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. As a member of the krueppel C2H2-type zinc-finger protein family, ZNF449 is a 518 amino acid protein that contains one SCAN box domain and seven C2H2-type zinc fingers. ZNF449 is ubiquitously expressed and localizes to the nucleus. There are three isoforms of ZNF449 that are produced as a result of alternative splicing events.