PHD finger protein 1 (PHF1)

PHD finger protein 1 (PHF1) is a Polycomb group protein and acts as a histone modification reader with a critical role in epigenetic regulation, genome stability, and transcriptional repression[1][3][4]. PHF1 possesses a Tudor domain, two PHD fingers, and additional homology domains, enabling it to recognize specific histone marks such as H3K36 trimethylation and H4R3 symmetric dimethylation (H4R3me2s). PHF1 binds to and coordinates complexes including the PRMT5–WDR77 complex and the CUL4B-Ring E3 ligase (CRL4B), contributing to histone ubiquitination and gene repression. It is an essential factor in recruiting the PRC2 complex to chromatin and is involved in the DNA damage response. PHF1 has been shown to promote cell proliferation, invasion, and tumorigenesis. Its expression is increased in several human cancers, highlighting its relevance as a potential therapeutic target in oncology[1][2][4][5].

Other names

Polycomb-like protein 1PCL1hPHF1hPCl1MTF2L2TDRD19Ctesticular tissue protein Li 140tudor domain containing 19C

PHF1 acts as a reader of histone modifications (e.g., H4R3me2s, H3K36me3). It is involved in the recruitment of the PRC2 complex (Polycomb repressive complex 2) and coordinates with ubiquitin ligase complexes (e.g., CRL4B).