The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
GPS 5.0: An Update on the Prediction of Kinase-Specific Phosphorylation Sites in Proteins
Open accessAbstract
In eukaryotes, protein phosphorylation is specifically catalyzed by numerous protein kinases (PKs), faithfully orchestrates various biological processes, and reversibly determines cellular dynamics and plasticity. Here we report an updated algorithm of Group-based Prediction System (GPS) 5.0 to improve the performance for predicting kinase-specific phosphorylation sites (p-sites). Two novel methods, position weight determination (PWD) and scoring matrix optimization (SMO), were developed. Compared with other existing tools, GPS 5.0 exhibits a highly competitive accuracy. Besides serine/threonine or tyrosine kinases, GPS 5.0 also supports the prediction of dual-specificity kinase-specific p-sites. In the classical module of GPS 5.0, 617 individual predictors were constructed for predicting p-sites of 479 human PKs. To extend the application of GPS 5.0, a species-specific module was implemented to predict kinase-specific p-sites for 44,795 PKs in 161 eukaryotes. The online service and local packages of GPS 5.0 are freely available for academic research at http://gps.biocuckoo.cn.
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AKT/PKB signaling: navigating downstream
Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115
ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
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Akt-Mediated Regulation of Autophagy and Tumorigenesis Through Beclin 1 Phosphorylation
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Cited by
Mari, T., Mösbauer, K., Wyler, E., Landthaler, M., Drosten, C., & Selbach, M. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00198 · Cited by 70
Wang, D., Pourmirzaei, M., Abbas, U. L., Zeng, S., Manshour, N., Esmaili, F., Poudel, B., Jiang, Y., Shao, Q., Chen, J., et al. (2025) · Advanced Science · doi:10.1002/advs.202404212 · Cited by 46
Molecular profiling of sponge deflation reveals an ancient relaxant-inflammatory response
Ruperti, F., Becher, I., Stokkermans, A., Wang, L., Marschlich, N., Potel, C., Maus, E., Stein, F., Drotleff, B., Schippers, K. J., et al. (2024) · Current Biology · doi:10.1016/j.cub.2023.12.021 · Cited by 23
AURKB-driven dissolution of CIZ1–RNA assemblies from the inactive X chromosome in mitosis
Byrom, L., Turvey, G. L., Dowle, A. A., Thomas, M., Shirodkar, N., Green, B. J., Brown, M., Ball, C., Chapman, K. E., Guglielmi, E., et al. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag018 · Cited by 2
Metadata
- Authors
- Wang, C., Xu, H., Lin, S., Deng, W., Zhou, J., Zhang, Y., Shi, Y., Peng, D., & Xue, Y.
- Venue
- Genomics, Proteomics & Bioinformatics
- Publisher
- Oxford University Press (OUP)
- Published
- 2020-02-01
- Volume
- 18
- Issue
- 1
- Pages
- 72-80
- ISSN
- 1672-0229 (ISSN-L)
- 2210-3244
- OpenAlex
- W3011725683
- Cited by
- 297
- References
- 5
- FWCI
- 13.28
- Type
- journal article
- Language
- en
- Open access
- gold
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