PHD finger protein 20-like protein 1 (PHF20L1)

PHD finger protein 20-like protein 1 (PHF20L1) is an epigenetic reader protein belonging to a family of Tudor domain–containing proteins that recognize methylated lysine residues on histones and non-histone proteins. PHF20L1 is a component of the nonspecific lethal (NSL) complex and interacts with other chromatin-modifying protein complexes, including the MOF acetyltransferase complex and transcriptional repressor complexes such as PRC2 and NuRD[1][3][5]. It binds monomethylated lysine residues in histones H3 and H4 and in proteins such as DNMT1 and the retinoblastoma tumor suppressor (pRb), influencing gene expression, cell cycle control, and DNA damage response[1][5]. PHF20L1 acts primarily as a transcriptional repressor by reading secondary histone methylation marks (notably H3K27me2) and recruiting repressor complexes, thereby modulating chromatin state and gene activity[3]. Aberrant expression or genetic alterations of PHF20L1 are associated with several cancer types and may affect developmental processes[1][5]. PHF20L1 is currently being explored as a potential "undruggable" epigenetic target, with structural analyses suggesting that its Tudor domain could be inhibited by rationally designed small molecules[2].

Other names

CGI-72FLJ13649FLJ21615MGC64923TDRD20Btudor domain containing 20Btudor domain-containing protein PHF20L1up-regulated in lung cancer 1URLC1

Not applicable; no known mechanisms of action for drugs as there are currently no approved drugs directly targeting PHF20L1.