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. GLI-4, also known as HKR4, is a 376 amino acid protein that localizes to the nucleus and contains seven C2H2-type zinc fingers. Belonging to the krueppel C2H2-type zinc-finger protein family, GLI-4 may function as a transcriptional regulator, effectively activating or repressing the transcription of target genes. The gene encoding GLI-4 maps to human chromosome 8, which consists of nearly 146 million base pairs, houses more than 800 genes and is associated with a variety of diseases and malignancies.