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 Kr¨?ppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ZFAND1 (AN1-type zinc finger protein 1) is a 268 amino acid protein that contains 2 AN1-type zinc fingers, which are often found in proteins that contain a ubiquitin-like domain and therefore play a role in the ubiquitination pathway. AN1-type zinc fingers contains six conserved cysteines and two histidines and have a dimetal (zinc)-bound alpha/beta fold. There are two isoforms of ZFAND1 that are produced as a result of alternative splicing events.