SET domain containing lysine methyltransferase 7 (SETD7)

SET domain containing lysine methyltransferase 7 (SETD7, also known as SET7 or SET7/9) is a protein lysine methyltransferase that catalyzes the monomethylation of specific lysine residues on histone and non-histone proteins[1][4][10]. SETD7 contains a conserved SET domain, which transfers a methyl group from the cofactor S-adenosylmethionine (SAM) to lysine residues, most notably lysine 4 of histone H3 (H3K4)[1][10][2]. This modification is a key epigenetic mark associated with transcriptional activation, affecting chromatin structure and gene expression. In addition to histones, SETD7 also methylates important transcription factors and regulatory proteins such as p53, TAF10, E2F1, and others, affecting their stability, localization, and activity[1][4][10]. The enzyme is involved in diverse cellular processes, including the cell cycle, DNA damage response, and cell differentiation. Dysregulation of SETD7 activity is implicated in the pathogenesis of cancers and other diseases, and SETD7 is being explored as a potential therapeutic target, with experimental inhibitors like (R)-PFI-2 demonstrating selective inhibition of its methyltransferase activity[1][13].

Other names

SET7SET7/9KIAA1717SET domain containing 7Histone lysine methyltransferase SETD7SET9

Inhibitors block the methyltransferase activity of SETD7 by occupying the substrate lysine-binding site, preventing methyl transfer to lysine residues on histone or non-histone proteins[1][13].