| Modification Notes |
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. As a member of the krueppel C2H2-type zinc-finger protein family, ZNF74 (Zinc finger protein 74) is a 643 amino acid nuclear protein that contains one KRAB domain and twelve C2H2-type zinc fingers. These internal features enable ZNF74 to bind tightly to the nuclear matrix and be involved in protein-protein interactions. Mapping to chromosome 22, the gene encoding ZNF74 is found to be consistently deleted in DiGeorge syndrome, a disease characterized by congenital heart defects, recurrent infections, palate abnormalities and learning disabilities. There are four isoforms of ZNF74 that are produced as a result of alternative splicing events. |
