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SETD7 methylates TP53 on lysine. 8 / 8
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"C-terminal lysine residues of p53 are methylated in vivo at K370, K372, K373, and K382 by histone lysine methyl transferases, Smyd2, SET9, G9a/Glp, and Set8, respectively. xref – xref While K372 methylation by SET9 in human cells enhanced p53 transcriptional activities, the role of p53 methylation in the mouse by Set7/9 was controversial. xref – xref However, it should be pointed out that the results from mouse embryonic fibroblasts in the mouse study might be inappropriate to apply to human epithelial cells."

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"Indeed, histone lysine methyltransferases KMT5 (Set9), KMT3C (Smyd2), and KMT5A (Set8) methylate p53 at specific C-terminal lysines."

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"Mechanism of product specificity of AdoMet methylation catalyzed by lysine methyltransferases : transcriptional factor p53 methylation by histone lysine methyltransferase SET7/9."

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"For instance, lysine methylation of p53 by the SETD7 and the nuclear factor κB by the methyl transferase nuclear receptor-binding SET domain-containing protein 1 distinctly increase their ability to bind the promoter and activation of downstream genes [156, 158]."

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"We provide the first genetic evidence demonstrating that lysine methylation of p53 by Set7/9 is important for p53 activation in vivo and suggest a mechanistic link between methylation and acetylation of p53 through Tip60."

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"QPCR analysis also showed that Mll2 Gdf9 cKO oocytes overexpressed several apoptosis associated genes (XREF_TABLE), including p53 (transformation related protein 53; TRP53) and Setd7 (SET domain lysine methyltransferase 7, also know as Set7/9) (XREF_TABLE and XREF_SUPPLEMENTARY), which methylates p53 and prevents its degradation XREF_BIBR."

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"In 2004, Chuikov et al. found that K372 of p53 is mono-methylated by Set7/9 lysine methyltransferase [49]."

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"Originally defined as a critical layer of p53 regulation in human cell lines, p53 lysine methylation by Set7/9 (also called Setd7) was proposed to fulfill a similar function invivo in the mouse, promoting p53 acetylation, stabilization, and activation upon DNA damage (Kurash etal., 2008)."