Related Experiment Video
Updated: Jul 18, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
Published on: March 3, 2015
How complete are current yeast and human protein-interaction networks?
G Traver Hart1, Arun K Ramani, Edward M Marcotte
1Center for Systems and Synthetic Biology, Institute for Cellular and Molecular Biology, University of Texas at Austin, 2500 Speedway, Austin, TX 78712, USA.
Estimating protein-protein interaction networks reveals vast potential interactions in yeast and humans. However, high false-positive rates limit current map accuracy, suggesting raw data release could improve true interaction identification.
Area of Science:
- Biochemistry
- Systems Biology
- Bioinformatics
Background:
- Protein-protein interactions (PPIs) are fundamental to cellular processes.
- Current protein-protein interaction network maps are incomplete due to experimental limitations and high false-positive rates.
- Understanding the scale and accuracy of PPI networks is crucial for biological discovery.
Purpose of the Study:
- To estimate the total number of protein-protein interactions in yeast and human interactomes.
- To assess the completeness of current protein-protein interaction network maps.
- To explore strategies for improving the accuracy of protein-protein interaction data.
Main Methods:
- Computational analysis and network inference to estimate the size of yeast and human PPI networks.
- Evaluation of current experimental data completeness based on estimated network sizes.
- Analysis of the impact of false-positive rates on network accuracy.
Main Results:
- The full yeast PPI network is estimated to contain 37,800–75,500 interactions.
- The full human PPI network is estimated to contain 154,000–369,000 interactions.
- Current yeast PPI maps are approximately 50% complete, while human maps are only 10% complete due to high false-positive rates.
Conclusions:
- Despite significant progress, current protein-protein interaction network maps are far from complete.
- High false-positive rates in experimental assays are a major bottleneck for accurate interactome mapping.
- Releasing raw, unfiltered assay data may paradoxically improve the identification of true protein-protein interactions.
Related Concept Videos
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces
Protein-Protein Interfaces
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

