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. HSZFP36, also known as ZNF823 (zinc finger protein 823) or ZFP36, is a 610 amino acid member of the Krüppel C2H2-type zinc-finger protein family and is thought be involved in transcriptional regulation. Localized to the nucleus, HSZFP36 contains one KRAB domain and 16 C2H2-type zinc fingers through which it may convey DNA, RNA and protein binding capabilities.