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. Zinc finger and SCAN domain-containing protein 5A (ZSCAN5), also known as ZNF495 or ZSCAN5A, is a 496 amino acid member of the Krüppel C2H2-type zinc finger protein family. Localized to the nucleus, ZSCAN5 contains five C2H2-type zinc fingers at the carboxy terminus and one SCAN box domain, a leucine rich region of about 80 amino acids, at the amino terminus through which it is thought to be involved in DNA-binding and transcriptional regulation