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Q15910

- EZH2_HUMAN

UniProt

Q15910 - EZH2_HUMAN

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Protein
Histone-lysine N-methyltransferase EZH2
Gene
EZH2, KMT6
Organism
Homo sapiens (Human)
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 '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.15 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. RNA binding Source: Ensembl
  3. chromatin DNA binding Source: UniProt
  4. chromatin binding Source: UniProtKB
  5. core promoter binding Source: Ensembl
  6. histone methyltransferase activity Source: MGI
  7. histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
  8. protein binding Source: UniProtKB
  9. sequence-specific DNA binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. G1 to G0 transition Source: Ensembl
  2. cerebellar cortex development Source: Ensembl
  3. chromatin organization Source: ProtInc
  4. histone H3-K27 methylation Source: UniProtKB
  5. negative regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  6. negative regulation of epidermal cell differentiation Source: Ensembl
  7. negative regulation of gene expression, epigenetic Source: UniProtKB
  8. negative regulation of retinoic acid receptor signaling pathway Source: UniProtKB
  9. negative regulation of striated muscle cell differentiation Source: Ensembl
  10. negative regulation of transcription elongation from RNA polymerase II promoter Source: Ensembl
  11. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. negative regulation of transcription, DNA-templated Source: UniProtKB
  13. positive regulation of MAP kinase activity Source: UniProtKB
  14. positive regulation of Ras GTPase activity Source: UniProtKB
  15. positive regulation of epithelial to mesenchymal transition Source: UniProtKB
  16. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  17. regulation of cell proliferation Source: Ensembl
  18. regulation of gliogenesis Source: Ensembl
  19. regulation of transcription, DNA-templated Source: ProtInc
  20. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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_169436. Oxidative Stress Induced Senescence.
REACT_200808. PRC2 methylates histones and DNA.
SignaLinkiQ15910.

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
Lysine N-methyltransferase 6
Gene namesi
Name:EZH2
Synonyms:KMT6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:3527. EZH2.

Subcellular locationi

Nucleus 4 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321P → S in WVS. 1 Publication
VAR_067595
Natural varianti153 – 1531Missing in WVS. 1 Publication
VAR_067596
Natural varianti689 – 6891H → Y in WVS. 1 Publication
VAR_067597

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211S → A: Enhances methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1. 1 Publication
Mutagenesisi21 – 211S → D: Reduces methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1. 1 Publication
Mutagenesisi75 – 751S → A: Reduced protein stability. 1 Publication
Mutagenesisi345 – 3451T → A: Impaired CDK1- and CDK-2 mediated phosphorylation and subsequent gene silencing. Altered EZH2-mediated cell proliferation and migration. 1 Publication
Mutagenesisi588 – 5881C → Y: Strongly impairs methyltransferase activity towards 'Lys-27' of histone H3. 1 Publication
Mutagenesisi689 – 6891H → A: Abrogates methyltransferase activity. 2 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi277590. phenotype.
Orphaneti3447. Weaver syndrome.
PharmGKBiPA27939.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 746746Histone-lysine N-methyltransferase EZH2
PRO_0000213992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine; by PKB/AKT11 Publication
Glycosylationi75 – 751O-linked (GlcNAc)1 Publication
Modified residuei345 – 3451Phosphothreonine; by CDK1 and CDK21 Publication
Modified residuei366 – 3661Phosphoserine1 Publication
Modified residuei367 – 3671Phosphothreonine1 Publication
Modified residuei487 – 4871Phosphothreonine8 Publications

Post-translational modificationi

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.2 Publications
Sumoylated.1 Publication
Glycosylated: O-GlcNAcylation at Ser-75 by OGT increases stability of EZH2 and facilitates the formation of H3K27me3 by the PRC2/EED-EZH2 complex.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15910.
PaxDbiQ15910.
PRIDEiQ15910.

PTM databases

PhosphoSiteiQ15910.

Expressioni

Tissue specificityi

Expressed in many tissues. Overexpressed in numerous tumor types including carcinomas of the breast, colon, larynx, lymphoma and testis.1 Publication

Developmental stagei

Expression decreases during senescence of embryonic fibroblasts (HEFs). Expression peaks at the G1/S phase boundary.3 Publications

Inductioni

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/TP53.3 Publications

Gene expression databases

ArrayExpressiQ15910.
BgeeiQ15910.
CleanExiHS_EZH2.
GenevestigatoriQ15910.

Organism-specific databases

HPAiCAB009589.
HPA029131.

Interactioni

Subunit structurei

Binds ATRX via the SET domain Inferred. 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/BMAL1.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASXL1Q8IXJ96EBI-530054,EBI-1646500
DNMT1P263588EBI-530054,EBI-719459
DNMT3AQ9Y6K16EBI-530054,EBI-923653
DNMT3BQ9UBC38EBI-530054,EBI-80125
Dnmt3lQ9CWR82EBI-530054,EBI-3043871From a different organism.
EEDO755307EBI-530054,EBI-923794
PML-RARQ151568EBI-530054,EBI-867256
RARAP102762EBI-530054,EBI-413374
STAT3P407635EBI-530054,EBI-518675
SUV39H1O434632EBI-530054,EBI-349968

Protein-protein interaction databases

BioGridi108446. 237 interactions.
DIPiDIP-34002N.
IntActiQ15910. 64 interactions.
MINTiMINT-1371596.
STRINGi9606.ENSP00000320147.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi535 – 5384
Beta strandi563 – 5653
Helixi572 – 5754
Turni582 – 5843
Beta strandi587 – 5893
Beta strandi600 – 6034
Helixi605 – 6084
Beta strandi614 – 6185
Beta strandi620 – 63011
Beta strandi637 – 6404
Beta strandi643 – 6475
Helixi648 – 6569
Beta strandi666 – 6683
Beta strandi670 – 6767
Turni678 – 6803
Helixi683 – 6864
Beta strandi687 – 6893
Beta strandi694 – 7029
Beta strandi705 – 71410

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C6Vmodel-A508-734[»]
4MI0X-ray2.00A520-746[»]
4MI5X-ray2.00A521-746[»]
ProteinModelPortaliQ15910.
SMRiQ15910. Positions 40-68, 520-729.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 605103CXC
Add
BLAST
Domaini612 – 727116SET
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 340340Interaction with DNMT1, DNMT3A and DNMT3B
Add
BLAST
Regioni39 – 6830Interaction with EED By similarity
Add
BLAST
Regioni329 – 522194Interaction with CDYL
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 CXC domain.
Contains 1 SET domain.

Phylogenomic databases

eggNOGiCOG2940.
HOVERGENiHBG002453.
InParanoidiQ15910.
KOiK11430.
OMAiNRDDKES.
OrthoDBiEOG7VB2DR.
PhylomeDBiQ15910.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15910-1) [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 RFRRADEVKS MFSSNRQKIL    50
ERTEILNQEW KQRRIQPVHI LTSVSSLRGT RECSVTSDLD FPTQVIPLKT 100
LNAVASVPIM YSWSPLQQNF MVEDETVLHN IPYMGDEVLD QDGTFIEELI 150
KNYDGKVHGD RECGFINDEI FVELVNALGQ YNDDDDDDDG DDPEEREEKQ 200
KDLEDHRDDK ESRPPRKFPS DKIFEAISSM FPDKGTAEEL KEKYKELTEQ 250
QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH 300
ATPNTYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP 350
GGRRRGRLPN NSSRPSTPTI NVLESKDTDS DREAGTETGG ENNDKEEEEK 400
KDETSSSSEA NSRCQTPIKM KPNIEPPENV EWSGAEASMF RVLIGTYYDN 450
FCAIARLIGT KTCRQVYEFR VKESSIIAPA PAEDVDTPPR 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):85,363
Last modified:July 15, 1998 - v2
Checksum:i1B5029EB9D509BE5
GO
Isoform 2 (identifier: Q15910-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     297-298: HP → HRKCNYS

Show »
Length:751
Mass (Da):86,018
Checksum:iD885CF02E60EF836
GO
Isoform 3 (identifier: Q15910-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     83-121: Missing.

Show »
Length:707
Mass (Da):81,038
Checksum:i48EAF1393A9EA4F2
GO
Isoform 4 (identifier: Q15910-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-82: Missing.

Note: No experimental confirmation available.

Show »
Length:737
Mass (Da):84,377
Checksum:i3DC6EA40E093A80B
GO
Isoform 5 (identifier: Q15910-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-82: Missing.
     511-553: DGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSEC → G

Note: No experimental confirmation available.

Show »
Length:695
Mass (Da):79,621
Checksum:i9DEAFE0755468660
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321P → S in WVS. 1 Publication
VAR_067595
Natural varianti153 – 1531Missing in WVS. 1 Publication
VAR_067596
Natural varianti185 – 1851D → H.
Corresponds to variant rs2302427 [ dbSNP | Ensembl ].
VAR_055795
Natural varianti641 – 6411Y → C in a patient with diffuse large B-cell lymphoma; somatic mutation. 1 Publication
VAR_067228
Natural varianti641 – 6411Y → F Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 Publication
VAR_067229
Natural varianti641 – 6411Y → H Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 Publication
VAR_067230
Natural varianti641 – 6411Y → N Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 Publication
VAR_067231
Natural varianti641 – 6411Y → S Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 Publication
VAR_067232
Natural varianti685 – 6851R → H in a patient with chronic myelomonocytic leukemia. 1 Publication
VAR_067233
Natural varianti689 – 6891H → Y in WVS. 1 Publication
VAR_067597

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei74 – 829Missing in isoform 4 and isoform 5.
VSP_038813
Alternative sequencei83 – 12139Missing in isoform 3.
VSP_038814Add
BLAST
Alternative sequencei297 – 2982HP → HRKCNYS in isoform 2.
VSP_038815
Alternative sequencei511 – 55343DGSSN…CSSEC → G in isoform 5.
VSP_038816Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391K → N in BAG52592. 1 Publication
Sequence conflicti224 – 2241F → L in CAA64955. 1 Publication
Sequence conflicti724 – 7241F → V in CAA64955. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS56516.1. [Q15910-1]
CCDS56517.1. [Q15910-5]
CCDS56518.1. [Q15910-4]
CCDS5891.1. [Q15910-2]
CCDS5892.1. [Q15910-3]
PIRiG02838.
RefSeqiNP_001190176.1. NM_001203247.1. [Q15910-1]
NP_001190177.1. NM_001203248.1. [Q15910-4]
NP_001190178.1. NM_001203249.1. [Q15910-5]
NP_004447.2. NM_004456.4. [Q15910-2]
NP_694543.1. NM_152998.2. [Q15910-3]
XP_006715946.1. XM_006715883.1. [Q15910-1]
XP_006715948.1. XM_006715885.1. [Q15910-4]
UniGeneiHs.444082.
Hs.732308.

Genome annotation databases

EnsembliENST00000320356; 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]
GeneIDi2146.
KEGGihsa:2146.
UCSCiuc003wfb.2. human. [Q15910-2]
uc003wfc.2. human. [Q15910-3]
uc003wfd.2. human. [Q15910-1]
uc011kug.2. human. [Q15910-5]
uc011kuh.2. human. [Q15910-4]

Polymorphism databases

DMDMi3334180.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS56516.1. [Q15910-1 ]
CCDS56517.1. [Q15910-5 ]
CCDS56518.1. [Q15910-4 ]
CCDS5891.1. [Q15910-2 ]
CCDS5892.1. [Q15910-3 ]
PIRi G02838.
RefSeqi NP_001190176.1. NM_001203247.1. [Q15910-1 ]
NP_001190177.1. NM_001203248.1. [Q15910-4 ]
NP_001190178.1. NM_001203249.1. [Q15910-5 ]
NP_004447.2. NM_004456.4. [Q15910-2 ]
NP_694543.1. NM_152998.2. [Q15910-3 ]
XP_006715946.1. XM_006715883.1. [Q15910-1 ]
XP_006715948.1. XM_006715885.1. [Q15910-4 ]
UniGenei Hs.444082.
Hs.732308.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C6V model - A 508-734 [» ]
4MI0 X-ray 2.00 A 520-746 [» ]
4MI5 X-ray 2.00 A 521-746 [» ]
ProteinModelPortali Q15910.
SMRi Q15910. Positions 40-68, 520-729.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108446. 237 interactions.
DIPi DIP-34002N.
IntActi Q15910. 64 interactions.
MINTi MINT-1371596.
STRINGi 9606.ENSP00000320147.

Chemistry

ChEMBLi CHEMBL2189110.
GuidetoPHARMACOLOGYi 2654.

PTM databases

PhosphoSitei Q15910.

Polymorphism databases

DMDMi 3334180.

Proteomic databases

MaxQBi Q15910.
PaxDbi Q15910.
PRIDEi Q15910.

Protocols and materials databases

DNASUi 2146.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320356 ; 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 ]
GeneIDi 2146.
KEGGi hsa:2146.
UCSCi uc003wfb.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

CTDi 2146.
GeneCardsi GC07M148504.
GeneReviewsi EZH2.
HGNCi HGNC:3527. EZH2.
HPAi CAB009589.
HPA029131.
MIMi 277590. phenotype.
601573. gene.
neXtProti NX_Q15910.
Orphaneti 3447. Weaver syndrome.
PharmGKBi PA27939.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
HOVERGENi HBG002453.
InParanoidi Q15910.
KOi K11430.
OMAi NRDDKES.
OrthoDBi EOG7VB2DR.
PhylomeDBi Q15910.
TreeFami TF314509.

Enzyme and pathway databases

Reactomei REACT_169436. Oxidative Stress Induced Senescence.
REACT_200808. PRC2 methylates histones and DNA.
SignaLinki Q15910.

Miscellaneous databases

ChiTaRSi EZH2. human.
GeneWikii EZH2.
GenomeRNAii 2146.
NextBioi 8675.
PROi Q15910.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15910.
Bgeei Q15910.
CleanExi HS_EZH2.
Genevestigatori Q15910.

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 ]
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Publicationsi

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  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.
    , 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.
    , 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. 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 AT SER-21 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. Cited for: FUNCTION, INTERACTION OF THE PRC2 COMPLEX WITH DNMT1; DNMT3A AND DNMT3B.
  29. "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.
  30. "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.
  31. "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.
  32. "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.
  33. "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.
  34. "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.
  35. "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.
  36. "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.
  37. "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.
  38. "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.
  39. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; THR-367 AND THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  40. "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].
  41. "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.
  42. "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.
  43. "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.
  44. "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.
  45. "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].
  46. "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.
  47. Cited for: GLYCOSYLATION AT SER-75, MUTAGENESIS OF SER-75, FUNCTION.
  48. Cited for: VARIANTS PHE-641; SER-641; ASN-641; HIS-641 AND CYS-641.
  49. "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.
  50. Cited for: VARIANTS WVS SER-132; TYR-153 DEL AND TYR-689.

Entry informationi

Entry nameiEZH2_HUMAN
AccessioniPrimary (citable) accession number: Q15910
Secondary accession number(s): B2RAQ1
, B3KS30, B7Z1D6, B7Z7L6, Q15755, Q75MG3, Q92857, Q96FI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: September 3, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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