PHD finger protein 11 (PHF11)

PHD finger protein 11 (PHF11) is a zinc-binding protein with an extended plant homeodomain (PHD) finger motif, expressed as multiple isoforms through alternative splicing. The PHD finger mediates protein–protein interactions, particularly with methylated histone tails, implicating PHF11 in chromatin-associated functions. PHF11 is critically involved in 5′ end resection at sites of DNA double-strand breaks, acting as a gatekeeper that negotiates RPA-coated DNA repair intermediates, facilitating homologous recombination and maintenance of genomic stability. Additionally, PHF11 regulates Th1-type cytokine gene expression, contributing to T-cell activation and viability, and has been identified as a candidate gene in atopic diseases such as asthma and IgE responsiveness. It also interacts with multiple DNA repair proteins including EXO1, RPA, BARD1, and others. Its malfunction or deficiency could theoretically affect immune function and DNA repair fidelity, with disease associations seen in inflammatory conditions and cancer. Note: There are no direct drug interactions, mechanisms of action, or safety profiles established for active pharmaceutical modulation of PHF11 as of current literature and searchable databases. It is primarily of interest as a molecular target in immunology and DNA repair research.

Other names

APYBCAPIGELIGERIGHERNY-REN-34NYREN34BRCA1 C-terminus-associated proteinRenal carcinoma antigen NY-REN-34

Not applicable; no reported direct drug modulators. Its principal molecular action is mediation of protein-protein interactions in DNA repair and immune regulation.