Reduction of ambiguity in phosphorylation-site localization in large-scale phosphopeptide profiling by data filter using unique mass class information

Inamul Hasan Madar, Seunghoon Back, Dong Gi Mun, Hokeun Kim, Jae Hun Jung, Kwang Pyo Kim, Sang-Won Lee

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The rapid development of shotgun proteomics is paving the way for extensive proteome profiling, while providing extensive information on various post translational modifications (PTMs) that occur to a proteome of interest. For example, the current phosphoproteomic methods can yield more than 10,000 phosphopeptides identified from a proteome sample. Despite these developments, it remains a challenging issue to pinpoint the true phosphorylation sites, especially when multiple sites are possible for phosphorylation in the peptides. We developed the Phospho-UMC filter, which is a simple method of localizing the site of phosphorylation using unique mass classes (UMCs) information to differentiate phosphopeptides with different phosphorylation sites and increase the confidence in phosphorylation site localization. The method was applied to large scale phosphopeptide profiling data and was demonstrated to be effective in the reducing ambiguity associated with the tandem mass spectrometric data analysis of phosphopeptides.

Original languageEnglish
Pages (from-to)845-850
Number of pages6
JournalBulletin of the Korean Chemical Society
Volume35
Issue number3
DOIs
Publication statusPublished - 2014 Mar 20

Keywords

  • Phosphoproteomics
  • Phosphorylation site
  • Unique mass class

ASJC Scopus subject areas

  • Chemistry(all)

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