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UniProtKB - Q15910 (EZH2_HUMAN)

Entry version 205 (07 Apr 2021)
Sequence version 2 (15 Jul 1998)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2 (PubMed:22323599, PubMed:30923826). Compared to EZH1-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.18 Publications

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, Methyltransferase, Repressor, Transferase
Biological processBiological rhythms, Transcription, Transcription regulation
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS02911-MONOMER

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q15910

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-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
R-HSA-8943724, Regulation of PTEN gene transcription
R-HSA-8953750, Transcriptional Regulation by E2F6
R-HSA-9609690, HCMV Early Events

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q15910

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q15910

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone-lysine N-methyltransferase EZH2Curated (EC:2.1.1.3561 Publication)
Alternative name(s):
ENX-1
Enhancer of zeste homolog 21 Publication
Lysine N-methyltransferase 6
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EZH2Imported
Synonyms:KMT6
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3527, EZH2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601573, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q15910

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000106462.10

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Weaver syndrome (WVS)5 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_067595132P → S in WVS; decreased histone methyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs193921148EnsemblClinVar.1
Natural variantiVAR_078320133Y → C in WVS; decreased histone methyltransferase activity. 1 Publication1
Natural variantiVAR_078321134M → T in WVS. 1 Publication1
Natural variantiVAR_067596153Missing in WVS; decreased histone methyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs193921146Ensembl.1
Natural variantiVAR_078322156K → E in WVS. 1 Publication1
Natural variantiVAR_078323279H → R in WVS. 1 Publication1
Natural variantiVAR_078325621V → M in WVS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs587783625Ensembl.1
Natural variantiVAR_078326658Y → N in WVS. 1 Publication1
Natural variantiVAR_078328677A → T in WVS. 1 PublicationCorresponds to variant dbSNP:rs397515547Ensembl.1
Natural variantiVAR_078329679R → C in WVS; decreased histone methyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs587783626Ensembl.1
Natural variantiVAR_067597689H → Y in WVS; decreased histone methyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs193921147Ensembl.1
Natural variantiVAR_078331690S → L in WVS. 1 Publication1
Natural variantiVAR_078333728 – 746Missing in WVS. 1 PublicationAdd BLAST19
Natural variantiVAR_078334736Y → C in WVS. 1 Publication1
Natural variantiVAR_078335740E → K in WVS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs397515548Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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
Mutagenesisi667F → I: Strongly decreases histone methyltransferase activity. 1 Publication1
Mutagenesisi689H → A: Abrogates methyltransferase activity. 2 Publications1

Keywords - Diseasei

Disease variant

Organism-specific databases

DisGeNET

More...DisGeNETi		2146

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		EZH2

MalaCards human disease database

More...MalaCardsi		EZH2
MIMi277590, phenotype

Open Targets

More...OpenTargetsi		ENSG00000106462

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		3447, Weaver syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27939

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q15910, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2189110

Drug and drug target database

More...DrugBanki		DB14581, CPI-1205
DB12887, Tazemetostat

DrugCentral

More...DrugCentrali		Q15910

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2654

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		EZH2

Domain mapping of disease mutations (DMDM)

More...DMDMi		3334180

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002139921 – 746Histone-lysine N-methyltransferase EZH2Add BLAST746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei21Phosphoserine; by PKB/AKT11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi75O-linked (GlcNAc) serine1 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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki634Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q15910

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q15910

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q15910

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q15910

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q15910

PeptideAtlas

More...PeptideAtlasi		Q15910

PRoteomics IDEntifications database

More...PRIDEi		Q15910

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		60809 [Q15910-1]
60810 [Q15910-2]
60811 [Q15910-3]
60812 [Q15910-4]
60813 [Q15910-5]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q15910, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q15910

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q15910

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q15910

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

In the ovary, expressed in primordial follicles and oocytes and also in external follicle cells (at protein level) (PubMed:31451685). Expressed in many tissues (PubMed:14532106). Overexpressed in numerous tumor types including carcinomas of the breast, colon, larynx, lymphoma and testis (PubMed:14532106).2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000106462, Expressed in bone marrow and 172 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q15910, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q15910, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000106462, Tissue enhanced (bone marrow, lymphoid tissue)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

Interacts with DNMT3L; the interaction is direct (By similarity).

Interacts with EZHIP; the interaction blocks EZH2 methyltransferase activity (PubMed:30923826, PubMed:31086175, PubMed:31451685).

By similarityCurated17 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		108446, 746 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q15910

Database of interacting proteins

More...DIPi		DIP-34002N

Protein interaction database and analysis system

More...IntActi		Q15910, 126 interactors

Molecular INTeraction database

More...MINTi		Q15910

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000320147

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q15910

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q15910, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1746
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q15910

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini503 – 605CXCPROSITE-ProRule annotationAdd BLAST103
Domaini612 – 727SETPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi523 – 605Cys-richAdd BLAST83

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1079, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155013

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_011342_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q15910

Identification of Orthologs from Complete Genome Data

More...OMAi		KTFADPC

Database of Orthologous Groups

More...OrthoDBi		875190at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q15910

TreeFam database of animal gene trees

More...TreeFami		TF314509

Family and domain databases

Conserved Domains Database

More...CDDi		cd19218, SET_EZH2, 1 hit

Database of protein disorder

More...DisProti		DP01817

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR026489, CXC_dom
IPR021654, EZH1/EZH2
IPR044439, EZH2_SET
IPR041343, PRC2_HTH_1
IPR041355, Pre-SET_CXC
IPR001005, SANT/Myb
IPR001214, SET_dom
IPR033467, Tesmin/TSO1-like_CXC

Pfam protein domain database

More...Pfami		View protein in Pfam
PF11616, EZH2_WD-Binding, 1 hit
PF18118, PRC2_HTH_1, 1 hit
PF18264, preSET_CXC, 1 hit
PF00856, SET, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01114, CXC, 1 hit
SM00717, SANT, 2 hits
SM00317, SET, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51633, CXC, 1 hit
PS50280, SET, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q15910-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3XAL2G3XAL2_HUMAN
Enhancer of zeste homolog 2 (Drosop...
EZH2 hCG_15497
334Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PDH6E9PDH6_HUMAN
Histone-lysine N-methyltransferase ...
EZH2
144Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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; decreased histone methyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs193921148EnsemblClinVar.1
Natural variantiVAR_078320133Y → C in WVS; decreased histone methyltransferase activity. 1 Publication1
Natural variantiVAR_078321134M → T in WVS. 1 Publication1
Natural variantiVAR_067596153Missing in WVS; decreased histone methyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs193921146Ensembl.1
Natural variantiVAR_078322156K → E in WVS. 1 Publication1
Natural variantiVAR_055795185D → H Decreased histone methyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs2302427EnsemblClinVar.1
Natural variantiVAR_078323279H → R in WVS. 1 Publication1
Natural variantiVAR_078324571C → W Found in a patient with myelodysplastic syndrome and myelodysplastic-myeloproliferative neoplasms; somatic mutation; loss of histone methyltransferase activity. 1 Publication1
Natural variantiVAR_078325621V → M in WVS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs587783625Ensembl.1
Natural variantiVAR_067228641Y → C in a patient with diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2. 3 Publications1
Natural variantiVAR_067229641Y → F Found in a patient with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2. 2 PublicationsCorresponds to variant dbSNP:rs267601394Ensembl.1
Natural variantiVAR_067230641Y → H Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2. 2 PublicationsCorresponds to variant dbSNP:rs267601395Ensembl.1
Natural variantiVAR_067231641Y → N Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2. 2 PublicationsCorresponds to variant dbSNP:rs267601395Ensembl.1
Natural variantiVAR_067232641Y → S Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs267601394Ensembl.1
Natural variantiVAR_078326658Y → N in WVS. 1 Publication1
Natural variantiVAR_078327677A → G Found in a patient with B-cell lymphoma; increased hypertrimethylation of H3K27; changed substrate preferences; confers biochemical activity independent of H3K27 methylation state. 1 PublicationCorresponds to variant dbSNP:rs1057519833Ensembl.1
Natural variantiVAR_078328677A → T in WVS. 1 PublicationCorresponds to variant dbSNP:rs397515547Ensembl.1
Natural variantiVAR_078329679R → C in WVS; decreased histone methyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs587783626Ensembl.1
Natural variantiVAR_078330685R → C Found in a patient with myeloid disorders; somatic mutation; loss of histone methyltransferase activity. 1 Publication1
Natural variantiVAR_067233685R → H in a patient with chronic myelomonocytic leukemia. 1 PublicationCorresponds to variant dbSNP:rs1554481435Ensembl.1
Natural variantiVAR_067597689H → Y in WVS; decreased histone methyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs193921147Ensembl.1
Natural variantiVAR_078331690S → L in WVS. 1 Publication1
Natural variantiVAR_078332726Y → D Found in a patient with chronic myelomonocytic leukemia; somatic mutation; loss of histone methyltransferase activity. 1 Publication1
Natural variantiVAR_078333728 – 746Missing in WVS. 1 PublicationAdd BLAST19
Natural variantiVAR_078334736Y → C in WVS. 1 Publication1
Natural variantiVAR_078335740E → K in WVS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs397515548Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS56516.1 [Q15910-1]
CCDS56517.1 [Q15910-5]
CCDS56518.1 [Q15910-4]
CCDS5891.1 [Q15910-2]
CCDS5892.1 [Q15910-3]

Protein sequence database of the Protein Information Resource

More...PIRi		G02838

NCBI Reference Sequences

More...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_011514186.1, XM_011515884.2 [Q15910-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...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]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2146

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2146

UCSC genome browser

More...UCSCi		uc003wfb.3, human [Q15910-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C6Vmodel-A508-734[»]
4MI0X-ray2.00A520-746[»]
4MI5X-ray2.00A521-746[»]
5GSAX-ray2.49C/D40-68[»]
5H14X-ray1.90C/D40-68[»]
5H15X-ray2.27C/D40-68[»]
5H17X-ray2.30B40-68[»]
5H19X-ray1.90B40-68[»]
5H24X-ray2.50C/D40-68[»]
5H25X-ray2.88C/D40-68[»]
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[»]
5LS6X-ray3.47A/D/G/J1-385[»]
A/D/G/J421-746[»]
5U5TX-ray1.60C/D39-68[»]
5U62X-ray1.90C/D39-68[»]
5WG6X-ray3.90A/C2-746[»]
5WUKX-ray2.03B41-68[»]
6C23electron microscopy3.90C/K1-746[»]
6C24electron microscopy3.50C/K1-746[»]
6P5LX-ray3.30D489-496[»]
6U4YX-ray2.91A/B/C2-182[»]
A/B/C220-257[»]
7AT8electron microscopy4.40A1-746[»]
SMRiQ15910
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi108446, 746 interactors
CORUMiQ15910
DIPiDIP-34002N
IntActiQ15910, 126 interactors
MINTiQ15910
STRINGi9606.ENSP00000320147

Chemistry databases

BindingDBiQ15910
ChEMBLiCHEMBL2189110
DrugBankiDB14581, CPI-1205
DB12887, Tazemetostat
DrugCentraliQ15910
GuidetoPHARMACOLOGYi2654

PTM databases

GlyGeniQ15910, 1 site
iPTMnetiQ15910
PhosphoSitePlusiQ15910
SwissPalmiQ15910

Genetic variation databases

BioMutaiEZH2
DMDMi3334180

Proteomic databases

EPDiQ15910
jPOSTiQ15910
MassIVEiQ15910
MaxQBiQ15910
PaxDbiQ15910
PeptideAtlasiQ15910
PRIDEiQ15910
ProteomicsDBi60809 [Q15910-1]
60810 [Q15910-2]
60811 [Q15910-3]
60812 [Q15910-4]
60813 [Q15910-5]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		32761, 829 antibodies

The DNASU plasmid repository

More...DNASUi		2146

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

Comparative Toxicogenomics Database

More...CTDi		2146
DisGeNETi2146

GeneCards: human genes, protein and diseases

More...GeneCardsi		EZH2
GeneReviewsiEZH2
HGNCiHGNC:3527, EZH2
HPAiENSG00000106462, Tissue enhanced (bone marrow, lymphoid tissue)
MalaCardsiEZH2
MIMi277590, phenotype
601573, gene
neXtProtiNX_Q15910
OpenTargetsiENSG00000106462
Orphaneti3447, Weaver syndrome
PharmGKBiPA27939
VEuPathDBiHostDB:ENSG00000106462.10

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1079, Eukaryota
GeneTreeiENSGT00940000155013
HOGENOMiCLU_011342_0_0_1
InParanoidiQ15910
OMAiKTFADPC
OrthoDBi875190at2759
PhylomeDBiQ15910
TreeFamiTF314509

Enzyme and pathway databases

BioCyciMetaCyc:HS02911-MONOMER
PathwayCommonsiQ15910
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
R-HSA-8943724, Regulation of PTEN gene transcription
R-HSA-8953750, Transcriptional Regulation by E2F6
R-HSA-9609690, HCMV Early Events
SignaLinkiQ15910
SIGNORiQ15910

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		2146, 56 hits in 1009 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		EZH2, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		EZH2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2146
PharosiQ15910, Tchem

Protein Ontology

More...PROi		PR:Q15910
RNActiQ15910, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000106462, Expressed in bone marrow and 172 other tissues
ExpressionAtlasiQ15910, baseline and differential
GenevisibleiQ15910, HS

Family and domain databases

CDDicd19218, SET_EZH2, 1 hit
DisProtiDP01817
InterProiView protein in InterPro
IPR026489, CXC_dom
IPR021654, EZH1/EZH2
IPR044439, EZH2_SET
IPR041343, PRC2_HTH_1
IPR041355, Pre-SET_CXC
IPR001005, SANT/Myb
IPR001214, SET_dom
IPR033467, Tesmin/TSO1-like_CXC
PfamiView protein in Pfam
PF11616, EZH2_WD-Binding, 1 hit
PF18118, PRC2_HTH_1, 1 hit
PF18264, preSET_CXC, 1 hit
PF00856, SET, 1 hit
SMARTiView protein in SMART
SM01114, CXC, 1 hit
SM00717, SANT, 2 hits
SM00317, SET, 1 hit
PROSITEiView protein in PROSITE
PS51633, CXC, 1 hit
PS50280, SET, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEZH2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q15910
Secondary accession number(s): B2RAQ1
, B3KS30, B7Z1D6, B7Z7L6, Q15755, Q75MG3, Q92857, Q96FI6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 7, 2021
This is version 205 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
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