DCTPP1 (dCTP pyrophosphatase 1) is a ubiquitous nucleotide-metabolizing enzyme that hydrolyzes deoxycytidine triphosphate (dCTP) and related nucleotides to their monophosphate forms 1. The enzyme preferentially catalyzes dCTP hydrolysis with particularly high efficiency toward 5-formyl-dCTP, 5-iodo-dCTP, and 5-methyl-dCTP 1. DCTPP1 localizes to the nucleus, cytosol, and mitochondria 1, where it maintains deoxyribonucleoside triphosphate (dNTP) pool homeostasis critical for accurate DNA replication and genome stability 2. The enzyme protects cells from genotoxic nucleotide analogs through catabolism; DCTPP1-deficient cells accumulate dCTP and show hypersensitivity to pyrimidine analogs 1. Clinically, DCTPP1 emerges as a promising cancer therapeutic target. It is significantly overexpressed across multiple cancers and associates with poor prognosis 34. In colorectal cancer, DCTPP1 inhibition by natural compounds suppresses proliferation, induces apoptosis, and arrests the cell cycle through metabolic reprogramming 5. In ovarian cancer, high DCTPP1 expression correlates with cisplatin resistance; DCTPP1 knockdown enhances intracellular reactive oxygen species accumulation and restores drug sensitivity 3. Beyond cancer, DCTPP1 regulates oxidative stress homeostasis in placental trophoblasts through interaction with RNA-binding protein AUF1, with implications for pregnancy loss 6. DCTPP1 also participates in Wnt/β-catenin signaling regulation via USP7 interaction 7, suggesting pleiotropic biological roles beyond nucleotide metabolism.