PHF1 Polyclonal antibody

Background

Plant homeodomain finger protein 1 (PHF1) has a specific role in histone modification and in non-homologous end joining. It is a human homolog of the Drosophila protein Polycomb-like protein.

PHF1 acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. PHF1 regulates also p53/TP53 stability.

What is the molecular weight of PHF1?

62 kDa

What is the structure of PHF1?

PHF1 contains two zinc finger-like plant homeodomain (PHD) sequences, a Cys4-His-Cys3 motif that is able to recognize and modify histone tails, making it important in epigenetic regulation (PMID: 18682256). It also contains a Tudor domain, a sequence of approximately 60 amino acids that has also been shown to bind to methylated histone tails (PMID: 16601153). The sequence of PHF1 is similar to the Polycomb family of genes in Drosophila, chromatin remodeling genes that act in embryogenesis.

What is the role of PHF1?

PHF1 has a key role in histone modification. It acts by binding to the histone H3K36me3, a lysine methylation of histone H3 that is a mark for transcriptional activation (PMID: 17189264). PHF1 then recruits Polycomb repressive complex 2 (PRC2) to mark genes for repression. These epigenetic chromatin modifiers are important in cancer development, gene silencing, and stem cell maintenance.

PHF1 is also found to be recruited to double-strand breaks in DNA and plays an important part in the repair in non-homologous end joining (PMID: 18385154), the main DNA repair process in which ends of DNA are ligated without a homologous template. Interacting with proteins involved in DNA damage response, PH1 appears to have a role beyond the polycomb function (PMID: 18385154).