| 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, EZI, also known as ZNF467 (zinc finger protein 467) or Zfp467, is a 595 amino acid nuclear protein that contains twelve C2H2-type zinc fingers. EZI interacts with Stat3, thereby keeping it in the nucleus and enhancing Stat3 activity. Involved in transcriptional regulation, EZI transactivates several promoters including c-Fos and OSM. EZI is considered a novel cargo protein for importin-7 and is able to perform a nucleocytoplasmic shuttling mechanism that is mediated by importin-7-dependent nuclear localization and CRM1-independent nuclear export. |