EHMT2 (euchromatic histone-lysine N-methyltransferase 2)

2013-07-01   Chandra-Prakash Chaturvedi , Marjorie Brand 


Atlas Image
Genomic location of EHMT2/G9a gene along with adjustment genes on chromosome 6 (minus strand).


Atlas Image
EHMT2/G9a gene and RNA structure. Schematic representation of the human EHMT2/G9a gene organization demonstrating the relative position of each of the 28 exons (5UTR, exons and 3UTR are not drawn to scale). The shorter EHMT2 isoform b has missing exon 10 compared to full length EHMT2.


The human EHMT2/G9a Gene (NC_000006.11) is located on the minus strand and spans 17929 bps of genomic region (31847536 - 31865464). The long isoform of EHMT2/G9a comprises 28 exons, whereas the short isoform consists of 27 exons and lacks the sequence corresponding to exon 10 of the long isoform.


EHMT2/G9a gene has two differentially spliced transcript variants (Brown et al., 2001). G9a transcript variant I NG36/EHMT2 (accession number NM_006709.3) also called long isoform or isoform a, has 3982 bps open reading frame. G9a transcript variant II NG36/EHMT2-SP1 (accession number NM_025256.5) also called short Isoform or isoform b, has open reading frame of 3880 bps (Brown et al., 2001).


There is no known pseudogene for EHMT2/G9a.


Atlas Image
Schematic representation of the domain structure of EHMT2/G9a isoform a and isoform b. Isoform b is missing amino acid sequence 373-406 (34 aa) compared to the canonical isoform a (aa 1-1210). Isoform b is numbered according to isoform a, as well as separately. The positions of known domains within G9a are displayed. Transcription activation domain (TAD), E rich, glutamine-rich domain, NRSF- binding cysteine rich domain (12Cys) and ankyrin domain with seven ankyrin repeats and Set domain containing pre and post SET domains.


EHMT2/G9a isoform a (accession number NP_006700.3) is composed of 1210 amino acid residues while the shorter isoform b (accession number NP_079532.5) comprises 1176 amino acid residues (Figure 2). The G9a protein contains several evolutionarily conserved domains including, the N-terminus transcription activation domain (TAD), E-rich domain containing 24 contiguous glutamic acid residues and the cysteine (Cys) rich domain that contains 12 cysteine residues, the centrally located ankyrin (ANK) domain containing seven ankyrin repeats and the C-terminus SET domain (Milner and Campbell, 1993; Brown et al., 2001; Dillon et al., 2005). Functionally, the TAD domain of G9a has been shown to be involved in transcription activation and is sufficient to activate transcription of several nuclear receptor genes (Lee et al., 2006; Purcell et al., 2011, Bittencourt et al., 2012). The E-rich domain has been shown to be present in several proteins including the nuclear protein nucleolin, the chromosomal protein HMG1 and the centromere auto-antigen CENP-B (Milner and Campbell, 1993; Brown et al., 2001). The Cys rich domain acts as a binding site for neuron-restrictive silencing factor (NRSF) and has been shown to be involved in repression of neuronal genes in non-neuronal tissue (Roopra et al., 2004). The ANK domain, which is conserved in diverse proteins including transcription factors has been shown to be involved in protein-protein interactions (Milner and Campbell, 1993; Sedgwick and Smerdon, 1999), and binding to histone mono- and dimethylated H3 lysine 9 marks (Collins et al., 2008). The C-terminal SET domain is responsible for the methyltransferase activity of G9a (Tachibana et al., 2001; Tachibana et al., 2002) and is also required for interaction with GLP (Tachibana et al., 2005).


EHMT2/G9a RNA is present in a wide range of human tissues and cells with high levels in fetal liver, thymus, lymph node, spleen and peripheral blood leukocytes and lower level in bone marrow (Milner and Campbell, 1993; Brown et al., 2001).


EHMT2/G9a is localized in the nucleus. It is mostly associated with euchromatic regions of chromatin and absent from heterochromatin (Tachibana et al., 2002).


The histone methyltransferase G9a mono and dimethylates Lys-9 of histone H3 specifically in euchromatin (Tachibana et al., 2001; Tachibana et al., 2002). Furthermore, G9a can also mono and dimethylates Lys-27 of histone H3 and mono methylates histone H1 (Tachibana et al., 2001; Chaturvedi et al., 2009; Trojer et al 2009; Weiss et al., 2010; Wu et al., 2011). In addition, G9a methylates several non-histone proteins including p53, CDYL, WIZ, CSB, ACINUS, DNMT1, HDAC1, KLF12, MyoD, DNMT3a and MTA1 (Rathert et al., 2008; Haung et al., 2010; Chang et al., 2011; Ling at al., 2012; Nair et al., 2013) and automethylates (Chin et al., 2007; Rathert et al., 2008). G9a also plays an important role in mediating DNA methylation through its association with DNA methyltransferases (Epsztejn-Litman et al., 2008; Tachibana et al., 2008; Dong et al., 2008).
Transcriptionally, G9a can function both as a corepressor and/or a coactivator of gene expression, (Collins and Cheng, 2010; Yoichi and Tachibana, 2011; Shnakar et al., 2013; Lee et al., 2006; Chaturvedi et al., 2009; Purcell et al., 2011; Chaturvedi et al., 2012; Bittencourt et al., 2012). The corepressor function of the G9a is dependent on its enzymatic activity as well as on its interaction with other factors that are involved in gene repression (Tachibana et al., 2002; Yoichi and Tachibana, 2011; Chaturvedi et al., 2012; Shnakar et al., 2013). G9a gets targeted to specific genes by associating with various transcriptional repressors and corepressors such as, CDP/Cut, E2F6, Gfi1/zfp163, Blimp-1/PRDI-BF1, REST/NRSF, ZNF217 and PRISM/PRDM6 and several others (Tachibana et al., 2002; Ogawa et al., 2002; Gyory et al., 2004; Nashio and Walsh, 2004; Roopra et al., 2004; Daun et al., 2005; Davis et al., 2006; Nagano et al., 2008; Banck et al., 2009; Yoichi and Tachibana, 2011; Shnakar et al., 2013). The coactivator function of the G9a does not require its enzymatic activity but requires association with other transcriptional activators and/or coactivators factors including CARM1, p300, RNA polymerases or the Mediator complex (Lee et al., 2006; Chaturvedi et al., 2009; Purcell et al., 2011; Bittencourt et al., 2012; Chaturvedi et al., 2012).
Functionally, G9a has been shown to play important roles in regulating the expression of genes involved in various developmental and differentiation processes. G9a is indispensible for early embryonic development (Tachibana et al., 2002; Yoichi and Tachibana, 2011). The G9a knockout embryonic stem cells (ESCs) show severe defects in differentiation, suggesting that G9a positively regulates ESCs differentiation (Tachibana et al., 2002; Feldman et al., 2006; Kubicek et al., 2007; Shi et al., 2008). Similarly, G9a is required for proper differentiation, survival and lineage commitment of adult or somatic stem cells i.e hematopoietic progenitor stem cells, retinal progenitor cells (Chen et al., 2012; Katoh et al., 1212). Genome wide studies have revealed the presence of G9a mediated large H3K9 dimethylation (H3K9me2) chromatin blocks (LOCKS) on large chromatin region in the genome (Wen et al., 2009; Chen et al., 2012). These G9a mediated LOCKS are necessary for proper differentiation as the loss of LOCKs inhibits or delays differentiation and lineage commitment of both embryonic and adult stem cells (Wen et al., 2009; Chen et al., 2012). In contrast to its positive regulatory role in maintaining differentiation, G9a has been shown to negatively regulate differentiation by repressing differentiation specific genes in myogenesis and adipogenesis (Shankar et al., 2013; Ling et al., 2012a; Ling et al., 2012b; Wang and Abete-Shen, 2011; Wang et al., 2013).
Furthermore, G9a has been shown to regulate gene expression in multiple other biological processes including, genomic imprinting (Nagano et al., 2008; Wagschal et al., 2008), germ cells development (Tachibana et al., 2007), erythropoiesis (Chaturvedi et al., 2009; Chaturvedi et al., 2012), T and B cell mediated immune response (Thomas et al., 2008; Lehnertz et al., 2010) and nuclear receptor mediated gene expression (Lee et al., 2006; Purcell et al., 2011; Bittencourt et al., 2012). In the brain, G9a is required for proper expression of genes involved in lineage specific expression (Roopra et al., 2004, Schaefer et al., 2009), memory consolidation (Gupta et al., 2012), and cocaine induced neuronal responses and behavioural plasticity (Maze et al., 2010). G9a has been also shown to plays critical role in cell proliferation (Yang et al., 2012), senescence (Takahashi et al., 2012), DNA replication (Esteva et al., 2006; Yu et al., 2012), and in the establishment of proviral gene silencing (Leung et al., 2011).


EHMT2/G9a homologues have been found in various species like chimpanzee (99.7 % homology), cow (98.1% homology), rat (95.97% homology), C. elegans (25 % homology) and mouse (95.5% homology).



No mutations have been reported so far.


No mutations have been reported so far.

Implicated in

Entity name
Various cancers
EHMT2/G9a is overexpressed in various types of tumors, which include solid and haematological tumors (Cho et al., 2011). High-level expression of G9a in cancerous cells has been correlated with aggressiveness and poor prognosis in patients of lung, hepatocellular, ovarian, colon cancer and B cell chronic lymphocytic leukemia (Haung et al., 2010). Functionally, G9a has been linked to multiple cellular functions associated with tumor progression including proliferation, adhesion, migration, invasion, and cancer stem cell maintenance. Knockdown of G9a protein in cancer cells induces apoptosis suggesting that G9a plays a crucial role in cell cycle regulation of cancerous cells (Watanabe et al., 2008). Use of G9a-specific inhibitors, had been shown to significantly suppress the growth of cancerous cells, indicating that G9a enzymatic activity plays an important role in cancer development and growth (Cho et al., 2011). The following paragraphs summarize the discoveries on the functional role of G9a in various types of cancer development.
Entity name
Lung cancer
Lung cancer is a disease characterized by uncontrolled cell growth of lung tissue. G9a is highly expressed in aggressive lung cancer cells, and its elevated level has been correlated to poor prognosis with increase in cell migration, invasion and metastasis (Chen et al., 2010). G9a enhances the metastasis of lung cancer cells by repressing expression of the cell adhesion molecule Ep-CAM. High level of G9a in lung cancer cells promotes enrichment of DNA methylation and H3K9 dimethylation marks on Ep-CAM gene promoter region, leading to repression of this gene (Chen et al., 2010). Depletion of the G9a protein in lung cancer cells reduces the levels of H3K9 dimethylation and decreases recruitment of the transcriptional cofactors HP1, DNMT1, and HDAC1 to the Ep-CAM promoter, leading to de-repression of Ep-CAM gene and inhibition of cell migration and invasion (Chen et al., 2010).
Entity name
Breast cancer
Human breast cancer is a heterogeneous disease with respect to molecular alterations, incidence, survival, and response to therapy. Claudin-low breast cancer (CLBC) is characterized by the expression of markers of epithelial-mesenchymal transition (EMT), which has been linked with CLBC metastasis (Dong et al., 2012). G9a promotes EMT expression by repressing E-cadherin expression in CLBC models. G9a associates with Snail and recruits HP1 and DNA methyltransferases to the E-cadherin gene promoter for repression (Dong et al., 2012). Knockdown of G9a in CLBC models restores E-cadherin expression by suppressing H3K9me2 and DNA methylation, which results in inhibition of cell migration, invasion, suppression of tumor growth and metastasis (Dong et al., 2012).
Entity name
Prostate cancer
Prostate cancer is one of the most frequent cancers in men. G9a is coexpressed at high levels with Runx2, in metastatic prostate cancer cells and directly regulates the expression of several Runx2 target genes, which are important regulators of tumor growth, invasion and/or metastasis (Purcell at al., 2012). Downregulation of G9a in prostate cancer cells represses several RUNX2 target genes including, MMP9, CSF2, SDF1, CST7 and enhances the expression of others, such as MMP13 and PIP (Purcell et al., 2012). A study by Kondo et al., (2008) demonstrates that downregulation of G9a in prostate cancer cells, disrupts centrosome and chromosome stability, leading to inhibition of cancer cell growth. Another study by Yuan et al., (2012) demonstrates that treatment of pancreatic cancer cells with G9a inhibitor BRD4770 induces senescence and inhibits proliferation. Collectively, these studies reveal a potential oncogenic role of G9a in prostate cancer progression.
Entity name
Gastric cancer
G9a is involved in gastric cancer progression by inhibiting expression of the tumor suppressor gene RUNX3. In RUNX3 expressing gastric cell lines, hypoxia leads to upregulation of G9a, leading to the accumulation of H3K9me2 marks on RUNX3 promoter and repression of RUNX3 expression (Lee et al., 2009). Knocking down G9a in hypoxia-induced gastric cancer cells restores the expression of RUNX3 with suppression of gastric cancer progression (Lee et al., 2009).
Entity name
Bladder carcinomas
G9a expression is upregulated in human bladder carcinomas compared to non-neoplastic bladder tissues (Cho et al., 2011). Enhanced expression of G9a promotes the proliferation of bladder carcinomas cells by negatively regulating the tumor suppressor gene SIAH1 (Cho et al., 2011). G9a suppresses transcription of the SIAH1 gene by binding to its promoter followed by methylation of lysine 9 of histone H3. Downregulation of G9a activity by knock down or through the use of a G9a specific inhibitor, BIX-01294, significantly suppresses the growth of cancer cells by de-repressing the SIAH1 gene (Cho et al., 2011).
Entity name
Neuroendocrine tumors
Neuroendocrine tumors (NETs) are neoplasms that arise from cells of the endocrine and nervous systems. A study by Kim et al., (2013) has revealed altered expression of Wnt/β-catenin signaling components in neuroendocrine tumors. G9a contributes to the pathogenesis and growth of NETs by upregulating the expression of β-catenin. High level expression of G9a in neuroendocrine tumors downregulates the expression of specific β-catenin inhibitory genes inclusing DKK-1, DKK-2, and WIF-1, leading to overexpression of β-catenin, which in turn leads to increased cell proliferation and tumor growth (Kim et al., 2013). Use of the G9a inhibitor UNC0638 derepresses β-catenin inhibitory genes and suppresses Wnt/β-catenin induced cell proliferation, colony formation and tumor growth, demonstrating the oncogenic potential of G9a in NETs progression (Kim et al., 2013).
Entity name
Haematological malignancies
G9a is over expressed in haematological malignancies including AML and CML (Haung et al., 2010; Cho et al., 2011). The oncoprotein EVI-1 (ecotropic viral integration site-1) is aberrantly expressed in myeloid leukemias and has been linked to a poor patient survival rate. A study by Goyama et al., (2010) demonstrates that G9a interacts EVI-1 and contributes to EVI-1-mediated leukemogenesis. Depletion of G9a protein in EVI-1-expressing progenitors significantly reduces their colony-forming activity, indicating a possible role of G9a in generating leukemia-initiating cells by Evi-1 (Goyama et al., 2010).
JAK2 (Janus kinase 2) mediated phosphorylation plays a critical role during normal hematopoiesis and leukemogenesis. JAK2 induces leukemogenesis by activating the lmo2 leukemogenic gene through phosphorylation of histone H3Y41 and exclusion of HP1α from chromatin (Dawson et al., 2009). A recent study by Son et al., (2012) demonstrated that G9a negatively regulates the expression of JAK2 and favors ATRA-mediated leukemia cell differentiation. G9a mediated repression of JAK2, results in the downregulation of H3Y41 phosphorylation on the leukemogenic oncogene lmo2 promoter, indicating a role for G9a in JAK2-H3Y41P-HP1α transcriptional signaling during leukemogenesis (Son et al., 2012).


Pubmed IDLast YearTitleAuthors
192420952009The ZNF217 oncogene is a candidate organizer of repressive histone modifiers.Banck MS et al
231515072012G9a functions as a molecular scaffold for assembly of transcriptional coactivators on a subset of glucocorticoid receptor target genes.Bittencourt D et al
117077782001Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions.Brown SE et al
220863342011MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a.Chang Y et al
231121892012Maintenance of gene silencing by the coordinate action of the H3K9 methyltransferase G9a/KMT1C and the H3K4 demethylase Jarid1a/KDM5A.Chaturvedi CP et al
209404082010H3K9 histone methyltransferase G9a promotes lung cancer invasion and metastasis by silencing the cell adhesion molecule Ep-CAM.Chen MW et al
231050052012G9a/GLP-dependent histone H3K9me2 patterning during human hematopoietic stem cell lineage commitment.Chen X et al
179623122007Automethylation of G9a and its implication in wider substrate specificity and HP1 binding.Chin HG et al
218473592011Enhanced expression of EHMT2 is involved in the proliferation of cancer cells through negative regulation of SIAH1.Cho HS et al
201599952010A case study in cross-talk: the histone lysine methyltransferases G9a and GLP.Collins R et al
182641132008The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.Collins RE et al
165379072006PRISM/PRDM6, a transcriptional repressor that promotes the proliferative gene program in smooth muscle cells.Davis CA et al
197839802009JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin.Dawson MA et al
160868572005The SET-domain protein superfamily: protein lysine methyltransferases.Dillon SC et al
224065312012G9a interacts with Snail and is critical for Snail-mediated E-cadherin repression in human breast cancer.Dong C et al
188186932008DNA methylation in ES cells requires the lysine methyltransferase G9a but not its catalytic activity.Dong KB et al
162878492005Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of histone lysine methyltransferase G9a and histone deacetylase 1.Duan Z et al
189533372008De novo DNA methylation promoted by G9a prevents reprogramming of embryonically silenced genes.Epsztejn-Litman S et al
170854822006Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication.Estève PO et al
164158562006G9a-mediated irreversible epigenetic inactivation of Oct-3/4 during early embryogenesis.Feldman N et al
197767572010EVI-1 interacts with histone methyltransferases SUV39H1 and G9a for transcriptional repression and bone marrow immortalization.Goyama S et al
225143072012G9a/GLP histone lysine dimethyltransferase complex activity in the hippocampus and the entorhinal cortex is required for gene activation and silencing during memory consolidation.Gupta-Agarwal S et al
149857132004PRDI-BF1 recruits the histone H3 methyltransferase G9a in transcriptional silencing.Gyory I et al
201182332010G9a and Glp methylate lysine 373 in the tumor suppressor p53.Huang J et al
232232882012G9a histone methyltransferase activity in retinal progenitors is essential for proper differentiation and survival of mouse retinal cells.Katoh K et al
233543042013Deregulation of Wnt/β-catenin signaling through genetic or epigenetic alterations in human neuroendocrine tumors.Kim JT et al
184462232008Downregulation of histone H3 lysine 9 methyltransferase G9a induces centrosome disruption and chromosome instability in cancer cells.Kondo Y et al
172895932007Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase.Kubicek S et al
164617742006Histone H3 lysine 9 methyltransferase G9a is a transcriptional coactivator for nuclear receptors.Lee DY et al
188500072009Hypoxic silencing of tumor suppressor RUNX3 by histone modification in gastric cancer cells.Lee SH et al
204213882010Activating and inhibitory functions for the histone lysine methyltransferase G9a in T helper cell differentiation and function.Lehnertz B et al
214272302011Lysine methyltransferase G9a is required for de novo DNA methylation and the establishment, but not the maintenance, of proviral silencing.Leung DC et al
222156002012Lysine methyltransferase G9a methylates the transcription factor MyoD and regulates skeletal muscle differentiation.Ling BM et al
230872132012G9a mediates Sharp-1-dependent inhibition of skeletal muscle differentiation.Ling BM et al
200568912010Essential role of the histone methyltransferase G9a in cocaine-induced plasticity.Maze I et al
84572111993The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats.Milner CM et al
189888102008The Air noncoding RNA epigenetically silences transcription by targeting G9a to chromatin.Nagano T et al
233524532013A core chromatin remodeling factor instructs global chromatin signaling through multivalent reading of nucleosome codes.Nair SS et al
152693442004CCAAT displacement protein/cut homolog recruits G9a histone lysine methyltransferase to repress transcription.Nishio H et al
120041352002A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.Ogawa H et al
223890012012Recruitment of coregulator G9a by Runx2 for selective enhancement or suppression of transcription.Purcell DJ et al
184384032008Protein lysine methyltransferase G9a acts on non-histone targets.Rathert P et al
152009512004Localized domains of G9a-mediated histone methylation are required for silencing of neuronal genes.Roopra A et al
200058242009Control of cognition and adaptive behavior by the GLP/G9a epigenetic suppressor complex.Schaefer A et al
104311751999The ankyrin repeat: a diversity of interactions on a common structural framework.Sedgwick SG et al
232579132013G9a, a multipotent regulator of gene expression.Shankar SR et al
189839702008Induction of pluripotent stem cells from mouse embryonic fibroblasts by Oct4 and Klf4 with small-molecule compounds.Shi Y et al
214985672011H3K9 methyltransferase G9a and the related molecule GLP.Shinkai Y et al
228013672012Negative regulation of JAK2 by H3K9 methyltransferase G9a in leukemia.Son HJ et al
28134331989Human major histocompatibility complex contains a minimum of 19 genes between the complement cluster and HLA-B.Spies T et al
157676602005Relationship between histone H3 lysine 9 methylation, transcription repression, and heterochromatin protein 1 recruitment.Stewart MD et al
188186942008G9a/GLP complexes independently mediate H3K9 and DNA methylation to silence transcription.Tachibana M et al
221783962012DNA damage signaling triggers degradation of histone methyltransferases through APC/C(Cdh1) in senescent cells.Takahashi A et al
185664142008Functional analysis of histone methyltransferase g9a in B and T lymphocytes.Thomas LR et al
191446452009Dynamic Histone H1 Isotype 4 Methylation and Demethylation by Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji Domain-containing JMJD2/KDM4 Proteins.Trojer P et al
167022102006Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP.Ueda J et al
180398422008G9a histone methyltransferase contributes to imprinting in the mouse placenta.Wagschal A et al
226294372012The MSX1 homeoprotein recruits G9a methyltransferase to repressed target genes in myoblast cells.Wang J et al
231785912013Histone H3K9 methyltransferase G9a represses PPARγ expression and adipogenesis.Wang L et al
189806802008Deregulation of histone lysine methyltransferases contributes to oncogenic transformation of human bronchoepithelial cells.Watanabe H et al
203346382010Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D.Weiss T et al
191517162009Large histone H3 lysine 9 dimethylated chromatin blocks distinguish differentiated from embryonic stem cells.Wen B et al
210796502011Histone methyltransferase G9a contributes to H3K27 methylation in vivo.Wu H et al
227045172012Protein kinase A determines timing of early differentiation through epigenetic regulation with G9a.Yamamizu K et al
226911072012BIX-01294 treatment blocks cell proliferation, migration and contractility in ovine foetal pulmonary arterial smooth muscle cells.Yang Q et al
223870262012Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA.Yu Y et al
225369502012A small-molecule probe of the histone methyltransferase G9a induces cellular senescence in pancreatic adenocarcinoma.Yuan Y et al

Other Information

Locus ID:

NCBI: 10919
MIM: 604599
HGNC: 14129
Ensembl: ENSG00000204371


dbSNP: 10919
ClinVar: 10919
TCGA: ENSG00000204371


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
Lysine degradationKEGGko00310
Lysine degradationKEGGhsa00310
Gene ExpressionREACTOMER-HSA-74160
Generic Transcription PathwayREACTOMER-HSA-212436
Transcriptional Regulation by TP53REACTOMER-HSA-3700989
RNA Polymerase I, RNA Polymerase III, and Mitochondrial TranscriptionREACTOMER-HSA-504046
RNA Polymerase I TranscriptionREACTOMER-HSA-73864
RNA Polymerase I Promoter ClearanceREACTOMER-HSA-73854
RNA Polymerase I Transcription InitiationREACTOMER-HSA-73762
Epigenetic regulation of gene expressionREACTOMER-HSA-212165
Cellular responses to stressREACTOMER-HSA-2262752
Cellular SenescenceREACTOMER-HSA-2559583
Senescence-Associated Secretory Phenotype (SASP)REACTOMER-HSA-2559582
Chromatin organizationREACTOMER-HSA-4839726
Chromatin modifying enzymesREACTOMER-HSA-3247509
PKMTs methylate histone lysinesREACTOMER-HSA-3214841
Longevity regulating pathwayKEGGhsa04211
Positive epigenetic regulation of rRNA expressionREACTOMER-HSA-5250913
Regulation of TP53 ActivityREACTOMER-HSA-5633007
Regulation of TP53 Activity through MethylationREACTOMER-HSA-6804760
ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expressionREACTOMER-HSA-427389

Protein levels (Protein atlas)

Not detected


Entity IDNameTypeEvidenceAssociationPKPDPMIDs
PA164712499Antithyroid PreparationsChemicalClinicalAnnotationassociatedPD27157822


Pubmed IDYearTitleCitations
170854822006Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication.208
224065312012G9a interacts with Snail and is critical for Snail-mediated E-cadherin repression in human breast cancer.183
201182332010G9a and Glp methylate lysine 373 in the tumor suppressor p53.154
209404082010H3K9 histone methyltransferase G9a promotes lung cancer invasion and metastasis by silencing the cell adhesion molecule Ep-CAM.123
184462232008Downregulation of histone H3 lysine 9 methyltransferase G9a induces centrosome disruption and chromosome instability in cancer cells.94
203351632010Involvement of histone H3 lysine 9 (H3K9) methyltransferase G9a in the maintenance of HIV-1 latency and its reactivation by BIX01294.94
155906462005In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases.87
162878492005Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of histone lysine methyltransferase G9a and histone deacetylase 1.83
196901692009The NF-kappaB factor RelB and histone H3 lysine methyltransferase G9a directly interact to generate epigenetic silencing in endotoxin tolerance.83
243891032014The histone H3 lysine 9 methyltransferases G9a and GLP regulate polycomb repressive complex 2-mediated gene silencing.80


Chandra-Prakash Chaturvedi ; Marjorie Brand

EHMT2 (euchromatic histone-lysine N-methyltransferase 2)

Atlas Genet Cytogenet Oncol Haematol. 2013-07-01

Online version: