Date published: 2025-11-9

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LOC150383_2210021J22Rik Inhibitors

Cysteine-rich DPF motif domain containing 1, abbreviated as CDPF1, is a protein that, as indicated by its name, is characterized by the presence of a DPF (double PHD fingers) domain and an enrichment of cysteine residues. The DPF domain is typically associated with proteins that regulate chromatin remodeling, a crucial process for controlling gene expression by altering the structure of chromatin, thereby affecting the accessibility of DNA to transcription machinery.The cysteine-rich regions of CDPF1 suggest that this protein may have the ability to bind metal ions, which could be important for its structural stability or for mediating protein-protein interactions. Metal ion binding is a common feature of many proteins that are involved in signaling pathways, including those related to cell growth, differentiation, and repair.

While the specific biological functions of CDPF1 are not fully elucidated, proteins containing DPF domains are often implicated in the recruitment of chromatin remodeling complexes to particular regions of the genome. This recruitment is essential for the epigenetic regulation of gene expression, influencing various cellular processes such as development, differentiation, and response to external stimuliGiven the involvement of DPF domain-containing proteins in epigenetic regulation, CDPF1 may play a role in modulating the expression of genes necessary for various cellular functions. It is possible that CDPF1 interacts with other chromatin-associated proteins to facilitate the remodeling of chromatin structure, thereby enabling or repressing the transcription of specific genes.

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