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pmic7351-sup-0001-FigureS1.doc4254K

Figure S1. Synchronization of HeLa cells.

Figure S2. Comparison among different HeLa-cell phosphoproteome datasets.

Figure S3. The kinase-substrate interaction network.

pmic7351-sup-0002-TableS1.xls7498K

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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