PHF10 (PHD finger protein 10) is a subunit of chr6 remodeling complexes that plays critical roles in transcriptional regulation and cellular differentiation. PHF10 is incorporated into the PBAF (polybromo-associated BRG1-associated factor) complex, where it forms a histone tail-binding lobe together with PBRM1 and BRD7, contributing to nucleosome recognition 1. The protein exists as four isoforms, with PHD domain-containing isoforms (PHF10-P) essential for proliferation and chr6 remodeling during transcription activation, while PHD-lacking isoforms (PHF10-S) maintain transcription in terminally differentiated cells 2. PHF10 is required for normal cell proliferation, as both overexpression of truncated forms and knockdown result in reduced cell growth 3. The protein exhibits tissue-specific and context-dependent functions: it acts as a tumor suppressor in cholangiocarcinoma by coordinating with Setdb1 to suppress HMGB1 expression through H3K9me3 modifications 4, while paradoxically promoting gastric cancer carcinogenesis by inhibiting epithelial differentiation through DUSP5 repression and pERK1/2 activation 5. Additionally, PHF10 participates in DNA damage response, with its m6A modification by ZC3H13 being crucial for homologous recombination repair 6. The DPF domain of PHF10 shows unique structural features compared to other DPF-containing proteins, reflecting its specialized role in PBAF-mediated chr6 remodeling 7.