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Q61188 (EZH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase EZH2

EC=2.1.1.43
Alternative name(s):
ENX-1
Enhancer of zeste homolog 2
Gene names
Name:Ezh2
Synonyms:Enx1h
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length746 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.8 Ref.10 Ref.12 Ref.19 Ref.21

Catalytic activity

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

Subunit structure

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. Ref.5 Ref.17 Ref.19 Ref.22 Ref.23 Ref.24

Subcellular location

Nucleus. Chromosome. Note: Localizes to the inactive X chromosome in trophoblast stem cells. Ref.7 Ref.8 Ref.9 Ref.13 Ref.15 Ref.18

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. Ref.20

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. Ref.8 Ref.14 Ref.16

Induction

Repressed by the microRNA (miRNA) miR-26a. Ref.18

Post-translational modification

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.

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.

Disruption phenotype

Death early in development. Embryos cease development following implantation or initiate but fail to complete gastrulation. Ref.6

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.

Contains 1 CXC domain.

Contains 1 SET domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1 to G0 transition

Inferred from mutant phenotype PubMed 19303854. Source: MGI

cellular response to hydrogen peroxide

Inferred from direct assay PubMed 20808772. Source: MGI

cerebellar cortex development

Inferred from mutant phenotype PubMed 20798045. Source: MGI

histone H3-K27 methylation

Inferred from mutant phenotype PubMed 18311137PubMed 20798045. Source: MGI

histone methylation

Inferred from direct assay PubMed 12900441. Source: MGI

negative regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 19303854. Source: MGI

negative regulation of epidermal cell differentiation

Inferred from mutant phenotype PubMed 19303854. Source: MGI

negative regulation of gene expression, epigenetic

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of retinoic acid receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of striated muscle cell differentiation

Inferred from direct assay Ref.10. Source: MGI

negative regulation of transcription elongation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19303854. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Ras GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to chromatin

Inferred from mutant phenotype PubMed 18311137. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 19303854. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 20798045. Source: MGI

regulation of gliogenesis

Inferred from mutant phenotype PubMed 20798045. Source: MGI

regulation of neurogenesis

Inferred from mutant phenotype PubMed 20798045. Source: MGI

regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 19303854. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from direct assay PubMed 20064375PubMed 20064376Ref.22PubMed 22438827PubMed 23160351. Source: UniProtKB

chromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.10PubMed 19303854PubMed 22482507PubMed 22949634PubMed 9584197. Source: MGI

pronucleus

Inferred from direct assay PubMed 12900441. Source: MGI

   Molecular_functionRNA binding

Inferred from direct assay PubMed 21936910. Source: MGI

chromatin binding

Inferred from direct assay Ref.10PubMed 22056776. Source: MGI

core promoter binding

Inferred from direct assay PubMed 20798045. Source: MGI

histone methyltransferase activity

Inferred from direct assay PubMed 12900441. Source: MGI

histone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

sequence-specific DNA binding

Inferred from direct assay PubMed 20956546. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform ENX-1A (identifier: Q61188-1)

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.
Isoform ENX-1B (identifier: Q61188-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 746746Histone-lysine N-methyltransferase EZH2
PRO_0000213993

Regions

Domain503 – 605103CXC
Domain612 – 727116SET
Region1 – 340340Interaction with DNMT1, DNMT3A and DNMT3B By similarity
Region39 – 6830Interaction with EED
Region329 – 522194Interaction with CDYL By similarity
Compositional bias523 – 60583Cys-rich

Amino acid modifications

Modified residue211Phosphoserine; by PKB/AKT1 By similarity
Modified residue3451Phosphothreonine; by CDK1 and CDK2 By similarity
Modified residue3661Phosphoserine By similarity
Modified residue3671Phosphothreonine By similarity
Modified residue4871Phosphothreonine By similarity
Glycosylation751O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence511 – 55343DGSSN…CSSEC → G in isoform ENX-1B.
VSP_001501

Experimental info

Mutagenesis421F → D: Abrogates interaction with EED. Ref.24
Mutagenesis451N → A: Abrogates interaction with EED. Ref.24
Mutagenesis491I → E: Abrogates interaction with EED. Ref.24
Mutagenesis561L → E: Abrogates interaction with EED. Ref.24
Mutagenesis671P → D: Abrogates interaction with EED. Ref.24
Mutagenesis681V → E: Abrogates interaction with EED. Ref.24
Sequence conflict159 – 1613Missing in AAD54020. Ref.4
Sequence conflict6511A → D in AAC52655. Ref.1

Secondary structure

... 746
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform ENX-1A [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7442C751E13EA24B

FASTA74685,292
        10         20         30         40         50         60 
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKT MFSSNRQKIL ERTETLNQEW 

        70         80         90        100        110        120 
KQRRIQPVHI MTSVSSLRGT RECSVTSDLD FPAQVIPLKT LNAVASVPIM YSWSPLQQNF 

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

       190        200        210        220        230        240 
YNDDDDDDDG DDPDEREEKQ KDLEDNRDDK ETCPPRKFPA 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 SVLESKDTDS DREAGTETGG ENNDKEEEEK KDETSSSSEA NSRCQTPIKM 

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

       490        500        510        520        530        540 
PTEDVDTPPR 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 

« Hide

Isoform ENX-1B [UniParc].

Checksum: FDB869B96F929D75
Show »

FASTA70480,536

References

« Hide 'large scale' references
[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]"Role of histone H3 lysine 27 methylation in X inactivation."
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.
Science 300:131-135(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_031997.2. NM_007971.2.
UniGeneMm.246688.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QXVX-ray1.82B39-68[»]
ProteinModelPortalQ61188.
SMRQ61188. Positions 40-68, 520-729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199564. 29 interactions.
DIPDIP-29524N.
IntActQ61188. 25 interactions.
MINTMINT-4124083.

PTM databases

PhosphoSiteQ61188.

Proteomic databases

PaxDbQ61188.
PRIDEQ61188.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081721; ENSMUSP00000080419; ENSMUSG00000029687. [Q61188-1]
ENSMUST00000092648; ENSMUSP00000090318; ENSMUSG00000029687. [Q61188-2]
GeneID14056.
KEGGmmu:14056.
UCSCuc009btb.2. mouse. [Q61188-1]

Organism-specific databases

CTD2146.
MGIMGI:107940. Ezh2.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00740000115009.
HOGENOMHOG000008176.
HOVERGENHBG002453.
InParanoidQ99L74.
KOK11430.
OMANRDDKES.
OrthoDBEOG7VB2DR.
TreeFamTF314509.

Gene expression databases

ArrayExpressQ61188.
BgeeQ61188.
CleanExMM_EZH2.
GenevestigatorQ61188.

Family and domain databases

InterProIPR026489. CXC_dom.
IPR021654. EZH2_WD-Binding.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view]
PfamPF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEZH2. mouse.
EvolutionaryTraceQ61188.
NextBio285012.
PROQ61188.
SOURCESearch...

Entry information

Entry nameEZH2_MOUSE
AccessionPrimary (citable) accession number: Q61188
Secondary accession number(s): Q99L74, Q9R090
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot