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Q61188

- EZH2_MOUSE

UniProt

Q61188 - EZH2_MOUSE

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
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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.5 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. core promoter binding Source: MGI
    3. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
    4. histone methyltransferase activity Source: MGI
    5. protein binding Source: IntAct
    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: MGI
    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 gene expression Source: MGI
    22. regulation of gliogenesis Source: MGI
    23. regulation of neurogenesis Source: MGI
    24. regulation of protein phosphorylation Source: MGI
    25. regulation of transcription from RNA polymerase II promoter Source: MGI
    26. skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration Source: MGI
    27. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    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. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: Ensembl
    3. ESC/E(Z) complex Source: UniProtKB
    4. nucleus Source: MGI
    5. pronucleus Source: MGI

    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

    ArrayExpressiQ61188.
    BgeeiQ61188.
    CleanExiMM_EZH2.
    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.By similarity6 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. 31 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.
    GeneTreeiENSGT00740000115009.
    HOGENOMiHOG000008176.
    HOVERGENiHBG002453.
    InParanoidiQ99L74.
    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

    MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKT MFSSNRQKIL    50
    ERTETLNQEW KQRRIQPVHI MTSVSSLRGT RECSVTSDLD FPAQVIPLKT 100
    LNAVASVPIM YSWSPLQQNF MVEDETVLHN IPYMGDEVLD QDGTFIEELI 150
    KNYDGKVHGD RECGFINDEI FVELVNALGQ YNDDDDDDDG DDPDEREEKQ 200
    KDLEDNRDDK ETCPPRKFPA DKIFEAISSM FPDKGTAEEL KEKYKELTEQ 250
    QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH 300
    ATPNTYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP 350
    GGRRRGRLPN NSSRPSTPTI SVLESKDTDS DREAGTETGG ENNDKEEEEK 400
    KDETSSSSEA NSRCQTPIKM KPNIEPPENV EWSGAEASMF RVLIGTYYDN 450
    FCAIARLIGT KTCRQVYEFR VKESSIIAPV PTEDVDTPPR KKKRKHRLWA 500
    AHCRKIQLKK DGSSNHVYNY QPCDHPRQPC DSSCPCVIAQ NFCEKFCQCS 550
    SECQNRFPGC RCKAQCNTKQ CPCYLAVREC DPDLCLTCGA ADHWDSKNVS 600
    CKNCSIQRGS KKHLLLAPSD VAGWGIFIKD PVQKNEFISE YCGEIISQDE 650
    ADRRGKVYDK YMCSFLFNLN NDFVVDATRK GNKIRFANHS VNPNCYAKVM 700
    MVNGDHRIGI FAKRAIQTGE ELFFDYRYSQ ADALKYVGIE REMEIP 746
    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. 31 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 ENSGT00740000115009.
    HOGENOMi HOG000008176.
    HOVERGENi HBG002453.
    InParanoidi Q99L74.
    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

    ArrayExpressi Q61188.
    Bgeei Q61188.
    CleanExi MM_EZH2.
    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

    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 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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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.
    22. "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.
    23. "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.
    24. "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 1, 2014
    This is version 132 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