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Nature. 2014 May 29;509(7502):582-7. doi: 10.1038/nature13319.

Mass-spectrometry-based draft of the human proteome.

Author information

1
1] Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany [2] SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany [3].
2
1] SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany [2].
3
1] Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany [2].
4
SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany.
5
Cellzome GmbH, Meyerhofstraße 1, 69117 Heidelberg, Germany.
6
Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany.
7
JPT Peptide Technologies GmbH, Volmerstraße 5, 12489 Berlin, Germany.
8
Institute of Pathology, Technische Universität München, Trogerstraße 18, 81675 München, Germany.
9
1] Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany [2] Center for Integrated Protein Science Munich, Germany.

Abstract

Proteomes are characterized by large protein-abundance differences, cell-type- and time-dependent expression patterns and post-translational modifications, all of which carry biological information that is not accessible by genomics or transcriptomics. Here we present a mass-spectrometry-based draft of the human proteome and a public, high-performance, in-memory database for real-time analysis of terabytes of big data, called ProteomicsDB. The information assembled from human tissues, cell lines and body fluids enabled estimation of the size of the protein-coding genome, and identified organ-specific proteins and a large number of translated lincRNAs (long intergenic non-coding RNAs). Analysis of messenger RNA and protein-expression profiles of human tissues revealed conserved control of protein abundance, and integration of drug-sensitivity data enabled the identification of proteins predicting resistance or sensitivity. The proteome profiles also hold considerable promise for analysing the composition and stoichiometry of protein complexes. ProteomicsDB thus enables navigation of proteomes, provides biological insight and fosters the development of proteomic technology.

PMID:
24870543
DOI:
10.1038/nature13319
[Indexed for MEDLINE]

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