Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.
Metazoans employ reversible tyrosine phosphorylation to regulate innumerable biological processes. Thus, the large-scale identification of tyrosine phosphorylation sites from primary tissues is an essential step toward a molecular systems understanding of dynamic regulation in vivo. The relative paucity of phosphotyrosine has greatly limited its identification in large-scale phosphoproteomic experiments. However, using antiphosphotyrosine peptide immunoprecipitations, we report the largest study to date of tyrosine phosphorylation sites from primary tissue, identifying 414 unique tyrosine phosphorylation sites from murine brain. To measure the conservation of phosphorylated tyrosines and their surrounding residues, we constructed a computational pipeline and identified patterns of conservation within the signature of phosphotyrosine.
Ballif
Bryan A
BA
Department of Biology, University of Vermont, Burlington, Vermont 05405, USA. bballif@uvm.edu
Carey
G Richard
GR
Sunyaev
Shamil R
SR
Gygi
Steven P
SP
D000818:Animals; D000906:Antibodies; D001665:Binding Sites; D001923:Brain Chemistry; D017124:Conserved Sequence; D019143:Evolution, Molecular; D047468:Immunoprecipitation; D051379:Mice; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000032:analysis* / Q000276:immunology
D000906:Antibodies; D019000:Phosphotyrosine