Human SRMAtlas: A resource of targeted assays to quantify the complete human proteome Journal Article


Authors: Kusebauch, U.; Campbell, D. S.; Deutsch, E. W.; Chu, C. S.; Spicer, D. A.; Brusniak, M. Y.; Slagel, J.; Sun, Z.; Stevens, J.; Grimes, B.; Shteynberg, D.; Hoopmann, M. R.; Blattmann, P.; Ratushny, A. V.; Rinner, O.; Picotti, P.; Carapito, C.; Huang, C. Y.; Kapousouz, M.; Lam, H.; Tran, T.; Demir, E.; Aitchison, J. D.; Sander, C.; Hood, L.; Aebersold, R.; Moritz, R. L.
Article Title: Human SRMAtlas: A resource of targeted assays to quantify the complete human proteome
Abstract: The ability to reliably and reproducibly measure any protein of the human proteome in any tissue or cell type would be transformative for understanding systems-level properties as well as specific pathways in physiology and disease. Here, we describe the generation and verification of a compendium of highly specific assays that enable quantification of 99.7% of the 20,277 annotated human proteins by the widely accessible, sensitive, and robust targeted mass spectrometric method selected reaction monitoring, SRM. This human SRMAtlas provides definitive coordinates that conclusively identify the respective peptide in biological samples. We report data on 166,174 proteotypic peptides providing multiple, independent assays to quantify any human protein and numerous spliced variants, non-synonymous mutations, and post-translational modifications. The data are freely accessible as a resource at http://www.srmatlas.org/, and we demonstrate its utility by examining the network response to inhibition of cholesterol synthesis in liver cells and to docetaxel in prostate cancer lines. © 2016 Elsevier Inc.
Journal Title: Cell
Volume: 166
Issue: 3
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 2016-07-28
Start Page: 766
End Page: 778
Language: English
DOI: 10.1016/j.cell.2016.06.041
PROVIDER: scopus
PUBMED: 27453469
PMCID: PMC5245710
DOI/URL:
Notes: Article -- Export Date: 1 September 2016 -- Source: Scopus
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MSK Authors
  1. Chris Sander
    210 Sander
  2. Emek Demir
    27 Demir