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EHMT2 (euchromatic histone-lysine N-methyltransferase 2)

Written2013-07Chandra-Prakash Chaturvedi, Marjorie Brand
The Sprott Center for Stem Cell Research, Regenerative Medicine Program, Ottawa Hospital Research Institute, Ottawa, ON K1H 8L6, Canada (CPC, MB); University of Ottawa, Department of Cellular, Molecular Medicine, University of Ottawa, ON K1H 8L6, Canada (MB)

(Note : for Links provided by Atlas : click)

Identity

Alias_namesC6orf30
BAT8
chromosome 6 open reading frame 30
HLA-B associated transcript 8
Alias_symbol (synonym)G9A
Em:AF134726.3
NG36/G9a
KMT1C
Other aliasGAT8
NG36
HGNC (Hugo) EHMT2
LocusID (NCBI) 10919
Atlas_Id 51148
Location 6p21.33  [Link to chromosome band 6p21]
Location_base_pair Starts at 31879760 and ends at 31897206 bp from pter ( according to hg19-Feb_2009)  [Mapping EHMT2.png]
Local_order HSPA1A - HSPA1B - NEU1 - SLC44A4 - EHMT2 - C2 - ZBTB12.
 
  Genomic location of EHMT2/G9a gene along with adjustment genes on chromosome 6 (minus strand).
Fusion genes
(updated 2016)
EHMT2 (6p21.33) / ACLY (17q21.2)EHMT2 (6p21.33) / KRT18 (12q13.13)EHMT2 (6p21.33) / MSL2 (3q22.3)
MAST3 (19p13.11) / EHMT2 (6p21.33)VARS (6p21.33) / EHMT2 (6p21.33)

DNA/RNA

 
  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 (5'UTR, exons and 3'UTR are not drawn to scale). The shorter EHMT2 isoform b has missing exon 10 compared to full length EHMT2.
Description 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.
Transcription 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).
Pseudogene There is no known pseudogene for EHMT2/G9a.

Protein

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

Mutations

Germinal No mutations have been reported so far.
Somatic No mutations have been reported so far.

Implicated in

Note
  
Entity Various cancers
Note 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 Lung cancer
Note 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 Breast cancer
Note 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 Prostate cancer
Note 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 Gastric cancer
Note 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 Bladder carcinomas
Note 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 Neuroendocrine tumors
Note 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 Haematological malignancies
Note 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).
  

Breakpoints

Note No variables are reported for EHMT2/G9a gene so far.

To be noted

In summary, dysregulation of EHMT2/G9a is emerging as an important player in the pathobiology of various forms of cancer suggesting that G9a could serve as a promising therapeutic target for future treatments notably through the use of specific chemical inhibitors. For example, BIX-01294; a specific inhibitor of G9a methyltransferase activity has been shown to effectively suppress the growth of cancer cells (Cho et al., 2011). Another G9a inhibitor, BRD4770 induces senescence and inhibits proliferation of cancer cells (Yuan et al., 2012). Finally, a third G9a inhibitor UNC0638 showed similar results as BIX-01294 and BRD4770 and inhibits cell proliferation, colony formation and tumor growth (Kim et al., 2013). It will be interesting to test the effectiveness of these inhibitors in vivo. Further studies are required for better understanding of the molecular mechanism of G9a mediated positive and negative gene regulatory role in cancer development and for developing efficient therapy.

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Lysine methyltransferase G9a methylates the transcription factor MyoD and regulates skeletal muscle differentiation.
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Proc Natl Acad Sci U S A. 2012a Jan 17;109(3):841-6. doi: 10.1073/pnas.1111628109. Epub 2012 Jan 3.
PMID 22215600
 
G9a mediates Sharp-1-dependent inhibition of skeletal muscle differentiation.
Ling BM, Gopinadhan S, Kok WK, Shankar SR, Gopal P, Bharathy N, Wang Y, Taneja R.
Mol Biol Cell. 2012b Dec;23(24):4778-85. doi: 10.1091/mbc.E12-04-0311. Epub 2012 Oct 19.
PMID 23087213
 
Essential role of the histone methyltransferase G9a in cocaine-induced plasticity.
Maze I, Covington HE 3rd, Dietz DM, LaPlant Q, Renthal W, Russo SJ, Mechanic M, Mouzon E, Neve RL, Haggarty SJ, Ren Y, Sampath SC, Hurd YL, Greengard P, Tarakhovsky A, Schaefer A, Nestler EJ.
Science. 2010 Jan 8;327(5962):213-6. doi: 10.1126/science.1179438.
PMID 20056891
 
The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats.
Milner CM, Campbell RD.
Biochem J. 1993 Mar 15;290 ( Pt 3):811-8.
PMID 8457211
 
The Air noncoding RNA epigenetically silences transcription by targeting G9a to chromatin.
Nagano T, Mitchell JA, Sanz LA, Pauler FM, Ferguson-Smith AC, Feil R, Fraser P.
Science. 2008 Dec 12;322(5908):1717-20. doi: 10.1126/science.1163802. Epub 2008 Nov 6.
PMID 18988810
 
A core chromatin remodeling factor instructs global chromatin signaling through multivalent reading of nucleosome codes.
Nair SS, Li DQ, Kumar R.
Mol Cell. 2013 Feb 21;49(4):704-18. doi: 10.1016/j.molcel.2012.12.016. Epub 2013 Jan 24.
PMID 23352453
 
CCAAT displacement protein/cut homolog recruits G9a histone lysine methyltransferase to repress transcription.
Nishio H, Walsh MJ.
Proc Natl Acad Sci U S A. 2004 Aug 3;101(31):11257-62. Epub 2004 Jul 21.
PMID 15269344
 
A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.
Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y.
Science. 2002 May 10;296(5570):1132-6.
PMID 12004135
 
Recruitment of coregulator G9a by Runx2 for selective enhancement or suppression of transcription.
Purcell DJ, Khalid O, Ou CY, Little GH, Frenkel B, Baniwal SK, Stallcup MR.
J Cell Biochem. 2012 Jul;113(7):2406-14. doi: 10.1002/jcb.24114.
PMID 22389001
 
Protein lysine methyltransferase G9a acts on non-histone targets.
Rathert P, Dhayalan A, Murakami M, Zhang X, Tamas R, Jurkowska R, Komatsu Y, Shinkai Y, Cheng X, Jeltsch A.
Nat Chem Biol. 2008 Jun;4(6):344-6. doi: 10.1038/nchembio.88. Epub 2008 Apr 27.
PMID 18438403
 
Localized domains of G9a-mediated histone methylation are required for silencing of neuronal genes.
Roopra A, Qazi R, Schoenike B, Daley TJ, Morrison JF.
Mol Cell. 2004 Jun 18;14(6):727-38.
PMID 15200951
 
Control of cognition and adaptive behavior by the GLP/G9a epigenetic suppressor complex.
Schaefer A, Sampath SC, Intrator A, Min A, Gertler TS, Surmeier DJ, Tarakhovsky A, Greengard P.
Neuron. 2009 Dec 10;64(5):678-91. doi: 10.1016/j.neuron.2009.11.019.
PMID 20005824
 
The ankyrin repeat: a diversity of interactions on a common structural framework.
Sedgwick SG, Smerdon SJ.
Trends Biochem Sci. 1999 Aug;24(8):311-6. (REVIEW)
PMID 10431175
 
G9a, a multipotent regulator of gene expression.
Shankar SR, Bahirvani AG, Rao VK, Bharathy N, Ow JR, Taneja R.
Epigenetics. 2013 Jan;8(1):16-22. doi: 10.4161/epi.23331. Epub 2012 Dec 20. (REVIEW)
PMID 23257913
 
Induction of pluripotent stem cells from mouse embryonic fibroblasts by Oct4 and Klf4 with small-molecule compounds.
Shi Y, Desponts C, Do JT, Hahm HS, Scholer HR, Ding S.
Cell Stem Cell. 2008 Nov 6;3(5):568-74. doi: 10.1016/j.stem.2008.10.004.
PMID 18983970
 
H3K9 methyltransferase G9a and the related molecule GLP.
Shinkai Y, Tachibana M.
Genes Dev. 2011 Apr 15;25(8):781-8. doi: 10.1101/gad.2027411. (REVIEW)
PMID 21498567
 
Negative regulation of JAK2 by H3K9 methyltransferase G9a in leukemia.
Son HJ, Kim JY, Hahn Y, Seo SB.
Mol Cell Biol. 2012 Sep;32(18):3681-94. doi: 10.1128/MCB.00673-12. Epub 2012 Jul 16.
PMID 22801367
 
Human major histocompatibility complex contains a minimum of 19 genes between the complement cluster and HLA-B.
Spies T, Bresnahan M, Strominger JL.
Proc Natl Acad Sci U S A. 1989 Nov;86(22):8955-8.
PMID 2813433
 
Relationship between histone H3 lysine 9 methylation, transcription repression, and heterochromatin protein 1 recruitment.
Stewart MD, Li J, Wong J.
Mol Cell Biol. 2005 Apr;25(7):2525-38.
PMID 15767660
 
G9a/GLP complexes independently mediate H3K9 and DNA methylation to silence transcription.
Tachibana M, Matsumura Y, Fukuda M, Kimura H, Shinkai Y.
EMBO J. 2008 Oct 22;27(20):2681-90. doi: 10.1038/emboj.2008.192. Epub 2008 Sep 25.
PMID 18818694
 
DNA damage signaling triggers degradation of histone methyltransferases through APC/C(Cdh1) in senescent cells.
Takahashi A, Imai Y, Yamakoshi K, Kuninaka S, Ohtani N, Yoshimoto S, Hori S, Tachibana M, Anderton E, Takeuchi T, Shinkai Y, Peters G, Saya H, Hara E.
Mol Cell. 2012 Jan 13;45(1):123-31. doi: 10.1016/j.molcel.2011.10.018. Epub 2011 Dec 15.
PMID 22178396
 
Functional analysis of histone methyltransferase g9a in B and T lymphocytes.
Thomas LR, Miyashita H, Cobb RM, Pierce S, Tachibana M, Hobeika E, Reth M, Shinkai Y, Oltz EM.
J Immunol. 2008 Jul 1;181(1):485-93.
PMID 18566414
 
Dynamic Histone H1 Isotype 4 Methylation and Demethylation by Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji Domain-containing JMJD2/KDM4 Proteins.
Trojer P, Zhang J, Yonezawa M, Schmidt A, Zheng H, Jenuwein T, Reinberg D.
J Biol Chem. 2009 Mar 27;284(13):8395-405. doi: 10.1074/jbc.M807818200. Epub 2009 Jan 13.
PMID 19144645
 
Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP.
Ueda J, Tachibana M, Ikura T, Shinkai Y.
J Biol Chem. 2006 Jul 21;281(29):20120-8. Epub 2006 May 15.
PMID 16702210
 
G9a histone methyltransferase contributes to imprinting in the mouse placenta.
Wagschal A, Sutherland HG, Woodfine K, Henckel A, Chebli K, Schulz R, Oakey RJ, Bickmore WA, Feil R.
Mol Cell Biol. 2008 Feb;28(3):1104-13. Epub 2007 Nov 26.
PMID 18039842
 
The MSX1 homeoprotein recruits G9a methyltransferase to repressed target genes in myoblast cells.
Wang J, Abate-Shen C.
PLoS One. 2012;7(5):e37647. doi: 10.1371/journal.pone.0037647. Epub 2012 May 22.
PMID 22629437
 
Histone H3K9 methyltransferase G9a represses PPARγ expression and adipogenesis.
Wang L, Xu S, Lee JE, Baldridge A, Grullon S, Peng W, Ge K.
EMBO J. 2013 Jan 9;32(1):45-59. doi: 10.1038/emboj.2012.306. Epub 2012 Nov 23.
PMID 23178591
 
Deregulation of histone lysine methyltransferases contributes to oncogenic transformation of human bronchoepithelial cells.
Watanabe H, Soejima K, Yasuda H, Kawada I, Nakachi I, Yoda S, Naoki K, Ishizaka A.
Cancer Cell Int. 2008 Nov 3;8:15. doi: 10.1186/1475-2867-8-15.
PMID 18980680
 
Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D.
Weiss T, Hergeth S, Zeissler U, Izzo A, Tropberger P, Zee BM, Dundr M, Garcia BA, Daujat S, Schneider R.
Epigenetics Chromatin. 2010 Mar 24;3(1):7. doi: 10.1186/1756-8935-3-7.
PMID 20334638
 
Large histone H3 lysine 9 dimethylated chromatin blocks distinguish differentiated from embryonic stem cells.
Wen B, Wu H, Shinkai Y, Irizarry RA, Feinberg AP.
Nat Genet. 2009 Feb;41(2):246-50. doi: 10.1038/ng.297. Epub 2009 Jan 18.
PMID 19151716
 
Histone methyltransferase G9a contributes to H3K27 methylation in vivo.
Wu H, Chen X, Xiong J, Li Y, Li H, Ding X, Liu S, Chen S, Gao S, Zhu B.
Cell Res. 2011 Feb;21(2):365-7. doi: 10.1038/cr.2010.157. Epub 2010 Nov 16.
PMID 21079650
 
Protein kinase A determines timing of early differentiation through epigenetic regulation with G9a.
Yamamizu K, Fujihara M, Tachibana M, Katayama S, Takahashi A, Hara E, Imai H, Shinkai Y, Yamashita JK.
Cell Stem Cell. 2012 Jun 14;10(6):759-70. doi: 10.1016/j.stem.2012.02.022.
PMID 22704517
 
BIX-01294 treatment blocks cell proliferation, migration and contractility in ovine foetal pulmonary arterial smooth muscle cells.
Yang Q, Lu Z, Singh D, Raj JU.
Cell Prolif. 2012 Aug;45(4):335-44. doi: 10.1111/j.1365-2184.2012.00828.x. Epub 2012 Jun 13.
PMID 22691107
 
Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA.
Yu Y, Song C, Zhang Q, DiMaggio PA, Garcia BA, York A, Carey MF, Grunstein M.
Mol Cell. 2012 Apr 13;46(1):7-17. doi: 10.1016/j.molcel.2012.01.019. Epub 2012 Mar 1.
PMID 22387026
 
A small-molecule probe of the histone methyltransferase G9a induces cellular senescence in pancreatic adenocarcinoma.
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Citation

This paper should be referenced as such :
Chaturvedi, CP ; Brand, M
EHMT2 (euchromatic histone-lysine N-methyltransferase 2)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(1):38-45.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/EHMT2ID51148ch6p21.html


External links

Nomenclature
HGNC (Hugo)EHMT2   14129
Cards
AtlasEHMT2ID51148ch6p21
Entrez_Gene (NCBI)EHMT2  10919  euchromatic histone lysine methyltransferase 2
AliasesBAT8; C6orf30; G9A; GAT8; 
KMT1C; NG36
GeneCards (Weizmann)EHMT2
Ensembl hg19 (Hinxton)ENSG00000204371 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000204371 [Gene_View]  chr6:31879760-31897206 [Contig_View]  EHMT2 [Vega]
ICGC DataPortalENSG00000204371
TCGA cBioPortalEHMT2
AceView (NCBI)EHMT2
Genatlas (Paris)EHMT2
WikiGenes10919
SOURCE (Princeton)EHMT2
Genetics Home Reference (NIH)EHMT2
Genomic and cartography
GoldenPath hg38 (UCSC)EHMT2  -     chr6:31879760-31897206 -  6p21.33   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)EHMT2  -     6p21.33   [Description]    (hg19-Feb_2009)
EnsemblEHMT2 - 6p21.33 [CytoView hg19]  EHMT2 - 6p21.33 [CytoView hg38]
Mapping of homologs : NCBIEHMT2 [Mapview hg19]  EHMT2 [Mapview hg38]
OMIM604599   
Gene and transcription
Genbank (Entrez)AB209433 AJ315532 AK056936 AK092866 AK302904
RefSeq transcript (Entrez)NM_001289413 NM_001318833 NM_006709 NM_025256
RefSeq genomic (Entrez)NC_000006 NC_018917 NT_113891 NT_167244 NT_167245 NT_167247 NT_167248 NT_167249
Consensus coding sequences : CCDS (NCBI)EHMT2
Cluster EST : UnigeneHs.709218 [ NCBI ]
CGAP (NCI)Hs.709218
Alternative Splicing GalleryENSG00000204371
Gene ExpressionEHMT2 [ NCBI-GEO ]   EHMT2 [ EBI - ARRAY_EXPRESS ]   EHMT2 [ SEEK ]   EHMT2 [ MEM ]
Gene Expression Viewer (FireBrowse)EHMT2 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10919
GTEX Portal (Tissue expression)EHMT2
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ96KQ7   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ96KQ7  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ96KQ7
Splice isoforms : SwissVarQ96KQ7
Catalytic activity : Enzyme2.1.1.- [ Enzyme-Expasy ]   2.1.1.-2.1.1.- [ IntEnz-EBI ]   2.1.1.- [ BRENDA ]   2.1.1.- [ KEGG ]   
PhosPhoSitePlusQ96KQ7
Domaine pattern : Prosite (Expaxy)ANK_REP_REGION (PS50297)    ANK_REPEAT (PS50088)    PRE_SET (PS50867)    SET (PS50280)   
Domains : Interpro (EBI)Ankyrin_rpt    Ankyrin_rpt-contain_dom    Pre-SET_dom    SET_dom   
Domain families : Pfam (Sanger)Ank_2 (PF12796)    Pre-SET (PF05033)    SET (PF00856)   
Domain families : Pfam (NCBI)pfam12796    pfam05033    pfam00856   
Domain families : Smart (EMBL)ANK (SM00248)  PreSET (SM00468)  SET (SM00317)  
Conserved Domain (NCBI)EHMT2
DMDM Disease mutations10919
Blocks (Seattle)EHMT2
PDB (SRS)2O8J    3DM1    3K5K    3RJW    4NVQ    5JHN    5JIN    5JIY    5JJ0    5T0K    5T0M    5TTF   
PDB (PDBSum)2O8J    3DM1    3K5K    3RJW    4NVQ    5JHN    5JIN    5JIY    5JJ0    5T0K    5T0M    5TTF   
PDB (IMB)2O8J    3DM1    3K5K    3RJW    4NVQ    5JHN    5JIN    5JIY    5JJ0    5T0K    5T0M    5TTF   
PDB (RSDB)2O8J    3DM1    3K5K    3RJW    4NVQ    5JHN    5JIN    5JIY    5JJ0    5T0K    5T0M    5TTF   
Structural Biology KnowledgeBase2O8J    3DM1    3K5K    3RJW    4NVQ    5JHN    5JIN    5JIY    5JJ0    5T0K    5T0M    5TTF   
SCOP (Structural Classification of Proteins)2O8J    3DM1    3K5K    3RJW    4NVQ    5JHN    5JIN    5JIY    5JJ0    5T0K    5T0M    5TTF   
CATH (Classification of proteins structures)2O8J    3DM1    3K5K    3RJW    4NVQ    5JHN    5JIN    5JIY    5JJ0    5T0K    5T0M    5TTF   
SuperfamilyQ96KQ7
Human Protein AtlasENSG00000204371
Peptide AtlasQ96KQ7
HPRD06854
IPIIPI00096972   IPI00220795   IPI00220796   IPI00939492   IPI00797257   IPI00788863   IPI00892976   IPI00892914   IPI00892814   IPI00892722   IPI00893814   IPI00640176   
Protein Interaction databases
DIP (DOE-UCLA)Q96KQ7
IntAct (EBI)Q96KQ7
FunCoupENSG00000204371
BioGRIDEHMT2
STRING (EMBL)EHMT2
ZODIACEHMT2
Ontologies - Pathways
QuickGOQ96KQ7
Ontology : AmiGOnegative regulation of transcription from RNA polymerase II promoter  nuclear chromatin  p53 binding  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  regulation of DNA replication  DNA methylation  zinc ion binding  cellular response to starvation  protein-lysine N-methyltransferase activity  histone methylation  nuclear speck  histone-lysine N-methyltransferase activity  histone-lysine N-methyltransferase activity  peptidyl-lysine dimethylation  histone lysine methylation  histone methyltransferase activity (H3-K9 specific)  histone methyltransferase activity (H3-K27 specific)  histone H3-K9 methylation  histone H3-K27 methylation  C2H2 zinc finger domain binding  regulation of signal transduction by p53 class mediator  promoter-specific chromatin binding  
Ontology : EGO-EBInegative regulation of transcription from RNA polymerase II promoter  nuclear chromatin  p53 binding  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  regulation of DNA replication  DNA methylation  zinc ion binding  cellular response to starvation  protein-lysine N-methyltransferase activity  histone methylation  nuclear speck  histone-lysine N-methyltransferase activity  histone-lysine N-methyltransferase activity  peptidyl-lysine dimethylation  histone lysine methylation  histone methyltransferase activity (H3-K9 specific)  histone methyltransferase activity (H3-K27 specific)  histone H3-K9 methylation  histone H3-K27 methylation  C2H2 zinc finger domain binding  regulation of signal transduction by p53 class mediator  promoter-specific chromatin binding  
Pathways : KEGGLysine degradation   
REACTOMEQ96KQ7 [protein]
REACTOME PathwaysR-HSA-73762 [pathway]   
NDEx NetworkEHMT2
Atlas of Cancer Signalling NetworkEHMT2
Wikipedia pathwaysEHMT2
Orthology - Evolution
OrthoDB10919
GeneTree (enSembl)ENSG00000204371
Phylogenetic Trees/Animal Genes : TreeFamEHMT2
HOVERGENQ96KQ7
HOGENOMQ96KQ7
Homologs : HomoloGeneEHMT2
Homology/Alignments : Family Browser (UCSC)EHMT2
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerEHMT2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)EHMT2
dbVarEHMT2
ClinVarEHMT2
1000_GenomesEHMT2 
Exome Variant ServerEHMT2
ExAC (Exome Aggregation Consortium)EHMT2 (select the gene name)
Genetic variants : HAPMAP10919
Genomic Variants (DGV)EHMT2 [DGVbeta]
DECIPHEREHMT2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisEHMT2 
Mutations
ICGC Data PortalEHMT2 
TCGA Data PortalEHMT2 
Broad Tumor PortalEHMT2
OASIS PortalEHMT2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICEHMT2  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDEHMT2
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch EHMT2
DgiDB (Drug Gene Interaction Database)EHMT2
DoCM (Curated mutations)EHMT2 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)EHMT2 (select a term)
intoGenEHMT2
NCG5 (London)EHMT2
Cancer3DEHMT2(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM604599   
Orphanet
MedgenEHMT2
Genetic Testing Registry EHMT2
NextProtQ96KQ7 [Medical]
TSGene10919
GENETestsEHMT2
Target ValidationEHMT2
Huge Navigator EHMT2 [HugePedia]
snp3D : Map Gene to Disease10919
BioCentury BCIQEHMT2
ClinGenEHMT2
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD10919
Chemical/Pharm GKB GenePA25267
Clinical trialEHMT2
Miscellaneous
canSAR (ICR)EHMT2 (select the gene name)
Probes
Litterature
PubMed163 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineEHMT2
EVEXEHMT2
GoPubMedEHMT2
iHOPEHMT2
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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