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Article

Large-Scale Identification and Evolution Indexing of Tyrosine Phosphorylation Sites from Murine Brain

Supporting Info

Bryan A. Ballif*^§, G. Richard Carey^†^‡, Shamil R. Sunyaev^‡ and Steven P. Gygi^†

Department of Biology, University of Vermont, Burlington, Vermont 05405, Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, and Division of Genetics, Department of Medicine, Brigham and Women’s Hospital and Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115

J. Proteome Res., 2008, 7 (01), pp 311–318

DOI: 10.1021/pr0701254

Publication Date (Web): November 23, 2007

* Corresponding author: Bryan A. Ballif, Ph.D., Department of Biology, University of Vermont, 109 Carrigan Drive, Burlington, VT 05405. Telephone: (802) 656-1389 . Fax: (802) 656-2914. E-mail: bballif@uvm.edu.

University of Vermont.

†

Harvard Medical School.

‡

Brigham and Women’s Hospital and Harvard Medical School.

Abstract

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.

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