Histone-lysine N-methyltransferase SETD7 (SETD7)

Histone-lysine N-methyltransferase SETD7 (SETD7, also known as KMT7, SET7, SET9, or SET7/9) is a SET domain-containing lysine methyltransferase enzyme that primarily monomethylates lysine residues on both histone (notably H3K4) and non-histone proteins. By depositing methyl marks, SETD7 modulates chromatin structure and transcription, impacting cell cycle, apoptosis, proliferation, differentiation, and DNA damage response. While initially identified as a transcriptional activator through H3K4 methylation, SETD7 also methylates important non-histone proteins such as p53, the estrogen receptor, FOXA1, E2F1, Rb, and others, thereby regulating diverse cellular functions. Its biological roles are highly context dependent: SETD7 may function as a tumor suppressor or oncogene depending on the cellular and tissue environment, and is implicated in the development and progression of several cancers (including prostate, breast, liver, and gastrointestinal malignancies), as well as in cardiac function and other diseases. SETD7 is considered a valid therapeutic target for small-molecule inhibitors in research settings, but is currently not targeted by any approved drugs. Modulation of its activity may serve as a biomarker for disease prognosis and outcome, but also raises safety concerns related to the broad roles of epigenetic regulation in normal and disease physiology

Other names

SETD7KMT7SET7SET7/9SET9SET domain containing lysine methyltransferase 7SET domain containing 7Histone lysine methyltransferase

Inhibition of methyltransferase activity (prevents mono-methylation of target lysines on histone and non-histone proteins); Interference with Epigenetic regulation (alters transcriptional activation/repression by preventing methyl mark deposition); Modulation of transcription factor activity (for example, affects stability/activity of p53, estrogen receptor, FOXA1, etc.)