Fig. 1: Histone H3 N-terminal arginine mutations are prevalent in cancer. | Nature Communications

Fig. 1: Histone H3 N-terminal arginine mutations are prevalent in cancer.

From: Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation

Fig. 1

Using data from a published dataset of cancer-associated histone mutations18, A the frequency of mutations (y-axis) in histone H3 is plotted for each amino acid in the protein (x-axis) ranked by increasing frequency of mutations or B by sequence position with the single letter amino acid sequence of H3.1 noted (only positions 1–43 are shown). Blue indicates classical oncohistones. Red indicates H3 N-terminal arginine residues of interest. Selected sites of histone post-translational modifications64 are denoted (Me methyl, Cit citrullination, Ac acetylation, Cr crotonylation, Bu butyrylation, Ub ubiquitination).

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