Title: dbPTM 3.0: an informative resource for investigating substrate site specificity and functional association of protein post-translational modifications
Authors: Lu, Cheng-Tsung
Huang, Kai-Yao
Su, Min-Gang
Lee, Tzong-Yi
Bretana, Neil Arvin
Chang, Wen-Chi
Chen, Yi-Ju
Chen, Yu-Ju
Huang, Hsien-Da
生物科技學系
生物資訊及系統生物研究所
Department of Biological Science and Technology
Institude of Bioinformatics and Systems Biology
Issue Date: 1-Jan-2013
Abstract: Protein modification is an extremely important post-translational regulation that adjusts the physical and chemical properties, conformation, stability and activity of a protein; thus altering protein function. Due to the high throughput of mass spectrometry (MS)-based methods in identifying site-specific post-translational modifications (PTMs), dbPTM (http://dbPTM.mbc.nctu.edu.tw/) is updated to integrate experimental PTMs obtained from public resources as well as manually curated MS/MS peptides associated with PTMs from research articles. Version 3.0 of dbPTM aims to be an informative resource for investigating the substrate specificity of PTM sites and functional association of PTMs between substrates and their interacting proteins. In order to investigate the substrate specificity for modification sites, a newly developed statistical method has been applied to identify the significant substrate motifs for each type of PTMs containing sufficient experimental data. According to the data statistics in dbPTM, > 60% of PTM sites are located in the functional domains of proteins. It is known that most PTMs can create binding sites for specific protein-interaction domains that work together for cellular function. Thus, this update integrates protein-protein interaction and domain-domain interaction to determine the functional association of PTM sites located in protein-interacting domains. Additionally, the information of structural topologies on transmembrane (TM) proteins is integrated in dbPTM in order to delineate the structural correlation between the reported PTM sites and TM topologies. To facilitate the investigation of PTMs on TM proteins, the PTM substrate sites and the structural topology are graphically represented. Also, literature information related to PTMs, orthologous conservations and substrate motifs of PTMs are also provided in the resource. Finally, this version features an improved web interface to facilitate convenient access to the resource.
URI: http://dx.doi.org/10.1093/nar/gks1229
http://hdl.handle.net/11536/20797
ISSN: 0305-1048
DOI: 10.1093/nar/gks1229
Journal: NUCLEIC ACIDS RESEARCH
Volume: 41
Issue: D1
Begin Page: D295
End Page: D305
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