dbPTM is an integrated resource for protein post-translational modifications (PTMs). Due to the importance of protein post-translational modifications (PTMs) in regulating biological processes, the dbPTM was developed as a comprehensive database by integrating experimentally verified PTMs from several databases and annotating the potential PTMs for all UniProtKB protein entries. The dbPTM has been maintained for over ten years with an attempt to provide comprehensively functional and structural analyses for post-translational modifications (PTMs). In this update, dbPTM not only integrate more experimentally validated PTMs from available databases and manual curation of literature, but also provide disease association based on non-synonymous single nucleotide polymorphisms (nsSNPs). - [Data Statistics Page]

The high-throughput deep sequencing technology has leaded the analysis of association between SNPs and diseases into a data surge in both growth and scope. This update thus integrated disease-associated nsSNPs from dbSNP based on Genome-Wide Association Studies (GWAS). The PTM substrate sites locating in a specified distance of the amino acids encoded from nsSNPs were referred to having an association with its involving diseases (Figure 1). In recent years, an increasing evidence for crosstalk between PTMs has been reported.

Although mass spectrometry (MS)-based proteomics has substantially improved our knowledge about substrate site specificity of single PTM, this neglects the fact that the crosstalk of combinatorial PTMs may act in concert in the regulation of protein function. Due to the relatively limited information about the frequency and functional relevance of PTM crosstalk, in this update, the PTM sites neighbouring with other PTM sites in a specified window length were subjected to motif discovery and functional enrichment analysis. This update confronts the current state of PTM crosstalk research and breaks the bottleneck of how proteomics may contribute to understanding PTM codes, revealing the next level of data complexity and proteomic limitation in prospective PTM research.