AimTo analyze the structural and functional characteristics of potential candidate targets and biomarker ADAM17 in tumor tissue by using bioinformatics. MethodsDifferent databases such as ProtParam, ProtScale, STRING 12.0, the Human Protein Atlas, and cBioPortal were used to analyze the physical and chemical properties, signal peptide, nuclear localization sequence, phosphorylation and glycosylation sites, subcellular localization, secondary/tertiary structure, protein-protein interaction network, expression differences in various tumor and genetic alteration. Immunohistochemistry was used to validate the expression of ADAM17 in tumor tissues and normal samples of lung and colon tissues. ResultsHuman ADAM17 is a hydrophilic protein composed of 824 amino acids. The molecular formula is C₄₀₆₆H₆₃₅₆N₁₁₂₄O₁₂₇₇S₅₀, the theoretical isoelectric point is 5.50, and the average hydrophilicity is －0.573. ADAM17 is localized in the cytoplasm with 1 transmembrane domain, 1 signal peptide and 2 nuclear localization sequences. The secondary structure is mainly composed of irregular coils, with 89 possible phosphorylation sites, 5 N-glycosylation sites and 9 O-glycosylation sites. ADAM17 is widely distributed in lots of normal tissues, and highly expressed in bladder urothelial carcinoma, cervical squamous cell carcinoma, colon cancer (COAD), kidney clear cell carcinoma, liver hepatocellular carcinoma and lung squamous cell carcinoma (LUSC), and can interact with major proteins such as metalloproteinase-3 and epidermal growth factor, involving in tumor necrosis factor, nuclear factor-κB signaling pathways. The immunohistochemical verification results show that, ADAM17 is lowly expressed in normal human lung and colon tissues, while is highly expressied in LUSC and COAD tissues. ConclusionADAM17 may be a potential candidate target and biomarker for tumors.