NetPhosBac

NetPhosBac predicts serine and threonine phosphorylation sites in bacterial proteins to support studies of bacterial signaling and regulation.


Key Features:

  • Prediction targets: Serine and threonine phosphorylation sites in bacterial proteins.
  • Training data: Large datasets derived from gel-free high accuracy mass spectrometry (MS) studies, including sites identified in Bacillus subtilis and Escherichia coli.
  • Algorithm: Neural network algorithms tailored specifically for bacterial proteins.
  • Taxa-specific modeling: Captures bacterial phosphorylation patterns that differ from eukaryotic-type protein kinase motifs.
  • Benchmark performance: Demonstrated superior performance compared to predictors trained on eukaryotic data when applied to bacterial phosphorylation sites.
  • Experimental validation: Predictions experimentally verified at protein- and site-specific levels in Escherichia coli.

Scientific Applications:

  • Bacterial signaling and regulation studies: Identification of phosphorylated residues to study signaling pathways and regulatory mechanisms in bacteria.
  • Proteome annotation: Annotation of phosphorylation sites in bacterial proteomes such as Bacillus subtilis and Escherichia coli.
  • Comparative phosphorylation analysis: Comparison of bacterial phosphorylation patterns with eukaryotic phosphorylation to investigate motif differences.
  • Experimental prioritization: Selection of candidate phosphorylation sites for targeted experimental validation in bacterial systems.

Methodology:

Training on large gel-free high accuracy mass spectrometry (MS) datasets and application of neural network algorithms tailored for bacterial proteins.

Topics

Details

License:
Other
Maturity:
Emerging
Cost:
Free of charge (with restrictions)
Tool Type:
web application
Operating Systems:
Linux, Windows, Mac
Added:
6/29/2015
Last Updated:
12/29/2018

Operations

Publications

Miller ML, Soufi B, Jers C, Blom N, Macek B, Mijakovic I. NetPhosBac – A predictor for Ser/Thr phosphorylation sites in bacterial proteins. PROTEOMICS. 2008;9(1):116-125. doi:10.1002/pmic.200800285. PMID:19053140.

Documentation

Links