EHMT1
[7] Another important functional domain, which G9A and GLP both share, is a region containing ankryin repeats, which is involved in protein-protein interactions.[7] Therefore, the G9A/GLP complex can both methylate histone tails and bind to mono- and di-methylated H3K9 to recruit molecules, such as DNA methyltransferases, to the chromatin.[10][7] H3K9me2 is a reversible modification and can be removed by a wide range of histone lysine demethylases (KDMs) including KDM1, KDM3, KDM4 and KDM7 family members.[7][11][12] In addition to their role as histone lysine methyltransferases (HMTs), several studies have shown that G9A/GLP are also able to methylate a wide range of non-histone proteins.[13] However, as most of the reported methylation sites have been derived from mass spectrometry analyses, the function of many of these modifications remain unknown.