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Zinc finger protein 133 (ZNF133) is a member of the KRAB (Krüppel-associated box) domain-containing zinc finger protein family, which are among the largest groups of human transcription factors. ZNF133 consists of a KRAB domain at the N-terminal end and 14 contiguous C2H2-type zinc finger motifs at the C-terminal region. It functions primarily as a transcriptional repressor: the KRAB domain interacts with co-repressors such as TIF1β, while the zinc finger motifs promote transcriptional repression both by binding to DNA and through protein interactions. ZNF133 can interact with protein inhibitor of activated STAT1 (PIAS1) via its zinc finger motifs, and this interaction enhances its repressor activity, likely involving the recruitment of histone deacetylases (HDACs)[1]. ZNF133 expression has been observed to be upregulated in certain cancer types and after immune stimulation, supporting possible roles in oncogenesis and immune regulation. However, the precise biological targets and regulatory pathways of ZNF133 in normal and disease states remain largely undefined[1].
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