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Interferon regulatory factor 2-binding protein 2 (IRF2BP2) is a nuclear transcriptional coregulator that participates in multiple cell processes through both corepressor and coactivator functions, acting via its N-terminal zinc finger and C-terminal RING domains[1][2][3][4][5][6]. It was initially described as a corepressor of the transcription factor Interferon regulatory factor 2 (IRF-2), but it also interacts with multiple regulatory partners, influencing pathways governing immune response, cell differentiation, apoptosis, and angiogenesis[1][2][3][4][5][6]. IRF2BP2 is ubiquitously expressed and essential for physiological cell homeostasis, but genetic alterations can be linked to tumorigenesis, common variable immunodeficiency, and inflammatory conditions[2][3][6]. Various isoforms exist due to alternative splicing, and its functional domains enable interactions with a range of transcription factors and protein complexes, modulating gene expression relevant for development, immune defense, and cancer biology[1][2][3][4][6]. Key structural features include a Cys4 zinc finger, a nuclear localization sequence, and a Cys3HisCys4 RING domain important for protein–protein interactions and possibly for ubiquitination-related activities[6]. The protein plays a crucial regulatory role in specifying differentiation fates in hematopoietic, mesenchymal, and immune cells, as well as modulating apoptosis and inflammation[2][3][4][6][5]. There are no known direct small molecule drugs targeting IRF2BP2, nor is it currently established as a routine clinical biomarker or therapeutic target, but it represents a candidate for intervention in oncology and immunomodulatory settings based on preclinical data[2][3][6].
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