| Description | This is a cysteine-rich region (CRR) found in the centre of these sequences, which is unique to EHTM1/2 and mediates protein-protein interactions and recruitment of the methyltransferases to specific sites in chromatin [ ]. This domain adopts an unusual compact fold with four bound zinc atoms that contains an embedded RING domain, which represents a novel zinc-binding motif.This entry includes Histone-lysine N-methyltransferase EHMT1 and Histone-lysine N-methyltransferase EHMT2 ( ). EHMT1 and EHMT2 mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin [ ]. H3K9me is a specific tag for repression of epigenetic transcription, recruiting HP1 proteins to methylated histones. EHMT1 also methylates 'Lys-27' of histone H3 (H3K27me), but weakly [], while EHMT2 also monomethylates 'Lys-56' of histone H3 (H3K56me1) during the G1 phase of the cell cycle [], and methylates 'Lys-27' of histone H3 (H3K27me) []. EHMT1 and EHMT2 also dimethylate other proteins, including 'Lys-373' of p53 [, ].EHMT1 forms a heterodimer with EHMT2 [ ], and is a component of the E2F6.com-1 complex in G0 phase []. EHMT1 and EHMT2 contain ankyrin repeats (eight and seven ankyrin repeats, respectively), which bind the monomethylated RELA subunit of NF-kappa-B, a SET domain which interacts with WIZ [], and a pre-SET domain that binds three zinc ions via cysteine residues []. | Name | EHMT1/2, cysteine-rich region |
| Short Name | EHMT_CRR | Type | Domain |
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