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. 2012 Aug 22;6:107. doi: 10.1186/1752-0509-6-107

Table 2.

Summary of selected temporal phosphoproteomic data

Protein Residue Wolf-Yadlin et al. (2007) VanMeter et al. (2009) Ciaccio et al. (2010)
ERBB1 (EGFR)
 
 
 
 
 
Y845
 
 
X
 
Y992
 
X
 
 
Y998
X
 
 
 
Y1045
X
 
 
 
Y1068
 
X
X
 
Y1086
 
 
X
 
Y1148
X
X
 
 
Y1173
X
X
X
ERBB2 (HER2)
 
 
 
 
 
Y1221/1222
 
 
X
 
Y1248
X
X
 
ERBB3 (HER3)
 
 
 
 
 
Y1289
 
 
X
 
Y1328
 
 
 
ERBB4
 
 
 
 
 
Y1284
 
 
X
Shc1
 
 
 
 
 
Y239/240
X
 
X
 
Y317
X
X
X
Raf-1
 
 
 
 
 
S289/296/301
 
 
X
 
S338
 
 
X
MEK1/2
 
 
 
 
 
S217/T221
 
 
X
ERK1/2
 
 
 
 
 
T202/Y204
X
X
X
Gab1
 
 
 
 
 
Y373
X
 
 
 
Y406
X
 
 
 
Y627
X
X
X
 
Y659
X
 
 
Akt1
 
 
 
 
 
T308
 
X
X
  S473   X X

Time courses have been measured for many of the serine, threonine and tyrosine (S/T/Y) residues considered in the model presented here. Here, we focus on three studies that applied distinct experimental techniques to measure time courses of phosphorylation for specific S/T/Y sites. In the study of Wolf-Yadlin et al. [45], the technique of selected reaction monitoring and quantitative mass spectrometry was applied. In the study of VanMeter et al. [46], the technique of reverse phase protein array was applied. In the study of Ciaccio et al. [47], the technique of microwestern array was applied. An ‘X’ entry in this table signifies that a time course of phosphorylation for the indicated residue was measured in the indicated study.