Supplementary Materials for:
Quantitative Phosphoproteomic Analysis of T Cell Receptor Signaling
Reveals System-Wide Modulation of Protein-Protein Interactions
Viveka Mayya, Deborah H. Lundgren, Sun-Il Hwang, Karim Rezaul, Linfeng Wu,
Jimmy K. Eng, Vladimir Rodionov, David K. Han*
*To whom correspondence should be addressed. E-mail:
This PDF file includes:
- Materials and Methods (incorporating figs. S1 to S4)
- Fig. S5. Accumulation of unique phosphopeptides in the Jurkat phosphoproteome.
- Fig. S6. Distribution of the number of sites in phosphopeptides and the certainty in
- Fig. S7. Summary of TCR-responsive fold changes in the abundance of
phosphopeptides as determined by SILAC experiments.
- Fig. S8. Illustration of the quantification of fold change by targeted MS/MS.
- Fig. S9. Comparison of phosphopeptide spectral count data with SILAC data.
- Fig. S10. Global trends in the phosphorylation data set.
- Fig. S11. Abundance and subcellular localization of phosphoproteins based on
protein spectral count data.
- Fig. S12. Putative substrates of ERK during TCR signaling.
- Fig. S13. Validation of Thr260 of BCL11B as a target of ERK.
- Fig. S14. Predicted substrates of Zap70.
- Fig. S15. Primary sequence representation of transcriptional regulators with TCR-responsive
- Fig. S16. Interactions among proteins involved in alternative splicing of mRNA that
have TCR-responsive phosphorylation sites.
- Fig. S17. TCR-responsive phosphorylation events in nuclear pore components.
- Fig. S18. Network analysis to assess the influence of inducible phosphorylation of
Ser or Thr residues on PPIs.
- Fig. S19. Typical product ion chromatogram showing the lack of phosphorylation in
- Fig. S20. Network representation of nuclear proteins involved in hematopoiesis,
lymphoma, and leukemia for which phosphorylation sites were identified in the
- Fig. S21. Schematic of the experimental work flow used to identify TCR-responsive
phosphorylation sites by SILAC.
- Fig. S22. Phosphorylated forms of tubulins are excluded from polymerized
- Descriptions of supplementary tables
Format: Adobe Acrobat PDF
Size: 1.56 MB
Other Supplementary Material for this manuscript includes the following:
Tables S1 to S14
[Download Tables (Compressed)]
Format: Microsoft Excel format (XLS) (Zipped)
Size: 5.0 MB
V. Mayya, D. H. Lundgren, S.-I. Hwang, K. Rezaul, L. Wu, J. K. Eng, V. Rodionov,
D. K. Han, Quantitative phosphoproteomic analysis of T cell receptor signaling reveals
system-wide modulation of protein-protein interactions. Sci. Signal. 2, ra46 (2009).
© 2009 American Association for the Advancement of Science