PHD finger protein 20 (PHF20)

PHD finger protein 20 (PHF20) is a multidomain, chromatin-associated protein that acts as a methyllysine effector, binding specifically to methylated lysine residues on histones and non-histone proteins. PHF20 contains multiple domains, including Tudor, PHD finger, MBT, and AT-hook, enabling it to recognize diverse epigenetic marks. It is a component of the MOF-NSL histone acetyltransferase complex, involved in the acetylation of histone H4 and regulation of gene expression via chromatin remodeling. PHF20 is critical for the stabilization and activation of the tumor suppressor protein p53 in response to DNA damage, enhancing p53’s effects on cell cycle arrest, apoptosis, and DNA repair. It also directly interacts with and regulates the transcription factor Runx2 to promote osteoblast differentiation, with knockout models indicating essential roles in normal skeletal development. In addition, PHF20 acts as an epigenetic reader, influencing genes related to autophagy and other pathways. PHF20 is associated with certain cancer antigens and may be dysregulated in malignancies, implicating a potential role as a tumor biomarker. No drugs targeting PHF20 are currently reported, but its central epigenetic regulatory roles make it a protein of therapeutic interest in cancer and developmental disorders.

Other names

C20orf104GLEA2HCA58NZFTZPdJ1121G12.1TDRD20AGlioma-expressed antigen 2Hepatocellular carcinoma-associated antigen 58Novel zinc finger proteinTranscription factor TZPtudor domain containing 20A