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PHD finger protein 14 (PHF14) is a chromatin-binding nuclear protein and a member of the plant homeodomain (PHD) finger protein family, involved in recognizing and binding specific histone modifications to regulate gene expression epigenetically[1][2][3][4]. PHF14 directly interacts with nucleosomal histones—binding preferentially to unmodified histone H3—and participates in chromatin remodeling and transcriptional regulation by interpreting histone marks[2][3][4]. It plays a pivotal role in controlling cell proliferation, mitosis, and developmental processes, as well as repressing PDGFRA and CDKN1A/p21 gene expression, with consequences for tissue morphogenesis and tumorigenesis[1][2][3][4]. PHF14 is highly expressed in several cancers (notably lung cancer), where it promotes tumor cell growth and proliferation; its overexpression correlates with poor prognosis and may serve as a diagnostic and prognostic biomarker[1][3][4]. Functional disruption of PHF14 impairs organ development and cell cycle fidelity and can lead to severe developmental disorders in model organisms[1][3]. As a chromatin reader and cofactor in cancer, PHF14 represents a potential therapeutic target, although no drugs currently are known to modulate its activity.
Epigenetic modulation via histone mark recognition; Regulation of cell proliferation by controlling expression of cell cycle genes (e.g., PDGFRA, CDKN1A/p21)
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