Protein disorder region will be annotated on dbPTM!

It was proposed that protein modification is associated with the protein disorder region. Thus, we integrate the protein disorder prediction tool, DISOPRED 2, to comprehensively annotate the protein entries in dbPTM. Users can investigate more structural information for protein modifications.

PhosphoELM version 7.0 is integrated in dbPTM!

Phospho.ELM version 7.0 (July 2007) contains 4078 substrate proteins from different species covering 2083 tyrosine, 12025 serine and 2362 threonine instances

dbPTM 2.0 is starting up!

This update extends dbPTM to a knowledge base comprising the modified sites, solvent accessibility of substrate, protein secondary and tertiary structures, protein domains and protein variations. Literature related to PTM, protein conservations and substrate specificity are also analyzed. Moreover, various computational tools have been developed for more than ten PTM types, such as phosphorylation, glycosylation, acetylation, methylation, sulfation and sumoylation. This study compiles a PTM benchmark consisting of all available experimental PTM sites for performance evaluation of these computational tools. The interface is also redesigned and enhanced to facilitate access to the resource.

The orthologous conserved region of protein sequences is considered!

In order to observe whether a PTM sites located in the conserved regions of protein orthologous sequences, the Clusters of Orthologous Groups of proteins (COGs), was integrated. The alignment of the protein sequences in each cluster, which was implemented by ClustalW, is provided in the resource.

A novel ubiquitylation database UbiProt is integrated!

UbiProt stores experimental ubiquitylated proteins and ubiquitylation sites, which are implicated in protein degradation via an intracellular ATP-dependent proteolytic system. UbiProt, which contains 417 ubiquitylated proteins and 165 ubiquitylation sites, was integrated into this new version.