CRIP1 (cysteine-rich protein 1) functions as a regulatory protein involved in multiple cellular processes including protein homeostasis, metabolic regulation, and immune modulation. The protein plays critical roles in cancer progression through diverse mechanisms. In pancreatic cancer, CRIP1 facilitates NF-κB/p65 nuclear translocation, promoting CXCL1/5 expression and myeloid-derived suppressor cell recruitment to create an immunosuppressive tumor microenvironment 1. Similarly, in gastric cancer, CRIP1 enhances lymphangiogenesis and metastasis by activating CREB1-mediated VEGFC expression and recruiting macrophages through CCL5 2. CRIP1 regulates protein degradation pathways by binding to USP7 and PA200, simultaneously controlling proteasome activity and autophagy maturation, contributing to multiple myeloma pathogenesis and drug resistance 3. The protein also modulates metabolic processes by promoting BBOX1 ubiquitination and degradation, suppressing carnitine metabolism to enhance cancer stem-like properties in hepatocellular carcinoma 4. In normal physiology, CRIP1 promotes osteogenic differentiation through Wnt signaling 5 and inhibits fibrosis by metabolic reprogramming 6. However, CRIP1 shows context-dependent effects, as it inhibits melanoma progression by suppressing TFAM-mediated mitochondrial biogenesis 7. These findings establish CRIP1 as a multifunctional regulatory protein with significant therapeutic potential across various diseases.