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Zinc finger protein 410 is a highly selective transcription factor characterized by pentadactyl (five-finger) DNA-binding domains, encoded by the ZNF410 gene. Its primary recognized function is as an activator of the chromatin remodeler CHD4, leading to repression of fetal hemoglobin genes (HBG1 and HBG2) in adult erythroid cells. Recent research highlights its unique specificity in regulating only the CHD4 gene among genome-wide targets, with important implications for hemoglobinopathies where therapeutic reactivation of fetal hemoglobin is beneficial. Additional, but less established, roles include activating matrix-remodeling and gap junction genes in specific contexts. ZNF410 does not act as a broad gene regulator but has a precisely restricted activity profile
Modulation of fetal hemoglobin expression via transcriptional activation of CHD4, a NuRD complex component, which then represses fetal globin genes
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