Abstract

LymPHOS is a web-oriented database containing peptide and protein sequences and spectrometric information on the phosphoproteome of primary human T-Lymphocytes. Current release 2.0 contains 15 566 phosphorylation sites from 8273 unique phosphopeptides and 4937 proteins, which correspond to a 45-fold increase over the original database description. It now includes quantitative data on phosphorylation changes after time-dependent treatment with activators of the TCR-mediated signal transduction pathway. Sequence data quality has also been improved with the use of multiple search engines for database searching. LymPHOS can be publicly accessed at http://www.lymphos.org.Database URL: http://www.lymphos.org.

Highlights

  • Regulation of cell function is mediated by changes in protein activity, protein stability and protein–protein interactions, through the action of a wide range of posttranslational modifications (PTMs)

  • We have identified 15 566 phosphorylation sites in a total of 8273 unique phosphopeptides belonging to 4937 proteins

  • The LymPHOS web application consists of a relational database and a web interface that allows data submission, Figure 3

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Summary

Introduction

Regulation of cell function is mediated by changes in protein activity, protein stability and protein–protein interactions, through the action of a wide range of posttranslational modifications (PTMs). In 2008, UniProtKB/Swiss-Prot generated the first draft of the human proteome including 20 000 protein-coding genes. In 2013, spectrometric data repositories such as PRIDE accumulated more than 30 000 experiments with nearly 7 million unique peptides identified in different species [1]. The establishment of these databases has promoted many initiatives such as the Human Proteome Project (HPP), which has among its objectives to sequence all proteins encoded in the human genome (including modified forms), VC The Author(s) 2015.

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