PTMint Database of Experimentally Verified PTM Regulation on Protein-Protein Interaction


 
 
 Post translational modification (PTM) is an important biochemical process. which includes six most well studied types: phosphorylation (Phos), acetylation (Ac), methylation (Me), sumoylation (Sumo), ubiquitylation (Ub) and glycosylation (Glyco). PTM is involved in various cell signaling pathways and biological processes. Abnormal PTM status is closely associated with severe diseases (such as Cancer and neurologic diseases) by regulating protein functions, such as Protein-Protein Interactions (PPI). A set of databases was constructed separately for PTM sites and protein-protein interaction, however the resource of regulation for PTM on PPI is still unsolved.
 
 
 
 Here we firstly constructed a public accessible database of PTMint (PTMs that are associated with Protein-Protein Interactions) (https://ptmint.sjtu.edu.cn/) that contains manually curated complete experimental evidence of the PTM regulation on protein-protein interactions in multiple organisms, including Homo sapiens, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Saccharomyces cerevisiae and Schizosaccharomyces pombe. Currently, the first version of PTMint encompassed 2,477 non-redundant PTM sites in 1,169 proteins affecting 2,371 protein-protein pairs involving 357 diseases. Various annotations were systematically integrated, such as protein sequence, structure properties and protein complex analysis. PTMint database can help to insight into disease mechanism, disease diagnosis and drug discovery associated with PTM and PPI.
 
 
 
 PTMint is freely available at: https://ptmint.sjtu.edu.cn/.
 
 
 
 Supplementary data are available at Bioinformatics online.
