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 Krueppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc-finger protein 134 (ZNF134) is a 348 amino acid member of the Krueppel C2H2-type zinc-finger protein family. ZNF134 localizes to the nucleus and contains nine C2H2-type zinc fingers through which it is thought to be involved in DNA-binding and transcriptional regulation.
Zinc finger protein 134; zinc finger protein 134 (clone pHZ-15)