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Zinc-finger proteins contain DNA-binding domains characterized by the unique role of zinc and have a wide variety of functions such as transcriptional activation or repression. The protein folding and the DNA binding ability are governed by the coordination of a zinc ion. As a member of the MYM (myeloproliferative and mental retardation) gene family, ZMYM1 is widely expressed in different tissues in eukaryotes under several forms derived by alternative splicing. While its function remains unknown, the related protein ZMYM2 has been shown to associate with and stabilize the LSD1-CoREST-HDAC1 (LCH) complex of chromatin through its MYM-type zinc fingers, thereby enhancing the transcriptional repression of several genes, suggesting that ZMYM1 may play a similar role.
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