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. HIC-2 (hypermethylated in cancer 2) possesses zinc finger motifs that are thought to be important for DNA-binding and also has a BTB/POZ domain at the N-terminus, which is thought to be important for protein-protein binding, as well as for the binding of transcription factors. HIC-2 is also known as Hic-3, HIC1-related gene on chromosome 22 or Zinc finger and BTB domain-containing protein 30, and is a 615 amino acid protein that is expressed as two isoforms produced by alternative splicing. HIC-2 is highly expressed in cerebellum and is localized to the nucleus in cells. HIC-2 contains a short amino acid sequence that is thought to interact with CtBP, a transcriptional repressor. The gene sequence associated with HIC-2 is thought to be a target for miRNAs (microRNAs) which are expressed in many cancers, suggesting that HIC-2 could possess tumor suppressor capabilities.