{"title":"ModProt: a database for integrating laboratory and literature data about protein post-translational modifications","authors":"Y. Kimura, T. Toda, H. Hirano","doi":"10.2198/JELECTROPH.60.1","DOIUrl":null,"url":null,"abstract":"Protein post-translational modifications (PTMs) play crucial roles in regulation of protein function and cell signaling, and abnormalities in protein PTMs are both causes and consequences of disease. Mass spectrometry (MS) is widely used to analyze protein PTMs. In this study, we developed an original database, ModProt (Post-Translational Modification Map of Proteome), to integrate our laboratory data and literature information regarding PTM sites. To develop the ModProt database, we constructed a web-based laboratory information management system (LIMS). This system allows us to administer the ModProt database and to view PTM site maps and corresponding protein information including amino acid sequences, official gene symbols, UniProt accessions/IDs, chromosome number/ positions, and additional description. The ultimate goal of the ModProt database is to achieve PTM-based diagnosis and personalized medicine through detection of abnormal PTMs by comparing PTM site maps in healthy and disease states using the database.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"88 1","pages":"1-4"},"PeriodicalIF":0.0000,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of capillary electrophoresis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2198/JELECTROPH.60.1","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
Protein post-translational modifications (PTMs) play crucial roles in regulation of protein function and cell signaling, and abnormalities in protein PTMs are both causes and consequences of disease. Mass spectrometry (MS) is widely used to analyze protein PTMs. In this study, we developed an original database, ModProt (Post-Translational Modification Map of Proteome), to integrate our laboratory data and literature information regarding PTM sites. To develop the ModProt database, we constructed a web-based laboratory information management system (LIMS). This system allows us to administer the ModProt database and to view PTM site maps and corresponding protein information including amino acid sequences, official gene symbols, UniProt accessions/IDs, chromosome number/ positions, and additional description. The ultimate goal of the ModProt database is to achieve PTM-based diagnosis and personalized medicine through detection of abnormal PTMs by comparing PTM site maps in healthy and disease states using the database.