Aliases for EHMT2 Gene
External Ids for EHMT2 Gene
Previous HGNC Symbols for EHMT2 Gene
Previous GeneCards Identifiers for EHMT2 Gene
This gene encodes a methyltransferase that methylates lysine residues of histone H3. Methylation of H3 at lysine 9 by this protein results in recruitment of additional epigenetic regulators and repression of transcription. This gene was initially thought to be two different genes, NG36 and G9a, adjacent to each other in the HLA locus. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]
GeneCards Summary for EHMT2 Gene
EHMT2 (Euchromatic Histone Lysine Methyltransferase 2) is a Protein Coding gene. Among its related pathways are Gene Expression and Cellular Senescence (REACTOME). Gene Ontology (GO) annotations related to this gene include p53 binding and C2H2 zinc finger domain binding. An important paralog of this gene is EHMT1.
UniProtKB/Swiss-Prot for EHMT2 Gene
Histone methyltransferase that specifically mono- and dimethylates Lys-9 of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of Lys-56 of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates Lys-27 of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of Lys-373 of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.
Lysine methyltransferases are enyzmes that catalyze the transfer of methyl groups from S-adenosylmethionine (SAM) to the lysine residues on histones, particularly histones H3 and H4. The dysregulation of this methylation is critical in the development of cancer.