NDLI: Prediction of mucin-type O-glycosylation sites by a two-staged strategy

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Prediction of mucin-type O-glycosylation sites by a two-staged strategy

Content Provider	Springer Nature Link
Author	Cai, YuDong He, JianFeng Lu, Lin
Copyright Year	2010
Abstract	The mucin-type O-glycosylation of a protein is an important type of protein post-translational modification. This process is mediated by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases which transfer the N-acetylgalactosamine (GalNAc) to the serine or threonine residues with unknown specificity. In order to determine the glycosylation sites of a given protein, we present a two-staged prediction method here, which first determines whether a protein is a glycoprotein, and then determines the glycosylation sites of a protein that has been predicted to be glycosylated in the first stage. In the first stage, a protein is encoded by the protein families in PFAM, which is a collective annotated database of classified protein families; then it is predicted by a predictor trained by the training set. In the second stage, nonapeptides of the predicted mucin-type glycoproteins, with serine or threonine residues at their fifth sites, are represented by indices in AAIndex. Then, it is predicted whether the nonapeptides are attached by GalNAc by a predictor, which is constructed with features selected by feature selection methods [Maximum Relevance Minimum Redundancy (mRMR) method and Incremental Feature Selection method]. The prediction accuracy of the first stage is 94.9% validated by Leave-One-Out validation method; the prediction accuracy of the second stage is 99.4%. These results show that this method is valuable to study the mucin-type O-glycosylation. The analysis of the features used to construct the predictor of the second stage confirms the previously obtained results from other groups. The residues at position −1 and +3 have great impact on the prediction. Among other amino acid indices, the indices about alpha and turn propensities and indices about hydrophobicity of the residues in nonapeptide also influence the recognition of the GalNAc transferases. A web server is available at http://chemdata.shu.edu.cn/gal/.
Starting Page	427
Ending Page	433
Page Count	7
File Format	PDF
ISSN	13811991
Journal	Molecular Diversity
Volume Number	15
Issue Number	2
e-ISSN	1573501X
Language	English
Publisher	Springer Netherlands
Publisher Date	2010-07-22
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Mucin-type O-glycosylation sites PFAM Minimum Redundancy Maximum Relevance Feature Selection Nearest Neighbor Algorithm K-fold cross-validation Pharmacy Polymer Sciences Biochemistry Organic Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Medicine Drug Discovery Molecular Biology Physical and Theoretical Chemistry Information Systems Catalysis Inorganic Chemistry

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