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 protein 195 (ZNF195), also known as ZNFP104, is a 629 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZNF195 is expressed in adult brain, heart, placenta, pancreas and skeletal muscle and in fetal brain, lung and kidney. ZNF195 contains ten C2H2-type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation. Three isoforms of ZNF195 exist as a result of alternative splicing events.