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 Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger protein 568 (ZNF568) is a 644 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZNF568 contains fifteen C2H2-type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation. Two isoforms of ZNF568 exist as a result of alternative splicing events.