Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone-lysine N-methyltransferase EZH2

Gene

EZH2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription.16 Publications

Catalytic activityi

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

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • chromatin DNA binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • DNA binding Source: ProtInc
  • histone-lysine N-methyltransferase activity Source: MGI
  • histone methyltransferase activity Source: MGI
  • histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
  • promoter-specific chromatin binding Source: UniProtKB
  • protein-lysine N-methyltransferase activity Source: Reactome
  • ribonucleoprotein complex binding Source: Ensembl
  • RNA binding Source: Ensembl
  • sequence-specific DNA binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiQ15910.
SIGNORiQ15910.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:3527. EZH2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • ESC/E(Z) complex Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: MGI
  • pronucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Weaver syndrome (WVS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:277590
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321P → S in WVS. 1 Publication
Corresponds to variant rs193921148 [ dbSNP | Ensembl ].
VAR_067595
Natural varianti153 – 1531Missing in WVS. 1 Publication
VAR_067596
Natural varianti689 – 6891H → Y in WVS. 1 Publication
Corresponds to variant rs193921147 [ dbSNP | Ensembl ].
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

MalaCardsiEZH2.
MIMi277590. phenotype.
Orphaneti3447. Weaver syndrome.
PharmGKBiPA27939.

Chemistry

ChEMBLiCHEMBL3137286.
GuidetoPHARMACOLOGYi2654.

Polymorphism and mutation databases

BioMutaiEZH2.
DMDMi3334180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 746746Histone-lysine N-methyltransferase EZH2PRO_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 residuei76 – 761PhosphoserineCombined sources
Modified residuei339 – 3391PhosphothreonineCombined sources
Modified residuei345 – 3451Phosphothreonine; by CDK1 and CDK21 Publication
Modified residuei363 – 3631PhosphoserineCombined sources
Modified residuei366 – 3661PhosphoserineCombined sources
Modified residuei367 – 3671PhosphothreonineCombined sources
Modified residuei487 – 4871PhosphothreonineCombined sources

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

EPDiQ15910.
MaxQBiQ15910.
PaxDbiQ15910.
PeptideAtlasiQ15910.
PRIDEiQ15910.

PTM databases

iPTMnetiQ15910.
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

BgeeiENSG00000106462.
CleanExiHS_EZH2.
ExpressionAtlasiQ15910. baseline and differential.
GenevisibleiQ15910. HS.

Organism-specific databases

HPAiCAB009589.
HPA029131.

Interactioni

Subunit structurei

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 CLOCK, ARNTL/BMAL1 and CRY1 (By similarity).By similarityCurated14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASXL1Q8IXJ96EBI-530054,EBI-1646500
ATRXP461002EBI-530054,EBI-396461
CEP63Q96MT83EBI-530054,EBI-741977
DNMT1P263588EBI-530054,EBI-719459
DNMT3AQ9Y6K16EBI-530054,EBI-923653
DNMT3BQ9UBC38EBI-530054,EBI-80125
Dnmt3lQ9CWR82EBI-530054,EBI-3043871From a different organism.
EEDO755309EBI-530054,EBI-923794
LOXL2Q9Y4K02EBI-530054,EBI-7172227
PML-RARQ151568EBI-530054,EBI-867256
RARAP102762EBI-530054,EBI-413374
STAT3P407635EBI-530054,EBI-518675
SUV39H1O434632EBI-530054,EBI-349968

Protein-protein interaction databases

BioGridi108446. 276 interactions.
DIPiDIP-34002N.
IntActiQ15910. 101 interactions.
MINTiMINT-1371596.
STRINGi9606.ENSP00000320147.

Chemistry

BindingDBiQ15910.

Structurei

Secondary structure

1
746
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi535 – 5384Combined sources
Beta strandi563 – 5653Combined sources
Helixi572 – 5754Combined sources
Turni582 – 5843Combined sources
Beta strandi587 – 5893Combined sources
Beta strandi600 – 6034Combined sources
Helixi605 – 6084Combined sources
Beta strandi614 – 6185Combined sources
Beta strandi620 – 63011Combined sources
Beta strandi637 – 6404Combined sources
Beta strandi643 – 6475Combined sources
Helixi648 – 6569Combined sources
Beta strandi666 – 6683Combined sources
Beta strandi670 – 6767Combined sources
Turni678 – 6803Combined sources
Helixi683 – 6864Combined sources
Beta strandi687 – 6893Combined sources
Beta strandi694 – 7029Combined sources
Beta strandi705 – 71410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C6Vmodel-A508-734[»]
4MI0X-ray2.00A520-746[»]
4MI5X-ray2.00A521-746[»]
5HYNX-ray2.95A/F/K/Q1-746[»]
5IJ7X-ray2.62A/B429-487[»]
A/B511-746[»]
5IJ8X-ray2.99A/B429-487[»]
A/B511-531[»]
A/B533-746[»]
ProteinModelPortaliQ15910.
SMRiQ15910. Positions 40-68, 520-729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 340340Interaction with DNMT1, DNMT3A and DNMT3BAdd
BLAST
Regioni39 – 6830Interaction with EEDBy similarityAdd
BLAST
Regioni329 – 522194Interaction with CDYLAdd
BLAST

Compositional bias

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1079. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG002453.
InParanoidiQ15910.
KOiK11430.
OMAiITCKNVC.
PhylomeDBiQ15910.
TreeFamiTF314509.

Family and domain databases

InterProiIPR026489. CXC_dom.
IPR021654. EZH1/EZH2.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
IPR033467. Tesmin/TSO1-like_CXC.
[Graphical view]
PfamiPF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM01114. CXC. 1 hit.
SM00717. 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. AlignAdd to basket

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

        10         20         30         40         50
MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL
60 70 80 90 100
ERTEILNQEW KQRRIQPVHI LTSVSSLRGT RECSVTSDLD FPTQVIPLKT
110 120 130 140 150
LNAVASVPIM YSWSPLQQNF MVEDETVLHN IPYMGDEVLD QDGTFIEELI
160 170 180 190 200
KNYDGKVHGD RECGFINDEI FVELVNALGQ YNDDDDDDDG DDPEEREEKQ
210 220 230 240 250
KDLEDHRDDK ESRPPRKFPS DKIFEAISSM FPDKGTAEEL KEKYKELTEQ
260 270 280 290 300
QLPGALPPEC TPNIDGPNAK SVQREQSLHS FHTLFCRRCF KYDCFLHPFH
310 320 330 340 350
ATPNTYKRKN TETALDNKPC GPQCYQHLEG AKEFAAALTA ERIKTPPKRP
360 370 380 390 400
GGRRRGRLPN NSSRPSTPTI NVLESKDTDS DREAGTETGG ENNDKEEEEK
410 420 430 440 450
KDETSSSSEA NSRCQTPIKM KPNIEPPENV EWSGAEASMF RVLIGTYYDN
460 470 480 490 500
FCAIARLIGT KTCRQVYEFR VKESSIIAPA PAEDVDTPPR KKKRKHRLWA
510 520 530 540 550
AHCRKIQLKK DGSSNHVYNY QPCDHPRQPC DSSCPCVIAQ NFCEKFCQCS
560 570 580 590 600
SECQNRFPGC RCKAQCNTKQ CPCYLAVREC DPDLCLTCGA ADHWDSKNVS
610 620 630 640 650
CKNCSIQRGS KKHLLLAPSD VAGWGIFIKD PVQKNEFISE YCGEIISQDE
660 670 680 690 700
ADRRGKVYDK YMCSFLFNLN NDFVVDATRK GNKIRFANHS VNPNCYAKVM
710 720 730 740
MVNGDHRIGI FAKRAIQTGE ELFFDYRYSQ ADALKYVGIE REMEIP
Length:746
Mass (Da):85,363
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 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391K → N in BAG52592 (PubMed:14702039).Curated
Sequence conflicti224 – 2241F → L in CAA64955 (PubMed:8954776).Curated
Sequence conflicti724 – 7241F → V in CAA64955 (PubMed:8954776).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321P → S in WVS. 1 Publication
Corresponds to variant rs193921148 [ dbSNP | Ensembl ].
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
Corresponds to variant rs193921147 [ dbSNP | Ensembl ].
VAR_067597

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei74 – 829Missing in isoform 4 and isoform 5. 1 PublicationVSP_038813
Alternative sequencei83 – 12139Missing in isoform 3. 1 PublicationVSP_038814Add
BLAST
Alternative sequencei297 – 2982HP → HRKCNYS in isoform 2. 1 PublicationVSP_038815
Alternative sequencei511 – 55343DGSSN…CSSEC → G in isoform 5. 1 PublicationVSP_038816Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_011514186.1. XM_011515884.2. [Q15910-2]
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]
GeneIDi2146.
KEGGihsa:2146.
UCSCiuc003wfb.3. human. [Q15910-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_011514186.1. XM_011515884.2. [Q15910-2]
UniGeneiHs.444082.
Hs.732308.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C6Vmodel-A508-734[»]
4MI0X-ray2.00A520-746[»]
4MI5X-ray2.00A521-746[»]
5HYNX-ray2.95A/F/K/Q1-746[»]
5IJ7X-ray2.62A/B429-487[»]
A/B511-746[»]
5IJ8X-ray2.99A/B429-487[»]
A/B511-531[»]
A/B533-746[»]
ProteinModelPortaliQ15910.
SMRiQ15910. Positions 40-68, 520-729.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108446. 276 interactions.
DIPiDIP-34002N.
IntActiQ15910. 101 interactions.
MINTiMINT-1371596.
STRINGi9606.ENSP00000320147.

Chemistry

BindingDBiQ15910.
ChEMBLiCHEMBL3137286.
GuidetoPHARMACOLOGYi2654.

PTM databases

iPTMnetiQ15910.
PhosphoSiteiQ15910.

Polymorphism and mutation databases

BioMutaiEZH2.
DMDMi3334180.

Proteomic databases

EPDiQ15910.
MaxQBiQ15910.
PaxDbiQ15910.
PeptideAtlasiQ15910.
PRIDEiQ15910.

Protocols and materials databases

DNASUi2146.
Structural Biology KnowledgebaseSearch...

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]
GeneIDi2146.
KEGGihsa:2146.
UCSCiuc003wfb.3. human. [Q15910-1]

Organism-specific databases

CTDi2146.
GeneCardsiEZH2.
GeneReviewsiEZH2.
HGNCiHGNC:3527. EZH2.
HPAiCAB009589.
HPA029131.
MalaCardsiEZH2.
MIMi277590. phenotype.
601573. gene.
neXtProtiNX_Q15910.
Orphaneti3447. Weaver syndrome.
PharmGKBiPA27939.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1079. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG002453.
InParanoidiQ15910.
KOiK11430.
OMAiITCKNVC.
PhylomeDBiQ15910.
TreeFamiTF314509.

Enzyme and pathway databases

ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiQ15910.
SIGNORiQ15910.

Miscellaneous databases

ChiTaRSiEZH2. human.
GeneWikiiEZH2.
GenomeRNAii2146.
PROiQ15910.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106462.
CleanExiHS_EZH2.
ExpressionAtlasiQ15910. baseline and differential.
GenevisibleiQ15910. HS.

Family and domain databases

InterProiIPR026489. CXC_dom.
IPR021654. EZH1/EZH2.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
IPR033467. Tesmin/TSO1-like_CXC.
[Graphical view]
PfamiPF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM01114. CXC. 1 hit.
SM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 7, 2016
This is version 162 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

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 (PubMed:15099518 and PubMed:15684044), although other studies have demonstrated no methylation of 'Lys-26' of histone H1 by PRC2 (PubMed:16431907).1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.