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 Krueppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. As a member of the Krueppel C2H2-type zinc finger protein family, ZNF329 (zinc finger protein 329) is a 541 amino acid nuclear protein that contains twelve C2H2-type zinc fingers through which it is thought to be involved in DNA-binding and transcriptional regulation.