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 Krppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ZFP64 (Zinc finger protein 64), also known as ZNF338, is a 681 amino acid homolog of the mouse Zfp64 protein and is a member of the Krppel C2H2-type zinc-finger family. Localized to the nucleus, ZFP64 contains nine C2H2-type zinc fingers and is thought to be involved in transcriptional regulation. Four isoforms of ZFP64 exist due to alternative splicing events.