Aneuploidy is the leading genetic cause of human fertility failure. It is considered results from errors in meiotic and post-zygotic mitotic chromosome segregation. Using a
Protein phosphorylation, one of the most important protein post-translational modifications, is involved in various biological processes, and the identification of phosphorylation peptides （phosphopeptides） and thei...Protein phosphorylation, one of the most important protein post-translational modifications, is involved in various biological processes, and the identification of phosphorylation peptides （phosphopeptides） and their corresponding phosphorylation sites （phosphosites） will facilitate the understanding of the molecular mechanism and function of phosphorylation. Mass spectrometry （MS） provides a high- throughput technology that enables the identification of large numbers of phosphosites. PhoPepMass is designed to assist human phosphopeptide identification from MS data based on a specific database of phophopeptide masses and a multivariate hypergeometric matching algorithm. It contains 244,915 phosphosites from several public sources. Moreover, the accurate masses of peptides and fragments with phosphosites were calculated. It is the first database that provides a systematic resource for the query of phosphosites on peptides and their corresponding masses. This allows researchers to search certain proteins of which phosphosites have been reported, to browse detailed phosphopeptide and fragment information, to match masses from MS analyses with defined threshold to the corresponding phos- phopeptide, and to compare proprietary phosphopeptide discovery results with results from previous studies. Additionally, a database search software is created and a ＂two-stage search strategy＂ is suggested to identify phosphopeptides from tandem mass spectra of proteomics data. We expect PhoPepMass to be a useful tool and a source of reference for proteomics researchers.展开更多
文摘Aneuploidy is the leading genetic cause of human fertility failure. It is considered results from errors in meiotic and post-zygotic mitotic chromosome segregation. Using a
基金supported by National Key Research and Development Program of China (2016YFC0904101)Chinese Human Proteome Projects (CNHPP: 2014DFB30020, 2014DFB30030)+1 种基金Shanghai Municipal Science and Technology Commission of China (No. 17ZR1420300)National Hi-Tech Program (2015AA020101)
文摘Protein phosphorylation, one of the most important protein post-translational modifications, is involved in various biological processes, and the identification of phosphorylation peptides （phosphopeptides） and their corresponding phosphorylation sites （phosphosites） will facilitate the understanding of the molecular mechanism and function of phosphorylation. Mass spectrometry （MS） provides a high- throughput technology that enables the identification of large numbers of phosphosites. PhoPepMass is designed to assist human phosphopeptide identification from MS data based on a specific database of phophopeptide masses and a multivariate hypergeometric matching algorithm. It contains 244,915 phosphosites from several public sources. Moreover, the accurate masses of peptides and fragments with phosphosites were calculated. It is the first database that provides a systematic resource for the query of phosphosites on peptides and their corresponding masses. This allows researchers to search certain proteins of which phosphosites have been reported, to browse detailed phosphopeptide and fragment information, to match masses from MS analyses with defined threshold to the corresponding phos- phopeptide, and to compare proprietary phosphopeptide discovery results with results from previous studies. Additionally, a database search software is created and a ＂two-stage search strategy＂ is suggested to identify phosphopeptides from tandem mass spectra of proteomics data. We expect PhoPepMass to be a useful tool and a source of reference for proteomics researchers.
