| 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, ZNF336 (Zinc finger protein 336), also known as GZF1 (GDNF-inducible zinc finger protein 1) and ZBTB23 (Zinc finger and BTB domain-containing protein 23), is a 711 amino acid nuclear protein that contains one BTB (POZ) domain and ten C2H2-type zinc fingers. The gene encoding ZNF336 is upregulated in response to glial cell line-derived neurotrophic factor (GDNF) stimulation. Knockdown of ZNF336 mRNA impairs ureteric bud branching in mouse, suggesting that ZNF336 may be necessary for renal branching morphogenesis. |