qPTM

qPTM: Quantitative Database of Post-Translational Modification Dynamics

qPTM aggregates and curates quantitative data on post-translational modifications (PTMs) across multiple organisms to support analysis of dynamic protein regulation. It integrates datasets covering phosphorylation, acetylation, glycosylation, methylation, SUMOylation, and ubiquitylation, enabling comparative and temporal investigation of PTM site dynamics.

Key Features:

• Extensive Data Integration: Consolidates quantitative PTM datasets from multiple organisms and modification types to enable cross-condition and cross-species comparisons.
• Reliability Scoring System: Implements confidence scoring based on raw mass spectrometry false discovery rate control and recurrence of PTM site identifications across independent datasets.
• PTM Site Annotation and Temporal Profiles: Provides detailed PTM site annotations and time-course dynamics data represented as quantitative trend lines.
• Comprehensive Quantitative Repository: Centralizes large-scale quantitative PTM datasets for systematic analysis of protein modification dynamics.

Scientific Applications:

• PTM Dynamics Analysis: Supports investigation of dynamic regulation of protein function and disease-associated mechanisms mediated by phosphorylation, acetylation, glycosylation, methylation, SUMOylation, and ubiquitylation.
• Comparative PTM Studies: Enables cross-species and cross-condition comparison of PTM site regulation.

Methodology:

Quantitative PTM data are collected from mass spectrometry-based studies, curated, and integrated across datasets. PTM site reliability is evaluated using false discovery rate control and recurrence frequency across independent experiments, and temporal dynamics are represented using quantitative trend analyses.