Hu M., Zhang Y., Liu P., Chai J.
    Structure 15:1306-1315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 39-68 IN COMPLEX WITH EED, INTERACTION WITH EED, MUTAGENESIS OF PHE-42; ASN-45; ILE-49; LEU-56; PRO-67 AND VAL-68.

Entry informationi

Entry nameiEZH2_MOUSE
AccessioniPrimary (citable) accession number: Q61188
Secondary accession number(s): Q99L74, Q9R090
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3