FpClass

FpClass predicts proteome-wide protein-protein interactions to expand the human interactome and support studies of protein function, disease associations, and drug mechanisms.


Key Features:

  • Data mining-based methodology: Uses a data mining-based approach to generate proteome-wide PPI predictions.
  • Predicted interactions: Predicted 250,498 potential interactions among 10,531 human proteins.
  • Novel interactions for uncharacterized proteins: Identified 10,647 PPIs involving 1,089 proteins that previously had no known interactions.
  • False discovery rate estimate: Estimates a false discovery rate of approximately 60% for its predictions.
  • Experimental validation: Experimentally tested 233 high- and medium-confidence predictions and validated 137 interactions.
  • p53 interactors: Validated seven novel putative interactors of the tumor suppressor p53.
  • Agreement with experimental data: Demonstrated superior agreement with experimentally detected PPIs compared to previous prediction methods.

Scientific Applications:

  • Interactome expansion: Expands the mapped human interactome by predicting proteome-wide PPIs including interactions for previously uncharacterized proteins.
  • Protein function prediction: Supports inference of protein function through predicted interaction partners.
  • Disease association: Aids in linking proteins to diseases via predicted interaction networks.
  • Drug mechanism elucidation: Facilitates investigation of drug mechanisms of action through predicted PPIs.
  • Experimental prioritization: Provides candidate interactions for targeted experimental validation.

Methodology:

Employs a data mining-based approach to predict PPIs proteome-wide and reports an estimated false discovery rate of ~60%.

Topics

Details

Tool Type:
command-line tool, web application
Operating Systems:
Linux, Windows, Mac
Added:
8/3/2017
Last Updated:
12/10/2018

Operations

Data Inputs & Outputs

Protein-protein interaction prediction

Publications

Kotlyar M, et al. In silico prediction of physical protein interactions and characterization of interactome orphans. Nat Methods. 2015; 12:79-84. doi: 10.1038/nmeth.3178

PMID: 25402006

Documentation

Links