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The **Histone H4 transcription factor (HINFP)** is a zinc finger transcription factor that binds to conserved DNA motifs adjacent to the TATA box in most histone H4 genes and is critical for the activation of H4 gene expression, especially at the G1/S transition of the cell cycle[1][2][3]. HINFP forms a complex with the coactivator p220^NPAT^ (a substrate of cyclin E/CDK2), serving as the final essential effector in the cyclin E/CDK2/p220^NPAT^/HINFP pathway, which is indispensable for cell proliferation and chromatin assembly following DNA replication[2][3]. The factor is also known as MIZF due to its interaction with methyl-CpG-binding domain proteins such as MBD2, implicating it in DNA methylation and transcriptional repression[1]. HINFP is ubiquitously expressed in proliferating cells and tightly couples histone H4 transcription to cell cycle cues, but is downregulated in post-mitotic cells. Loss of HINFP function in animal models leads to early embryonic lethality due to a failure in cell proliferation and histone H4 gene expression[2][3]. Although its deregulation may contribute to proliferative diseases such as cancer, there are currently no known drugs that directly target HINFP, nor does it serve as a common biomarker or routine therapeutic target[2].
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