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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
  • primary miRNA binding Source: Ensembl
  • promoter-specific chromatin binding Source: UniProtKB
  • protein-lysine N-methyltransferase activity Source: Reactome
  • ribonucleoprotein complex binding Source: Ensembl
  • RNA polymerase II core promoter 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

BioCyciZFISH:HS02911-MONOMER.
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_067595132P → S in WVS. 1 PublicationCorresponds to variant rs193921148dbSNPEnsembl.1
Natural variantiVAR_067596153Missing in WVS. 1 Publication1
Natural variantiVAR_067597689H → Y in WVS. 1 PublicationCorresponds to variant rs193921147dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21S → A: Enhances methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1. 1 Publication1
Mutagenesisi21S → D: Reduces methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1. 1 Publication1
Mutagenesisi75S → A: Reduced protein stability. 1 Publication1
Mutagenesisi345T → A: Impaired CDK1- and CDK-2 mediated phosphorylation and subsequent gene silencing. Altered EZH2-mediated cell proliferation and migration. 1 Publication1
Mutagenesisi588C → Y: Strongly impairs methyltransferase activity towards 'Lys-27' of histone H3. 1 Publication1
Mutagenesisi689H → A: Abrogates methyltransferase activity. 2 Publications1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2146.
MalaCardsiEZH2.
MIMi277590. phenotype.
OpenTargetsiENSG00000106462.
Orphaneti3447. Weaver syndrome.
PharmGKBiPA27939.

Chemistry databases

ChEMBLiCHEMBL2189110.
GuidetoPHARMACOLOGYi2654.

Polymorphism and mutation databases

BioMutaiEZH2.
DMDMi3334180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002139921 – 746Histone-lysine N-methyltransferase EZH2Add BLAST746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Phosphoserine; by PKB/AKT11 Publication1
Glycosylationi75O-linked (GlcNAc)1 Publication1
Modified residuei76PhosphoserineCombined sources1
Modified residuei339PhosphothreonineCombined sources1
Modified residuei345Phosphothreonine; by CDK1 and CDK21 Publication1
Modified residuei363PhosphoserineCombined sources1
Modified residuei366PhosphoserineCombined sources1
Modified residuei367PhosphothreonineCombined sources1
Modified residuei487PhosphothreonineCombined sources1

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.
PhosphoSitePlusiQ15910.

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.
EEDO7553011EBI-530054,EBI-923794
LOXL2Q9Y4K02EBI-530054,EBI-7172227
PHF1O431894EBI-530054,EBI-530034
PML-RARQ151568EBI-530054,EBI-867256
RARAP102762EBI-530054,EBI-413374
STAT3P407635EBI-530054,EBI-518675
SUV39H1O434632EBI-530054,EBI-349968

Protein-protein interaction databases

BioGridi108446. 278 interactors.
DIPiDIP-34002N.
IntActiQ15910. 105 interactors.
MINTiMINT-1371596.
STRINGi9606.ENSP00000320147.

Chemistry databases

BindingDBiQ15910.

Structurei

Secondary structure

1746
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 62Combined sources51
Beta strandi82 – 87Combined sources6
Beta strandi94 – 97Combined sources4
Beta strandi99 – 101Combined sources3
Beta strandi126 – 129Combined sources4
Helixi135 – 138Combined sources4
Turni139 – 143Combined sources5
Helixi144 – 152Combined sources9
Turni153 – 155Combined sources3
Helixi168 – 181Combined sources14
Helixi221 – 230Combined sources10
Turni232 – 234Combined sources3
Helixi237 – 248Combined sources12
Helixi274 – 284Combined sources11
Turni287 – 289Combined sources3
Beta strandi291 – 293Combined sources3
Turni304 – 306Combined sources3
Helixi332 – 343Combined sources12
Helixi434 – 443Combined sources10
Turni444 – 446Combined sources3
Helixi451 – 458Combined sources8
Beta strandi459 – 461Combined sources3
Helixi463 – 471Combined sources9
Beta strandi526 – 528Combined sources3
Helixi535 – 538Combined sources4
Beta strandi563 – 565Combined sources3
Helixi572 – 575Combined sources4
Turni582 – 584Combined sources3
Beta strandi587 – 589Combined sources3
Beta strandi594 – 596Combined sources3
Beta strandi600 – 603Combined sources4
Helixi605 – 608Combined sources4
Beta strandi614 – 618Combined sources5
Beta strandi620 – 630Combined sources11
Beta strandi637 – 640Combined sources4
Beta strandi643 – 647Combined sources5
Helixi648 – 656Combined sources9
Beta strandi666 – 668Combined sources3
Beta strandi670 – 676Combined sources7
Turni678 – 680Combined sources3
Helixi683 – 686Combined sources4
Beta strandi687 – 689Combined sources3
Beta strandi694 – 702Combined sources9
Beta strandi705 – 714Combined sources10
Helixi726 – 730Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini503 – 605CXCPROSITE-ProRule annotationAdd BLAST103
Domaini612 – 727SETPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 340Interaction with DNMT1, DNMT3A and DNMT3BAdd BLAST340
Regioni39 – 68Interaction with EEDBy similarityAdd BLAST30
Regioni329 – 522Interaction with CDYL1 PublicationAdd BLAST194

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi523 – 605Cys-richAdd BLAST83

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.
GeneTreeiENSGT00780000121845.
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)DescriptionActionsGraphical viewLength
Sequence conflicti39K → N in BAG52592 (PubMed:14702039).Curated1
Sequence conflicti224F → L in CAA64955 (PubMed:8954776).Curated1
Sequence conflicti724F → V in CAA64955 (PubMed:8954776).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067595132P → S in WVS. 1 PublicationCorresponds to variant rs193921148dbSNPEnsembl.1
Natural variantiVAR_067596153Missing in WVS. 1 Publication1
Natural variantiVAR_055795185D → H.Corresponds to variant rs2302427dbSNPEnsembl.1
Natural variantiVAR_067228641Y → C in a patient with diffuse large B-cell lymphoma; somatic mutation. 1 Publication1
Natural variantiVAR_067229641Y → F Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 PublicationCorresponds to variant rs267601394dbSNPEnsembl.1
Natural variantiVAR_067230641Y → H Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 PublicationCorresponds to variant rs267601395dbSNPEnsembl.1
Natural variantiVAR_067231641Y → N Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 Publication1
Natural variantiVAR_067232641Y → S Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 Publication1
Natural variantiVAR_067233685R → H in a patient with chronic myelomonocytic leukemia. 1 Publication1
Natural variantiVAR_067597689H → Y in WVS. 1 PublicationCorresponds to variant rs193921147dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03881374 – 82Missing in isoform 4 and isoform 5. 1 Publication9
Alternative sequenceiVSP_03881483 – 121Missing in isoform 3. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_038815297 – 298HP → HRKCNYS in isoform 2. 1 Publication2
Alternative sequenceiVSP_038816511 – 553DGSSN…CSSEC → G in isoform 5. 1 PublicationAdd BLAST43

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108446. 278 interactors.
DIPiDIP-34002N.
IntActiQ15910. 105 interactors.
MINTiMINT-1371596.
STRINGi9606.ENSP00000320147.

Chemistry databases

BindingDBiQ15910.
ChEMBLiCHEMBL2189110.
GuidetoPHARMACOLOGYi2654.

PTM databases

iPTMnetiQ15910.
PhosphoSitePlusiQ15910.

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.
DisGeNETi2146.
GeneCardsiEZH2.
GeneReviewsiEZH2.
HGNCiHGNC:3527. EZH2.
HPAiCAB009589.
HPA029131.
MalaCardsiEZH2.
MIMi277590. phenotype.
601573. gene.
neXtProtiNX_Q15910.
OpenTargetsiENSG00000106462.
Orphaneti3447. Weaver syndrome.
PharmGKBiPA27939.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1079. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOVERGENiHBG002453.
InParanoidiQ15910.
KOiK11430.
OMAiITCKNVC.
PhylomeDBiQ15910.
TreeFamiTF314509.

Enzyme and pathway databases

BioCyciZFISH:HS02911-MONOMER.
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: November 30, 2016
This is version 165 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.