Protein post-translational modifications (PTMs) are important molecular mechanisms that regulate protein structure and function. They play critical roles in expanding protein functional diversity and in modulating protein activity, subcellular localization, protein–protein interactions, and degradation. PTMs are also widely involved in a variety of physiological and pathological processes, including cell proliferation, differentiation, and signal transduction. Systematic investigation of PTM characteristics and regulatory mechanisms is of great significance for elucidating the fundamental principles of life processes, identifying disease biomarkers, and developing precise therapeutic strategies.To address current challenges in PTM-related databases, such as dispersed data resources, inconvenient retrieval, limited functionality, and insufficient analytical capacity, we developed PTMs DB. This database integrates eight major types of PTMs, including phosphorylation, ubiquitination, crotonylation, and acetylation, and comprehensively compiles core data resources such as basic protein information and modification residue positions.PTMs DB not only provides researchers with efficient and convenient data retrieval functions, but also incorporates practical modules for online prediction, literature search, multidimensional data visualization, and integrative analysis. These features can support a wide range of research needs, including PTM site screening, functional annotation, mechanistic investigation, and subsequent experimental validation. The establishment of PTMs DB will help improve the systematic nature and efficiency of PTM-related research, providing reliable data support and a useful technical platform for protein function studies, disease mechanism exploration, and clinical translational research.