Systematic Analysis and Prediction of In Situ Cross Talk of O-GlcNAcylation and PhosphorylationReport as inadecuate




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BioMed Research International - Volume 2015 2015, Article ID 279823, 12 pages -

Research Article

School of Life Science, University of Science and Technology of China, Hefei 230027, China

School of Information Science and Technology, University of Science and Technology of China, Hefei 230027, China

Centers for Biomedical Engineering, University of Science and Technology of China, Hefei 230027, China

Received 2 August 2015; Revised 1 October 2015; Accepted 4 October 2015

Academic Editor: Cheng-Xin Gong

Copyright © 2015 Heming Yao et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Reversible posttranslational modification PTM plays a very important role in biological process by changing properties of proteins. As many proteins are multiply modified by PTMs, cross talk of PTMs is becoming an intriguing topic and draws much attention. Currently, lots of evidences suggest that the PTMs work together to accomplish a specific biological function. However, both the general principles and underlying mechanism of PTM crosstalk are elusive. In this study, by using large-scale datasets we performed evolutionary conservation analysis, gene ontology enrichment, motif extraction of proteins with cross talk of O-GlcNAcylation and phosphorylation cooccurring on the same residue. We found that proteins with in situ O-GlcNAc-Phos cross talk were significantly enriched in some specific gene ontology terms and no obvious evolutionary pressure was observed. Moreover, 3 functional motifs associated with O-GlcNAc-Phos sites were extracted. We further used sequence features and GO features to predict O-GlcNAc-Phos cross talk sites based on phosphorylated sites and O-GlcNAcylated sites separately by the use of SVM model. The AUC of classifier based on phosphorylated sites is 0.896 and the other classifier based on GlcNAcylated sites is 0.843. Both classifiers achieved a relatively better performance compared with other existing methods.





Author: Heming Yao, Ao Li, and Minghui Wang

Source: https://www.hindawi.com/



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