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. Author manuscript; available in PMC: 2016 Feb 6.

Published in final edited form as: Oncogene. 2014 Nov 10;34(32):4260–4269. doi: 10.1038/onc.2014.361

A, MS/MS spectrum of a quadruply-charged ion (m/z 1371.16) corresponding to a doubly phosphorylated peptide is shown. The phosphorylation sites are Y²²¹ and Y²³⁹. B, MS/MS spectrum of a doubly-charged ion (m/z 1055.53) corresponding to the peptide sequence with a phosphorylation modification at Y²⁵¹ is shown. The observed y- and b-ion series confirmed the peptide sequence and modification. C, GST-Crk was in vitro phosphorylated by immunoprecipitated Abl 1b in a kinase reaction and samples were analyzed by western blotting with anti-pY221 Crk (bottom), anti-pY239 Crk (middle) and anti-pY251 Crk (top) antibodies. D, Locations of Y239 and Y251 on the SH3C and Y221 on the inter-SH3 linker are depicted on the solution structure of Crk (PDB ID: 2EYZ).

Inline graphic — A, MS/MS spectrum of a quadruply-charged ion (m/z 1371.16) corresponding to a doubly phosphorylated peptide is shown. The phosphorylation sites are Y²²¹ and Y²³⁹. B, MS/MS spectrum of a doubly-charged ion (m/z 1055.53) corresponding to the peptide sequence with a phosphorylation modification at Y²⁵¹ is shown. The observed y- and b-ion series confirmed the peptide sequence and modification. C, GST-Crk was in vitro phosphorylated by immunoprecipitated Abl 1b in a kinase reaction and samples were analyzed by western blotting with anti-pY221 Crk (bottom), anti-pY239 Crk (middle) and anti-pY251 Crk (top) antibodies. D, Locations of Y239 and Y251 on the SH3C and Y221 on the inter-SH3 linker are depicted on the solution structure of Crk (PDB ID: 2EYZ).