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

Mass-spectrometry-based draft of the human proteome

Mathias Wilhelm  1 , Judith Schlegl  2 , Hannes Hahne  3 , Amin Moghaddas Gholami  3 , Marcus Lieberenz  4 , Mikhail M Savitski  5 , Emanuel Ziegler  4 , Lars Butzmann  4 , Siegfried Gessulat  4 , Harald Marx  6 , Toby Mathieson  5 , Simone Lemeer  6 , Karsten Schnatbaum  7 , Ulf Reimer  7 , Holger Wenschuh  7 , Martin Mollenhauer  8 , Julia Slotta-Huspenina  8 , Joos-Hendrik Boese  4 , Marcus Bantscheff  5 , Anja Gerstmair  4 , Franz Faerber  4 , Bernhard Kuster  9
Affiliations

Mass-spectrometry-based draft of the human proteome

Mathias Wilhelm et al. Nature. .

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.

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