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 Kruppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. As a member of the krueppel C2H2-type zinc-finger protein family, ZNF131 (Zinc finger protein 131) is a 623 amino acid nuclear protein that contains one BTB (POZ) domain and six C2H2-type zinc fingers. With predominant expression found in brain, it is likely that ZNF131 plays a role as a transcription regulator during development and organogenesis of the adult central nervous system. ZNF131 also represses ER Alpha (Estrogen receptor alpha)-mediated transactivation by interrupting ER?binding to the estrogen-response element. There are two isoforms of ZNF131 that are produced as a result of alternative splicing events.