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. ZNF496 (Zinc finger protein 496), also known as ZKSCAN17 or NIZP1, is a 587 amino acid member of the Krüppel C2H2-type zinc-finger protein family and is thought to act as a transcriptional repressor. Localized to the nucleus, ZNF496 contains one SCAN box domain, one KRAB domain and five C2H2-type zinc fingers through which it may convey DNA, RNA and protein binding capabilities.