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. ZNF98 (zinc finger protein 98) and ZNF492 (zinc finger protein 492) are zinc finger proteins belonging to the Krüppel C2H2-type zinc-finger protein family. Both ZNF98 and ZNF492 localize to the nucleus and contain thirteen C2H2-type zinc fingers and a KRAB domain. ZNF98 and ZNF492 may play a role in transcriptional regulation.