HIPK2 Protein, Human (Active, sf9, His-GST)

HIPK2, a serine/threonine-protein kinase, emerges as a versatile regulator, participating in transcriptional control, p53/TP53-mediated cellular apoptosis, and cell cycle modulation. Functioning as a corepressor for various transcription factors, including SMAD1, POU4F1/Brn3a, and potentially NK homeodomain transcription factors, HIPK2 exerts its influence through the phosphorylation of a spectrum of substrates, including PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1, ZBTB4, and DAZAP2. HIPK2 acts as a negative regulator through the phosphorylation-induced proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. Additionally, it serves as an intermediate kinase in the Wnt/beta-catenin signaling pathway, promoting the proteasomal degradation of MYB. HIPK2's intricate involvement in cellular responses includes transcriptional co-suppression of HIF1A in response to hypoxia and the activation of TP73. Furthermore, it plays a crucial role in DNA damage responses, stabilizing PML, triggering ZBTB4 protein degradation, and preventing DAZAP2-dependent ubiquitination of HIPK2. Moreover, HIPK2 contributes to angiogenesis, erythroid differentiation, and the regulation of eye development during late embryogenesis.