CHORDC1 (cysteine and histidine-rich domain containing 1) functions as a multifaceted regulatory protein with roles in cellular homeostasis and disease processes. The protein acts as a co-chaperone for HSP90 and possesses intrinsic chaperone activity, regulating centrosome duplication through inhibition of ROCK2 kinase activity 1. CHORDC1 serves as a critical component of the IKK/NF-κB signaling pathway, where it is essential for IκBα substrate recognition and NF-κB activation, thereby influencing cancer cell metastasis 2. The protein also interacts with tau protein, suggesting potential involvement in neurodegenerative processes 3. In viral infections, CHORDC1 promotes hepatitis B virus replication by enhancing viral enhancer/promoter activities, with its expression being negatively regulated by miR-26b 4. CHORDC1 influences extracellular vesicle secretion in prostate cancer cells and affects drug sensitivity in breast cancer, where elevated expression correlates with poor prognosis and reduced sensitivity to tamoxifen and paclitaxel 56. The protein demonstrates context-dependent oncogenic or tumor-suppressive properties, highlighting its complex role in cancer biology 7.