IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v509y2014i7502d10.1038_nature13319.html
   My bibliography  Save this article

Mass-spectrometry-based draft of the human proteome

Author

Listed:
  • Mathias Wilhelm

    (Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany
    SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Judith Schlegl

    (SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Hannes Hahne

    (Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany)

  • Amin Moghaddas Gholami

    (Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany)

  • Marcus Lieberenz

    (SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Mikhail M. Savitski

    (Cellzome GmbH, Meyerhofstraße 1, 69117 Heidelberg, Germany)

  • Emanuel Ziegler

    (SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Lars Butzmann

    (SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Siegfried Gessulat

    (SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Harald Marx

    (Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany)

  • Toby Mathieson

    (Cellzome GmbH, Meyerhofstraße 1, 69117 Heidelberg, Germany)

  • Simone Lemeer

    (Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany)

  • Karsten Schnatbaum

    (JPT Peptide Technologies GmbH, Volmerstraße 5, 12489 Berlin, Germany)

  • Ulf Reimer

    (JPT Peptide Technologies GmbH, Volmerstraße 5, 12489 Berlin, Germany)

  • Holger Wenschuh

    (JPT Peptide Technologies GmbH, Volmerstraße 5, 12489 Berlin, Germany)

  • Martin Mollenhauer

    (Institute of Pathology, Technische Universität München, Trogerstraße 18, 81675 München, Germany)

  • Julia Slotta-Huspenina

    (Institute of Pathology, Technische Universität München, Trogerstraße 18, 81675 München, Germany)

  • Joos-Hendrik Boese

    (SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Marcus Bantscheff

    (Cellzome GmbH, Meyerhofstraße 1, 69117 Heidelberg, Germany)

  • Anja Gerstmair

    (SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Franz Faerber

    (SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany)

  • Bernhard Kuster

    (Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany
    Center for Integrated Protein Science Munich)

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.

Suggested Citation

  • Mathias Wilhelm & Judith Schlegl & Hannes Hahne & Amin Moghaddas Gholami & Marcus Lieberenz & Mikhail M. Savitski & Emanuel Ziegler & Lars Butzmann & Siegfried Gessulat & Harald Marx & Toby Mathieson , 2014. "Mass-spectrometry-based draft of the human proteome," Nature, Nature, vol. 509(7502), pages 582-587, May.
    • Handle: RePEc:nat:nature:v:509:y:2014:i:7502:d:10.1038_nature13319
    DOI: 10.1038/nature13319
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature13319
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature13319?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Angela Re & Levi Waldron & Alessandro Quattrone, 2016. "Control of Gene Expression by RNA Binding Protein Action on Alternative Translation Initiation Sites," PLOS Computational Biology, Public Library of Science, vol. 12(12), pages 1-25, December.
    2. Karl K. Krull & Syed Azmal Ali & Jeroen Krijgsveld, 2024. "Enhanced feature matching in single-cell proteomics characterizes IFN-γ response and co-existence of cell states," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. Nora Linscheid & Alberto Santos & Pi Camilla Poulsen & Robert W Mills & Kirstine Calloe & Ulrike Leurs & Johan Z Ye & Christian Stolte & Morten B Thomsen & Bo H Bentzen & Pia R Lundegaard & Morten S O, 2021. "Quantitative proteome comparison of human hearts with those of model organisms," PLOS Biology, Public Library of Science, vol. 19(4), pages 1-22, April.
    4. Xiaojuan Fan & Yun Yang & Chuyun Chen & Zefeng Wang, 2022. "Pervasive translation of circular RNAs driven by short IRES-like elements," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:509:y:2014:i:7502:d:10.1038_nature13319. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.