CHERP (calcium homeostasis endoplasmic reticulum protein) is a ubiquitously expressed 100 kDa transmembrane protein located on chromosome 19.1 that functions as a critical regulator of intracellular calcium homeostasis and cell proliferation 1. The protein localizes to the endoplasmic reticulum and co-localizes with the inositol 1,4,5-trisphosphate (InsP3) receptor, mediating calcium release from intracellular stores 1. CHERP operates as a component of the spliceosomal machinery, interacting with RBM17 and U2SURP to regulate alternative splicing of RNA-processing factors and influence downstream gene expression 2. Functionally, CHERP depletion impairs intracellular calcium mobilization, reduces DNA synthesis, and causes growth arrest, demonstrating its essential role in cell maintenance 1. In IRE1α-deficient chondrocytes, elevated CHERP levels increase intracellular calcium content and impair autophagy, indicating CHERP's role in regulating autophagic flux 3. Pathologically, CHERP dysregulation contributes to colorectal cancer development through altered splicing of UPF3A, a factor promoting tumor cell survival 4. Additionally, CHERP expression is modulated by selenoprotein K during T-cell activation, linking calcium homeostasis to immune responses 5. These findings establish CHERP as a multifunctional protein integrating calcium signaling with splicing regulation and cellular proliferation.