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. 2013 Feb 20;8(2):e56150. doi: 10.1371/journal.pone.0056150

Table 1. Protein kinases eluted with drugs after 1M KCl wash of the affinity column.

Lapatinib
Protein Peptides Peptide Sequence Residue no.
Tb927.4.5180(TbLBPK1) 6 K.QQQQDLNHEK.K 280–291
R.RDEVEELK.K 220–229
K.AFDLQEAR.Y 336–345
R.RPFAEGESQQQIWQNK.L 537–554
R.QLTM’QLEELSVR.R 208–221
K.QATLPSYGLVNDTAVFR.K 92–110
Tb927.5.800(TbLBPK2) 4 K.TRHPQLAFEAR.F 45–57
R.GTNIQTGDPVAIK.L 27–41
K.TTLM’LAEQM’IAR.I 108–121
R.GSLPWQGLK.A 213–223
Tb927.3.1570(TbLBPK3) 2 R.RPLSICDSPSLEAK.F 118–133
K.ASLFTDILPTAATLPK.R 497–514
Tb10.61.3140(TbLBPK4) 2 R.VAGQGTFGTVQLAR.D 24–39
K.QPLPAEVYDLCGK.I 276–290
Canertinib
Protein Peptides Peptide Sequence Residue No.
Tb927.4.5180(TbLBPK1) 8 K.QQQQDLNHEK.K 280–291
R.RDEVEELKK.T 220–230
R.EVWVEGNK.M 198–207
K.AFDLQEAR.Y 336–345
R.RPFAEGESQQQIWQNK.L 537–554
R.VNDEDASAFVAVPALGHNGR.Y 299–320
K.QATLPSYGLVNDTAVFR.K 92–110
R.LIIM’QVVSALR.Y 426–438
Tb927.5.800(TbLBPK2) 7 R.THQHIPYK.E 165–174
K.RIHDTLQEGR.A 298–309
K.TRHPQLAFEAR.F 45–57
R.GTNIQTGDPVAIK.L 27–41
R.YCSINTHIGIEQSR.R 183–198
K.TTLM’LAEQM’IAR.I 110–121
R.GSLPWQGLK.A 213–223
Tb927.3.1570(TbLBPK3) 3 R.LAEQGLK.K 136–144
R.GDNTSGDWGYYK.R 198–211
K.ASLFTDILPTAATLPK.R 497–514
Tb10.61.3140(TbLBPK4) 2 K.NYFYTVGGEGR.R 80–92
R.VAGQGTFGTVQLAR.D 24–39
Tb10.61.1880(TbCBPK1) 2 K.LADFDQAK.V 154–163
K.GDNLLISM’DTGIAK.L 140–155
AEE788
Protein Peptides Peptide Sequence Residue No.
Tb927.4.5180(TbLBPK1) 8 K.QQQQDLNHEK.K 280–291
R.DAQIDELR.E 115–124
K.AFDLQEAR.Y 336–345
R.RPFAEGESQQQIWQNK.L 537–554
R.QLTM’QLEELSVR.R 208–221
R.VNDEDASAFVAVPALGHNGR.Y 299–320
K.QATLPSYGLVNDTAVFR.K 92–110
R.LIIM’QVVSALR.Y 426–438
Tb927.5.800(TbLBPK2) 4 R.IEFVHSK.S 120–128
K.TRHPQLAFEAR.F 45–57
R.GTNIQTGDPVAIK.L 27–41
R.GSLPWQGLK.A 213–223
Tb927.3.1570(TbLBPK3) 5 R.RGGGPETSPPR.G 187–199
R.RPLSICDSPSLEAK.F 118–133
R.LSNGEVVLEVENR.S 439–453
R.DLKPQNLLLTGR.S 348–361
K.ASLFTDILPTAATLPK.R 497–514

Proteins presented were detected at least twice in three independent affinity chromatography/mass spectrometry analyses.