PhosNetConstruct
PhosNetConstruct constructs phosphorylation networks by analyzing domain-specific kinase–substrate relationships to predict cognate kinase–substrate pairs and reveal preferential phosphorylation of protein domains within cellular signaling pathways.
Key Features:
- Domain-Level Analysis: Analyzes domain-specific kinase–substrate relationships to construct phosphorylation networks.
- Preferential Phosphorylation Identification: Detects preferential phosphorylation patterns of specific protein domains by particular kinases to inform regulatory mechanisms in signaling pathways.
- Automated Prediction System: Automates prediction of cognate kinase–substrate pairs and distinguishes them from non-cognate combinations based on domain compositions.
- Performance: Benchmarks predictions against independent datasets using statistical measures and reports improved performance with reduced false positives relative to existing predictors.
Scientific Applications:
- Phosphorylation Network Mapping: Maps phosphorylation networks that regulate cellular functions.
- Kinome–Phosphoproteome Integration: Links kinomes with phosphoproteomes to analyze signaling pathways.
- Therapeutic Target Identification: Identifies candidate therapeutic kinase targets through analysis of kinase–substrate relationships.
- Kinase–Substrate Interaction Analysis: Explores kinase–substrate interactions and domain-specific regulatory mechanisms in biological contexts.
Methodology:
Constructs phosphorylation networks by analyzing domain-specific kinase–substrate relationships, identifies preferential phosphorylation patterns of protein domains, automates prediction of cognate versus non-cognate kinase–substrate pairs based on domain composition, and benchmarks performance against independent datasets using statistical measures.
Topics
Details
- Tool Type:
- web application
- Operating Systems:
- Linux, Windows, Mac
- Added:
- 8/3/2017
- Last Updated:
- 11/25/2024
Operations
Publications
Damle NP, Mohanty D. Deciphering kinase–substrate relationships by analysis of domain-specific phosphorylation network. Bioinformatics. 2014;30(12):1730-1738. doi:10.1093/bioinformatics/btu112. PMID:24574117.