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Zinc finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc finger proteins contain a Kr ppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. As a member of the Kr ppel C2H2-type zinc finger protein family, ZNF358 (zinc finger protein 358) is a 481 amino acid nuclear protein that contains nine C2H2-type zinc fingers through which it is thought to be involved in DNA-binding and transcriptional regulation.
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