PHD finger protein 13 (PHF13)

PHF13 is a conserved chromatin regulatory protein containing a plant homeodomain (PHD) finger, which recognizes methylated lysine 4 on histone H3 (H3K4me2/3), allowing it to serve as an epigenetic reader and transcriptional co-regulator[1][3][4][5]. PHF13 modulates chromatin structure through multivalent interactions with DNA, histones, and other chromatin-associated complexes such as Polycomb repressive complex 2 (PRC2) and RNA Polymerase II[1][3][4]. It regulates key cellular processes including DNA repair, cell division, and differentiation, mainly through modulating gene transcription and chromatin compaction[1][2][3][4][6]. Aberrant expression of PHF13 has been implicated in oncogenesis, particularly promoting epithelial–mesenchymal transition (EMT)-like phenotypes and adverse cancer prognosis[1][4][6]. PHF13 can oligomerize through both ordered and disordered protein regions, impacting its chromatin affinity and the spatial organization of genome architecture[1][2]. Deficiency or overexpression of PHF13 leads to significant effects on cellular homeostasis, genome integrity, and development[1]. As of now, there are no direct small molecule modulators or approved drugs targeting PHF13[1][6].

Other names

SPOC1 (Survival time-associated PHD finger protein in ovarian cancer 1)MGC43399PHF5PHD zinc finger protein PHF5survival time-associated PHD protein in ovarian cancersurvival time-associated PHD finger protein in ovarian cancer 1

Not applicable (no current drugs directly targeting PHF13); potential mechanisms could involve disruption of its chromatin association, inhibition of histone binding, or modulation of its interactions with PRC2/RNA Polymerase II