Journal
JOURNAL OF PROTEOME RESEARCH
Volume 7, Issue 1, Pages 311-318Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr0701254
Keywords
phosphorylation brain; kinase; phosphoproteomics; mass spectrometry; evolution; bioinformatics
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Funding
- NCRR NIH HHS [P20 RR16462] Funding Source: Medline
- NHGRI NIH HHS [HG00041] Funding Source: Medline
- NIGMS NIH HHS [GM070986] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR016462] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM070986] Funding Source: NIH RePORTER
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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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