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. ZFP106 (Zinc finger protein 106), also known as zinc finger protein 474, is a 1883 amino acid human homolog of the mouse Zfp106 protein and is a member of the Krüppel C2H2-type zinc-finger family. Localized to the nucleus, ZFP106 contains two C2H2-type zinc fingers and is thought to be involved in transcriptional regulation.