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. 2018 Feb 19;9(18):14597–14607. doi: 10.18632/oncotarget.24523

Table 1. Post-radiation fold changes in phosphorylation at calpastatin serines 351 and 633.

Calpastatin Phospho-peptide Phosphosite Post-RT Time-point OSU-2 OSU-11 OSU-20 U87 NHA
KPADDQDPIDAL[S]GDLDSCPSTTETSQNTAK S633 30 s 5.0* 4.2 3.4* −1.6 N/A
KPADDQDPIDAL[S]GDLDSCPSTTETSQNTAK S633 4 h 6.3* 3.5 3.2* −1.7 N/A
SESELIDEL[S]EDFDR S351 30 s 2.2* 2.4 2.7* 1.6 N/A
SESELIDEL[S]EDFDR S351 4 h 3.4* 3.4* 3.5* 2.0 N/A

Fold changes were calculated for each time-point (30 s/Untreated and 4 h/Untreated) from triplicate intensity values from mass spectrometry data. Asterisk indicates a p-value of < 0.05. N/A indicates that no calpastatin peptides were identified in NHA. The phosphorylated residue in the phospho-peptide is indicated in brackets.