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Our lab demonstrated that trimethylation of lysine 27 on histone 3 (H3K27me3), a repressive epigenetic mark, is depleted and trimethylation of lysine 4 on histone 3 (H3K4me3), an activating histone modification, is enriched at cardiac promoters early in GMT cocktail reprogramming and is accompanied by a rapid increase in cardiac gene mRNA expression (Liu et al., 2016a).

This modification is enriched around the promoters and 5′ ends of actively transcribed genes.

H3K36me3 modification is enriched in the body of expressed genes (Bannister et al., 2005; Barski et al., 2007).

This modification is enriched at distal regulatory elements in ESCs, whereas it is enriched at the 5mC-depleted gene bodies of neuronal function-related genes.

H3K79me3 is associated with actively transcribed genes but Barski et al. found this modification is enriched at some silent genes [ 9, 18, 19].

If a particular modification is enriched to an equal degree at developmentally expressed and repressed imprinted genes, it is likely that this modification is not associated with developmental regulation, but rather with imprinting.

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It has been reported that membrane proteins with at least one transmembrane domain or with a hydrophobic modification are enriched in lipid rafts [13].

The modification was enriched at promoter regions, and particularly in linker regions between adjacent nucleosomes.

This modification was enriched in macronuclei (a3) and anlagen (a3), and antibodies reacted exclusively with a 15 kDa band.

We also ascertained that the genes belonging to the heat-shock response, DNA repair, translation, and protein modification were enriched in the heteroclite mutants.

In our study, the GO-slim term 'protein modification' was enriched in fast evolving genes, and contained many sub-terms including the regulation of Ser/Thr signaling, effects on translation, and post-translational modifications enabling actual protein function.

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