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dbPTM 2025 update: comprehensive integration of PTMs and proteomic data for advanced insights into cancer research
Chia-Ru Chung1, Yun Tang2, Yen-Peng Chiu3
1Department of Computer Science and Information Engineering, National Central University, No. 300, Zhongda Rd., Zhongli Dist., Taoyuan City 320317, Taiwan.
Abstract:
Post-translational modifications (PTMs) are essential for modulating protein function and influencing stability, activity and signaling processes. The dbPTM 2025 update significantly expands the database to include over 2.79 million PTM sites, of which 2.243 million are experimentally validated from 48 databases and over 80 000 research articles. This version integrates proteomic data from 13 cancer types, with a particular focus on phosphoproteomic data and kinase activity profiles, allowing the exploration of personalized phosphorylation patterns in tumor samples. Integrating kinase-substrate phosphorylations with E3 ligase-substrate interactions, dbPTM 2025 provides a detailed map of PTM regulatory networks, offering insights into cancer-specific post-translational regulations. This update also includes advanced search capabilities, enabling users to efficiently query PTM data across species, PTM types and modified residues. The platform's new features-interactive visualization tools and streamlined data downloads-allow researchers to access and analyze PTM data easily. dbPTM 2025 also enhances functional annotations, regulatory networks and disease associations, broadening its application for cancer research and the study of disease-associated PTMs. Through these enhancements, dbPTM 2025 is a comprehensive, user-friendly resource, facilitating the study of PTMs and their roles in cancer research. The database is now freely accessible at https://biomics.lab.nycu.edu.tw/dbPTM/.
Insights
The dbPTM 2025 database now includes over 2.79 million post-translational modification (PTM) sites, with a focus on cancer proteomic data. This resource aids researchers in exploring PTMs and their roles in cancer.
Area of Science:
- Biochemistry
- Bioinformatics
- Genomics
Background:
- Post-translational modifications (PTMs) are crucial for protein function, stability, activity, and signaling.
- The dbPTM database serves as a vital resource for PTM information.
Purpose of the Study:
- To present the significant expansion and new features of the dbPTM 2025 database update.
- To highlight the integration of cancer-specific proteomic data and regulatory networks.
- To enhance the utility of dbPTM for cancer research and the study of disease-associated PTMs.
Main Methods:
- Expansion of the dbPTM database to include over 2.79 million PTM sites (2.243 million experimentally validated).
- Integration of proteomic data from 13 cancer types, focusing on phosphoproteomics and kinase activity.
- Incorporation of kinase-substrate phosphorylations and E3 ligase-substrate interactions to map PTM regulatory networks.
- Development of advanced search capabilities, interactive visualization tools, and streamlined data downloads.
Main Results:
- dbPTM 2025 now contains over 2.79 million PTM sites, with 2.243 million experimentally validated.
- The database integrates extensive cancer proteomic data, enabling personalized phosphorylation pattern analysis in tumors.
- New features facilitate efficient data querying, analysis, and exploration of PTM regulatory networks.
- Enhanced functional annotations, regulatory networks, and disease associations are provided.
Conclusions:
- dbPTM 2025 is a comprehensive and user-friendly resource for studying PTMs.
- The updated database significantly advances cancer research by providing detailed insights into PTMs and their regulatory networks.
- dbPTM 2025 facilitates the investigation of disease-associated PTMs and personalized cancer therapies.
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