These authors contributed equally to this work.
Identification of complex relationship between protein kinases and substrates during the cell cycle of HeLa cells by phosphoproteomic analysis
Article first published online: 20 MAR 2013
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Special Issue: FOCUS ON INTEGRATIVE PROTEOMICS
Volume 13, Issue 8, pages 1233–1246, April 2013
How to Cite
Yang, X.-L., Li, Q.-R., Ning, Z.-B., Zhang, Y., Zeng, R. and Wu, J.-R. (2013), Identification of complex relationship between protein kinases and substrates during the cell cycle of HeLa cells by phosphoproteomic analysis. Proteomics, 13: 1233–1246. doi: 10.1002/pmic.201200357
Colour Online: See the article online to view Figs. 1–4 in colour.
- Issue published online: 12 APR 2013
- Article first published online: 20 MAR 2013
- Accepted manuscript online: 16 JAN 2013 05:40AM EST
- Manuscript Accepted: 25 OCT 2012
- Manuscript Revised: 8 OCT 2012
- Manuscript Received: 11 AUG 2012
- Ministry of Science and Technology. Grant Numbers: 2010CB912102, 2011CB910200
- National Natural Science Foundation of China. Grant Number: 31130034
- Chinese Academy of Sciences. Grant Numbers: KJCX2-YW-M15, 2012OHTP10
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Figure S1. Synchronization of HeLa cells.
Figure S2. Comparison among different HeLa-cell phosphoproteome datasets.
Figure S3. The kinase-substrate interaction network.
Table S1. Phosphosites of Class I group.
Table S2. The list of newly identified phosphosites of well-known, cell cycle–regulated proteins.
Table S3. The list of all newly identified phosphosites.
Table S4. Functional annotation for proteins with newly identified phosphosites.
Table S5. Distribution of phosphosites by predicted kinase groups.
Table S6. The analysis of statistically significant differences between the predicted kinases of proteins with different number of phophorysites.
Table S7. Functional annotation for proteins regulated by single-kinase group and multi-kinase group.
Table S8. The difference of functional annotation between proteins regulated by single-kinase and multi-kinases.
Table S9. Functional annotation clustering for proteins with two co-existing phosphorylation sites regulated by CK2, CDK2/3 and p38 kinase groups
Table S10. Functional annotation clustering for proteins with two co-existing phosphorylation sites regulated by two different kinase groups (CDK2/3-p38, CDK2/3-CK2 and CK2-p38).
Table S11. The pathway analysis of proteins regulated by the same or different kinase groups.
Table S12. The sub-cellular localisation of proteins regulated by the same or different kinase groups.
Table S13. The likelihood of phosphosites with predicted kinase groups occurring by chance.
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