Copyright © 2003 Elsevier Ltd. All rights reserved.
Brief communication
Reduced bio basis function neural network for identification of protein phosphorylation sites: comparison with pattern recognition algorithms
Received 17 September 2003;
References and further reading may be available for this article. To view references and further reading you must purchase this article.
Abstract
Protein phosphorylation is a post-translational modification performed by a group of enzymes known as the protein kinases or phosphotransferases (Enzyme Commission classification 2.7). It is essential to the correct functioning of both proteins and cells, being involved with enzyme control, cell signalling and apoptosis. The major problem when attempting prediction of these sites is the broad substrate specificity of the enzymes. This study employs back-propagation neural networks (BPNNs), the decision tree algorithm C4.5 and the reduced bio-basis function neural network (rBBFNN) to predict phosphorylation sites. The aim is to compare prediction efficiency of the three algorithms for this problem, and examine knowledge extraction capability. All three algorithms are effective for phosphorylation site prediction. Results indicate that rBBFNN is the fastest and most sensitive of the algorithms. BPNN has the highest area under the ROC curve and is therefore the most robust, and C4.5 has the highest prediction accuracy. C4.5 also reveals the amino acid 2 residues upstream from the phosporylation site is important for serine/threonine phosphorylation, whilst the amino acid 3 residues upstream is important for tyrosine phosphorylation.
Author Keywords: Protein phosphorylation; Neural networks; Genetic algorithm; Pattern recognition
Article Outline
- 1. Introduction
- 2. Materials and methods
- 2.1. Reduced bio basis function neural network
- 2.2. Back propagation neural networks
- 2.3. C4.5 decision tree program
- 2.4. Model assessment
- 2.5. Data organisation
- 2.6. Data encoding
- 2.7. Implementation
- 3. Results
- 4. Discussion
- 5. Requests for software
- Acknowledgements
- References






E-mail Article
Add to my Quick Links

Cited By in Scopus (24)






