Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairs

<p>Abstract</p> <p>Background</p> <p>As one of the most common protein post-translational modifications, glycosylation is involved in a variety of important biological processes. Computational identification of glycosylation sites in protein sequences becomes increasing...

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Main Authors: Sheng Zhi-Ya, Tang Yu-Rong, Chen Yong-Zi, Zhang Ziding
Format: Article
Language:English
Published: BMC 2008-02-01
Series:BMC Bioinformatics
Online Access:http://www.biomedcentral.com/1471-2105/9/101
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spelling doaj-8d0bacbfd1d44ddbb1c6f2504d11e3a92020-11-24T21:43:11ZengBMCBMC Bioinformatics1471-21052008-02-019110110.1186/1471-2105-9-101Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairsSheng Zhi-YaTang Yu-RongChen Yong-ZiZhang Ziding<p>Abstract</p> <p>Background</p> <p>As one of the most common protein post-translational modifications, glycosylation is involved in a variety of important biological processes. Computational identification of glycosylation sites in protein sequences becomes increasingly important in the post-genomic era. A new encoding scheme was employed to improve the prediction of mucin-type O-glycosylation sites in mammalian proteins.</p> <p>Results</p> <p>A new protein bioinformatics tool, CKSAAP_OGlySite, was developed to predict mucin-type O-glycosylation serine/threonine (S/T) sites in mammalian proteins. Using the composition of <it>k</it>-spaced amino acid pairs (CKSAAP) based encoding scheme, the proposed method was trained and tested in a new and stringent O-glycosylation dataset with the assistance of Support Vector Machine (SVM). When the ratio of O-glycosylation to non-glycosylation sites in training datasets was set as 1:1, 10-fold cross-validation tests showed that the proposed method yielded a high accuracy of 83.1% and 81.4% in predicting O-glycosylated S and T sites, respectively. Based on the same datasets, CKSAAP_OGlySite resulted in a higher accuracy than the conventional binary encoding based method (about +5.0%). When trained and tested in 1:5 datasets, the CKSAAP encoding showed a more significant improvement than the binary encoding. We also merged the training datasets of S and T sites and integrated the prediction of S and T sites into one single predictor (i.e. S+T predictor). Either in 1:1 or 1:5 datasets, the performance of this S+T predictor was always slightly better than those predictors where S and T sites were independently predicted, suggesting that the molecular recognition of O-glycosylated S/T sites seems to be similar and the increase of the S+T predictor's accuracy may be a result of expanded training datasets. Moreover, CKSAAP_OGlySite was also shown to have better performance when benchmarked against two existing predictors.</p> <p>Conclusion</p> <p>Because of CKSAAP encoding's ability of reflecting characteristics of the sequences surrounding mucin-type O-glycosylation sites, CKSAAP_ OGlySite has been proved more powerful than the conventional binary encoding based method. This suggests that it can be used as a competitive mucin-type O-glycosylation site predictor to the biological community. CKSAAP_OGlySite is now available at <url>http://bioinformatics.cau.edu.cn/zzd_lab/CKSAAP_OGlySite/</url>.</p> http://www.biomedcentral.com/1471-2105/9/101
collection DOAJ
language English
format Article
sources DOAJ
author Sheng Zhi-Ya
Tang Yu-Rong
Chen Yong-Zi
Zhang Ziding
spellingShingle Sheng Zhi-Ya
Tang Yu-Rong
Chen Yong-Zi
Zhang Ziding
Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairs
BMC Bioinformatics
author_facet Sheng Zhi-Ya
Tang Yu-Rong
Chen Yong-Zi
Zhang Ziding
author_sort Sheng Zhi-Ya
title Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairs
title_short Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairs
title_full Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairs
title_fullStr Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairs
title_full_unstemmed Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairs
title_sort prediction of mucin-type o-glycosylation sites in mammalian proteins using the composition of <it>k</it>-spaced amino acid pairs
publisher BMC
series BMC Bioinformatics
issn 1471-2105
publishDate 2008-02-01
description <p>Abstract</p> <p>Background</p> <p>As one of the most common protein post-translational modifications, glycosylation is involved in a variety of important biological processes. Computational identification of glycosylation sites in protein sequences becomes increasingly important in the post-genomic era. A new encoding scheme was employed to improve the prediction of mucin-type O-glycosylation sites in mammalian proteins.</p> <p>Results</p> <p>A new protein bioinformatics tool, CKSAAP_OGlySite, was developed to predict mucin-type O-glycosylation serine/threonine (S/T) sites in mammalian proteins. Using the composition of <it>k</it>-spaced amino acid pairs (CKSAAP) based encoding scheme, the proposed method was trained and tested in a new and stringent O-glycosylation dataset with the assistance of Support Vector Machine (SVM). When the ratio of O-glycosylation to non-glycosylation sites in training datasets was set as 1:1, 10-fold cross-validation tests showed that the proposed method yielded a high accuracy of 83.1% and 81.4% in predicting O-glycosylated S and T sites, respectively. Based on the same datasets, CKSAAP_OGlySite resulted in a higher accuracy than the conventional binary encoding based method (about +5.0%). When trained and tested in 1:5 datasets, the CKSAAP encoding showed a more significant improvement than the binary encoding. We also merged the training datasets of S and T sites and integrated the prediction of S and T sites into one single predictor (i.e. S+T predictor). Either in 1:1 or 1:5 datasets, the performance of this S+T predictor was always slightly better than those predictors where S and T sites were independently predicted, suggesting that the molecular recognition of O-glycosylated S/T sites seems to be similar and the increase of the S+T predictor's accuracy may be a result of expanded training datasets. Moreover, CKSAAP_OGlySite was also shown to have better performance when benchmarked against two existing predictors.</p> <p>Conclusion</p> <p>Because of CKSAAP encoding's ability of reflecting characteristics of the sequences surrounding mucin-type O-glycosylation sites, CKSAAP_ OGlySite has been proved more powerful than the conventional binary encoding based method. This suggests that it can be used as a competitive mucin-type O-glycosylation site predictor to the biological community. CKSAAP_OGlySite is now available at <url>http://bioinformatics.cau.edu.cn/zzd_lab/CKSAAP_OGlySite/</url>.</p>
url http://www.biomedcentral.com/1471-2105/9/101
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