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Q15910 (EZH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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
Lysine N-methyltransferase 6
Gene names
Name:EZH2
Synonyms:KMT6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 'Lys-9' (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 HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.25 Ref.28 Ref.30 Ref.31 Ref.32 Ref.36 Ref.38 Ref.43 Ref.47 Ref.48

Catalytic activity

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

Subunit structure

Binds ATRX via the SET domain Probable. Component of the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2. The minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12. The PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12 subunit. Interacts with HDAC1 and HDAC2. Interacts with PRAME. Interacts with CDYL. Interacts with ARNTL/BMAL1. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.21 Ref.23 Ref.28 Ref.36 Ref.37 Ref.38 Ref.45

Subcellular location

Nucleus Ref.9 Ref.13 Ref.15 Ref.17.

Tissue specificity

Expressed in many tissues. Overexpressed in numerous tumor types including carcinomas of the breast, colon, larynx, lymphoma and testis. Ref.15

Developmental stage

Expression decreases during senescence of embryonic fibroblasts (HEFs). Expression peaks at the G1/S phase boundary. Ref.15 Ref.20 Ref.32

Induction

Expression is induced by E2F1, E2F2 and E2F3. Expression is reduced in cells subject to numerous types of stress including UV-, IR- and bleomycin-induced DNA damage and by activation of p53/TP53. Ref.15 Ref.20 Ref.32

Post-translational modification

Phosphorylated by AKT1. 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. Ref.23 Ref.43

Sumoylated. Ref.39

Glycosylated: O-GlcNAcylation at Ser-75 by OGT increases stability of EZH2 and facilitates the formation of H3K27me3 by the PRC2/EED-EZH2 complex. Ref.48

Involvement in disease

Weaver syndrome (WVS) [MIM:277590]: A syndrome of accelerated growth and osseous maturation, unusual craniofacial appearance, hoarse and low-pitched cry, and hypertonia with camptodactyly. Distinguishing features of Weaver syndrome include broad forehead and face, ocular hypertelorism, prominent wide philtrum, micrognathia, deep horizontal chin groove, and deep-set nails. In addition, carpal bone development is advanced over the rest of the hand.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.51

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.

Caution

Two variants of the PRC2 complex have been described, termed PRC3 and PRC4. Each of the three complexes may include a different complement of EED isoforms, although the precise sequences of the isoforms in each complex have not been determined. The PRC2 and PRC4 complexes may also methylate 'Lys-26' of histone H1 in addition to 'Lys-27' of histone H3 (Ref.18 and Ref.22), although other studies have demonstrated no methylation of 'Lys-26' of histone H1 by PRC2 (Ref.26).

Sequence caution

The sequence AAS07448.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   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 electronic annotation. Source: Ensembl

cerebellar cortex development

Inferred from electronic annotation. Source: Ensembl

chromatin organization

Traceable author statement PubMed 8921387. Source: ProtInc

histone H3-K27 methylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of epidermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression, epigenetic

Inferred from direct assay PubMed 20154697. Source: UniProtKB

negative regulation of retinoic acid receptor signaling pathway

Inferred from mutant phenotype Ref.21. Source: UniProtKB

negative regulation of striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription elongation from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20154697. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 20154697. Source: UniProtKB

positive regulation of Ras GTPase activity

Inferred from direct assay PubMed 20154697. Source: UniProtKB

positive regulation of epithelial to mesenchymal transition

Inferred from direct assay PubMed 20154697. Source: UniProtKB

positive regulation of protein serine/threonine kinase activity

Inferred from direct assay PubMed 20154697. Source: UniProtKB

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of gliogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Traceable author statement PubMed 8921387. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from direct assay PubMed 20075857PubMed 23104054PubMed 23273982Ref.48. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

pronucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

RNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay PubMed 20154697. Source: UniProtKB

core promoter binding

Inferred from electronic annotation. Source: Ensembl

histone methyltransferase activity

Inferred from direct assay Ref.16. Source: MGI

histone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15910-1)

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 2 (identifier: Q15910-2)

The sequence of this isoform differs from the canonical sequence as follows:
     297-298: HP → HRKCNYS
Isoform 3 (identifier: Q15910-3)

The sequence of this isoform differs from the canonical sequence as follows:
     83-121: Missing.
Isoform 4 (identifier: Q15910-4)

The sequence of this isoform differs from the canonical sequence as follows:
     74-82: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q15910-5)

The sequence of this isoform differs from the canonical sequence as follows:
     74-82: Missing.
     511-553: DGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSEC → G
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 746746Histone-lysine N-methyltransferase EZH2
PRO_0000213992

Regions

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

Amino acid modifications

Modified residue211Phosphoserine; by PKB/AKT1
Modified residue3451Phosphothreonine; by CDK1 and CDK2 Ref.43
Modified residue3661Phosphoserine Ref.40
Modified residue3671Phosphothreonine Ref.40
Modified residue4871Phosphothreonine Ref.24 Ref.27 Ref.34 Ref.35 Ref.40 Ref.42 Ref.44 Ref.46
Glycosylation751O-linked (GlcNAc) Ref.48

Natural variations

Alternative sequence74 – 829Missing in isoform 4 and isoform 5.
VSP_038813
Alternative sequence83 – 12139Missing in isoform 3.
VSP_038814
Alternative sequence297 – 2982HP → HRKCNYS in isoform 2.
VSP_038815
Alternative sequence511 – 55343DGSSN…CSSEC → G in isoform 5.
VSP_038816
Natural variant1321P → S in WVS. Ref.51
VAR_067595
Natural variant1531Missing in WVS. Ref.51
VAR_067596
Natural variant1851D → H.
Corresponds to variant rs2302427 [ dbSNP | Ensembl ].
VAR_055795
Natural variant6411Y → C in a patient with diffuse large B-cell lymphoma; somatic mutation. Ref.49
VAR_067228
Natural variant6411Y → F Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. Ref.49
VAR_067229
Natural variant6411Y → H Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. Ref.49
VAR_067230
Natural variant6411Y → N Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. Ref.49
VAR_067231
Natural variant6411Y → S Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. Ref.49
VAR_067232
Natural variant6851R → H in a patient with chronic myelomonocytic leukemia. Ref.50
VAR_067233
Natural variant6891H → Y in WVS. Ref.51
VAR_067597

Experimental info

Mutagenesis211S → A: Enhances methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1. Ref.23
Mutagenesis211S → D: Reduces methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1. Ref.23
Mutagenesis751S → A: Reduced protein stability. Ref.48
Mutagenesis3451T → A: Impaired CDK1- and CDK-2 mediated phosphorylation and subsequent gene silencing. Altered EZH2-mediated cell proliferation and migration. Ref.43
Mutagenesis5881C → Y: Strongly impairs methyltransferase activity towards 'Lys-27' of histone H3. Ref.12
Mutagenesis6891H → A: Abrogates methyltransferase activity. Ref.12 Ref.38
Sequence conflict391K → N in BAG52592. Ref.3
Sequence conflict2241F → L in CAA64955. Ref.1
Sequence conflict7241F → V in CAA64955. Ref.1

Secondary structure

..................................... 746
Helix Strand Turn

Details...

Sequences

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

Last modified July 15, 1998. Version 2.
Checksum: 1B5029EB9D509BE5

FASTA74685,363
        10         20         30         40         50         60 
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL ERTEILNQEW 

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

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

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

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

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

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

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

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

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

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

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

       730        740 
ELFFDYRYSQ ADALKYVGIE REMEIP 

« Hide

Isoform 2 [UniParc].

Checksum: D885CF02E60EF836
Show »

FASTA75186,018
Isoform 3 [UniParc].

Checksum: 48EAF1393A9EA4F2
Show »

FASTA70781,038
Isoform 4 [UniParc].

Checksum: 3DC6EA40E093A80B
Show »

FASTA73784,377
Isoform 5 [UniParc].

Checksum: 9DEAFE0755468660
Show »

FASTA69579,621

References

« Hide 'large scale' references
[1]"Cloning of a human homolog of the Drosophila enhancer of zeste gene (EZH2) that maps to chromosome 21q22.2."
Chen H., Rossier C., Antonarakis S.E.
Genomics 38:30-37(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Mammalian homologues of the Polycomb-group gene Enhancer of zeste mediate gene silencing in Drosophila heterochromatin and at S. cerevisiae telomeres."
Laible G., Wolf A., Dorn R., Reuter G., Nislow C., Lebersorger A., Popkin D., Pillus L., Jenuwein T.
EMBO J. 16:3219-3232(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
Tissue: Brain and Testis.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 2).
Tissue: Pancreas.
[7]"Interaction of Vav with ENX-1, a putative transcriptional regulator of homeobox gene expression."
Hobert O., Jallal B., Ullrich A.
Mol. Cell. Biol. 16:3066-3073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-746.
[8]"Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein."
Cardoso C., Timsit S., Villard L., Khrestchatisky M., Fontes M., Colleaux L.
Hum. Mol. Genet. 7:679-684(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATRX.
[9]"Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes."
Sewalt R.G.A.B., van der Vlag J., Gunster M.J., Hamer K.M., den Blaauwen J.L., Satijn D.P.E., Hendrix T., van Driel R., Otte A.P.
Mol. Cell. Biol. 18:3586-3595(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EED, SUBCELLULAR LOCATION.
[10]"Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation."
van der Vlag J., Otte A.P.
Nat. Genet. 23:474-478(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EED; HDAC1 AND HDAC2.
[11]"The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos."
Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.
Mol. Cell. Biol. 21:1360-1369(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EED.
[12]"Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein."
Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.
Genes Dev. 16:2893-2905(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EED; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, MUTAGENESIS OF CYS-588 AND HIS-689.
[13]"Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins."
Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L., Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.
Mol. Cell. Biol. 22:5539-5553(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EED; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
[15]"EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer."
Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K.
EMBO J. 22:5323-5335(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, TISSUE SPECIFICITY.
[16]"Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity."
Pasini D., Bracken A.P., Jensen M.R., Lazzerini Denchi E., Helin K.
EMBO J. 23:4061-4071(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EED AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
[17]"Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27."
Kirmizis A., Bartley S.M., Kuzmichev A., Margueron R., Reinberg D., Green R., Farnham P.J.
Genes Dev. 18:1592-1605(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3."
Kuzmichev A., Jenuwein T., Tempst P., Reinberg D.
Mol. Cell 14:183-193(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND PRC3 COMPLEXES.
[19]"SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex."
Cao R., Zhang Y.
Mol. Cell 15:57-67(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED; EZH2; RBBP4 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
[20]"Activated p53 suppresses the histone methyltransferase EZH2 gene."
Tang X., Milyavsky M., Shats I., Erez N., Goldfinger N., Rotter V.
Oncogene 23:5759-5769(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, INDUCTION.
[21]"The human tumor antigen PRAME is a dominant repressor of retinoic acid receptor signaling."
Epping M.T., Wang L., Edel M.J., Carlee L., Hernandez M., Bernards R.
Cell 122:835-847(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RETINOIC ACID SIGNALING, INTERACTION WITH PRAME.
[22]"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: CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4; RBBP7; SUZ12 AND SIRT1, METHYLTRANSFERASE ACTIVITY OF THE PRC4 COMPLEX.
[23]"Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3."
Cha T.-L., Zhou B.P., Xia W., Wu Y., Yang C.-C., Chen C.-T., Ping B., Otte A.P., Hung M.-C.
Science 310:306-310(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EED AND SUZ12, PHOSPHORYLATION BY AKT1, MUTAGENESIS OF SER-21.
[24]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions."
Bracken A.P., Dietrich N., Pasini D., Hansen K.H., Helin K.
Genes Dev. 20:1123-1136(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[26]"Substrate preferences of the EZH2 histone methyltransferase complex."
Martin C., Cao R., Zhang Y.
J. Biol. Chem. 281:8365-8370(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
[27]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"The Polycomb group protein EZH2 directly controls DNA methylation."
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.
Nature 439:871-874(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION OF THE PRC2 COMPLEX WITH DNMT1; DNMT3A AND DNMT3B.
[29]Erratum
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.
Nature 446:824-824(2006)
[30]"Argonaute-1 directs siRNA-mediated transcriptional gene silencing in human cells."
Kim D.H., Villeneuve L.M., Morris K.V., Rossi J.J.
Nat. Struct. Mol. Biol. 13:793-797(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"pRB family proteins are required for H3K27 trimethylation and Polycomb repression complexes binding to and silencing p16INK4alpha tumor suppressor gene."
Kotake Y., Cao R., Viatour P., Sage J., Zhang Y., Xiong Y.
Genes Dev. 21:49-54(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[32]"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: FUNCTION, DEVELOPMENTAL STAGE, INDUCTION.
[33]"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer."
Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M., Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E., Bergman Y., Simon I., Cedar H.
Nat. Genet. 39:232-236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DE NOVO DNA METHYLATION OF PRC2 TARGET GENES.
[34]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"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: FUNCTION, IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
[37]"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: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
[38]"Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo."
Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.
Mol. Cell. Biol. 28:2718-2731(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EED; SUZ12 AND PHF1, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, MUTAGENESIS OF HIS-689.
[39]"The polycomb repressive complex 2 is a potential target of SUMO modifications."
Riising E.M., Boggio R., Chiocca S., Helin K., Pasini D.
PLoS ONE 3:E2704-E2704(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[40]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; THR-367 AND THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[41]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[43]"Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2."
Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A., Simon J.A., Huang H.
Nat. Cell Biol. 12:1108-1114(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-345 BY CDK1 AND CDK2, MUTAGENESIS OF THR-345.
[44]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[45]"Corepressor protein CDYL functions as a molecular bridge between polycomb repressor complex 2 and repressive chromatin mark trimethylated histone lysine 27."
Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.
J. Biol. Chem. 286:42414-42425(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDYL.
[46]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[47]"EZH2 generates a methyl degron that is recognized by the DCAF1/DDB1/CUL4 E3 ubiquitin ligase complex."
Lee J.M., Lee J.S., Kim H., Kim K., Park H., Kim J.Y., Lee S.H., Kim I.S., Kim J., Lee M., Chung C.H., Seo S.B., Yoon J.B., Ko E., Noh D.Y., Kim K.I., Kim K.K., Baek S.H.
Mol. Cell 48:572-586(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[48]"O-GlcNAcylation regulates EZH2 protein stability and function."
Chu C.S., Lo P.W., Yeh Y.H., Hsu P.H., Peng S.H., Teng Y.C., Kang M.L., Wong C.H., Juan L.J.
Proc. Natl. Acad. Sci. U.S.A. 111:1355-1360(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-75, MUTAGENESIS OF SER-75, FUNCTION.
[49]"Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin."
Morin R.D., Johnson N.A., Severson T.M., Mungall A.J., An J., Goya R., Paul J.E., Boyle M., Woolcock B.W., Kuchenbauer F., Yap D., Humphries R.K., Griffith O.L., Shah S., Zhu H., Kimbara M., Shashkin P., Charlot J.F. expand/collapse author list , Tcherpakov M., Corbett R., Tam A., Varhol R., Smailus D., Moksa M., Zhao Y., Delaney A., Qian H., Birol I., Schein J., Moore R., Holt R., Horsman D.E., Connors J.M., Jones S., Aparicio S., Hirst M., Gascoyne R.D., Marra M.A.
Nat. Genet. 42:181-185(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PHE-641; SER-641; ASN-641; HIS-641 AND CYS-641.
[50]"Mutational spectrum analysis of chronic myelomonocytic leukemia includes genes associated with epigenetic regulation: UTX, EZH2, and DNMT3A."
Jankowska A.M., Makishima H., Tiu R.V., Szpurka H., Huang Y., Traina F., Visconte V., Sugimoto Y., Prince C., O'Keefe C., Hsi E.D., List A., Sekeres M.A., Rao A., McDevitt M.A., Maciejewski J.P.
Blood 118:3932-3941(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-685.
[51]"Mutations in EZH2 cause Weaver syndrome."
Gibson W.T., Hood R.L., Zhan S.H., Bulman D.E., Fejes A.P., Moore R., Mungall A.J., Eydoux P., Babul-Hirji R., An J., Marra M.A., Chitayat D., Boycott K.M., Weaver D.D., Jones S.J.
Am. J. Hum. Genet. 90:110-118(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WVS SER-132; TYR-153 DEL AND TYR-689.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95653 mRNA. Translation: CAA64955.1.
U61145 mRNA. Translation: AAC51520.1.
AK302216 mRNA. Translation: BAH13652.1.
AK092676 mRNA. Translation: BAG52592.1.
AK293239 mRNA. Translation: BAH11472.1.
AK314291 mRNA. Translation: BAG36948.1.
AC006323 Genomic DNA. No translation available.
AC073140 Genomic DNA. Translation: AAS07448.1. Sequence problems.
CH471146 Genomic DNA. Translation: EAW80067.1.
CH471146 Genomic DNA. Translation: EAW80070.1.
BC010858 mRNA. Translation: AAH10858.1.
U52965 Genomic DNA. Translation: AAC50591.1.
PIRG02838.
RefSeqNP_001190176.1. NM_001203247.1.
NP_001190177.1. NM_001203248.1.
NP_001190178.1. NM_001203249.1.
NP_004447.2. NM_004456.4.
NP_694543.1. NM_152998.2.
UniGeneHs.444082.
Hs.732308.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C6Vmodel-A508-734[»]
4MI0X-ray2.00A520-746[»]
4MI5X-ray2.00A521-746[»]
ProteinModelPortalQ15910.
SMRQ15910. Positions 40-68, 520-729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108446. 100 interactions.
DIPDIP-34002N.
IntActQ15910. 64 interactions.
MINTMINT-1371596.
STRING9606.ENSP00000320147.

Chemistry

ChEMBLCHEMBL2189110.

PTM databases

PhosphoSiteQ15910.

Polymorphism databases

DMDM3334180.

Proteomic databases

PaxDbQ15910.
PRIDEQ15910.

Protocols and materials databases

DNASU2146.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320356; ENSP00000320147; ENSG00000106462. [Q15910-2]
ENST00000350995; ENSP00000223193; ENSG00000106462. [Q15910-3]
ENST00000460911; ENSP00000419711; ENSG00000106462. [Q15910-1]
ENST00000476773; ENSP00000419050; ENSG00000106462. [Q15910-5]
ENST00000478654; ENSP00000417062; ENSG00000106462. [Q15910-5]
ENST00000483967; ENSP00000419856; ENSG00000106462. [Q15910-4]
ENST00000541220; ENSP00000443219; ENSG00000106462. [Q15910-5]
GeneID2146.
KEGGhsa:2146.
UCSCuc003wfb.2. human. [Q15910-2]
uc003wfc.2. human. [Q15910-3]
uc003wfd.2. human. [Q15910-1]
uc011kug.2. human. [Q15910-5]
uc011kuh.2. human. [Q15910-4]

Organism-specific databases

CTD2146.
GeneCardsGC07M148504.
HGNCHGNC:3527. EZH2.
HPACAB009589.
HPA029131.
MIM277590. phenotype.
601573. gene.
neXtProtNX_Q15910.
Orphanet3447. Weaver syndrome.
PharmGKBPA27939.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG002453.
InParanoidQ15910.
KOK11430.
OMANRDDKES.
OrthoDBEOG7VB2DR.
PhylomeDBQ15910.
TreeFamTF314509.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkQ15910.

Gene expression databases

ArrayExpressQ15910.
BgeeQ15910.
CleanExHS_EZH2.
GenevestigatorQ15910.

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. human.
GeneWikiEZH2.
GenomeRNAi2146.
NextBio8675.
PROQ15910.
SOURCESearch...

Entry information

Entry nameEZH2_HUMAN
AccessionPrimary (citable) accession number: Q15910
Secondary accession number(s): B2RAQ1 expand/collapse secondary AC list , B3KS30, B7Z1D6, B7Z7L6, Q15755, Q75MG3, Q92857, Q96FI6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM