Zinc Finger Protein 197 (ZNF197)

ZnF197 contains the same SCAN domain and the KRAB-A domain, but differs from VHLaK at its C-terminus, which contains 22 C2H2-type zinc fingers. ZnF197 would interact with pVHL and KAP1/TIF-1b in the same or a similar manner, due to the same molecular structure in their N-termini.

ZnF197 may bind to DNA directly through its zinc fingers and function as a transcription factor. Its higher molecular weight and 22 zinc fingers may also provide multiple interfaces for interacting with other proteins. Since VHLaK can form homo-oligomers through its SCAN domain, VHLaK may well be able to form a heterodimer with ZnF197 though the same mechanism. It will be of interest to determine whether VHLaK and ZnF197 can also suppress HIF-2a and HIF-3a transactivation activities.