TY - JOUR
T1 - Human SRMAtlas
T2 - A Resource of Targeted Assays to Quantify the Complete Human Proteome
AU - Kusebauch, Ulrike
AU - Campbell, David S.
AU - Deutsch, Eric W.
AU - Chu, Caroline S.
AU - Spicer, Douglas A.
AU - Brusniak, Mi Youn
AU - Slagel, Joseph
AU - Sun, Zhi
AU - Stevens, Jeffrey
AU - Grimes, Barbara
AU - Shteynberg, David
AU - Hoopmann, Michael R.
AU - Blattmann, Peter
AU - Ratushny, Alexander V.
AU - Rinner, Oliver
AU - Picotti, Paola
AU - Carapito, Christine
AU - Huang, Chung Ying
AU - Kapousouz, Meghan
AU - Lam, Henry
AU - Tran, Tommy
AU - Demir, Emek
AU - Aitchison, John D.
AU - Sander, Chris
AU - Hood, Leroy
AU - Aebersold, Ruedi
AU - Moritz, Robert L.
N1 - Publisher Copyright:
© 2016 Elsevier Inc.
PY - 2016/7/28
Y1 - 2016/7/28
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84979649391&partnerID=8YFLogxK
U2 - 10.1016/j.cell.2016.06.041
DO - 10.1016/j.cell.2016.06.041
M3 - Article
C2 - 27453469
AN - SCOPUS:84979649391
SN - 0092-8674
VL - 166
SP - 766
EP - 778
JO - Cell
JF - Cell
IS - 3
ER -