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PaxDb, a Database of Protein Abundance Averages Across All Three Domains of Life

Although protein expression is regulated both temporally and spatially, most proteins have an intrinsic, “typical” range of functionally effective abundance levels. These extend from a few molecules per cell for signaling proteins, to millions of molecules for structural proteins. When addressing fu...

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Autores principales: Wang, M., Weiss, M., Simonovic, M., Haertinger, G., Schrimpf, S. P., Hengartner, M. O., von Mering, C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Biochemistry and Molecular Biology 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412977/
https://www.ncbi.nlm.nih.gov/pubmed/22535208
http://dx.doi.org/10.1074/mcp.O111.014704
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author Wang, M.
Weiss, M.
Simonovic, M.
Haertinger, G.
Schrimpf, S. P.
Hengartner, M. O.
von Mering, C.
author_facet Wang, M.
Weiss, M.
Simonovic, M.
Haertinger, G.
Schrimpf, S. P.
Hengartner, M. O.
von Mering, C.
author_sort Wang, M.
collection PubMed
description Although protein expression is regulated both temporally and spatially, most proteins have an intrinsic, “typical” range of functionally effective abundance levels. These extend from a few molecules per cell for signaling proteins, to millions of molecules for structural proteins. When addressing fundamental questions related to protein evolution, translation and folding, but also in routine laboratory work, a simple rough estimate of the average wild type abundance of each detectable protein in an organism is often desirable. Here, we introduce a meta-resource dedicated to integrating information on absolute protein abundance levels; we place particular emphasis on deep coverage, consistent post-processing and comparability across different organisms. Publicly available experimental data are mapped onto a common namespace and, in the case of tandem mass spectrometry data, re-processed using a standardized spectral counting pipeline. By aggregating and averaging over the various samples, conditions and cell-types, the resulting integrated data set achieves increased coverage and a high dynamic range. We score and rank each contributing, individual data set by assessing its consistency against externally provided protein-network information, and demonstrate that our weighted integration exhibits more consistency than the data sets individually. The current PaxDb-release 2.1 (at http://pax-db.org/) presents whole-organism data as well as tissue-resolved data, and covers 85,000 proteins in 12 model organisms. All values can be seamlessly compared across organisms via pre-computed orthology relationships.
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spelling pubmed-34129772012-08-10 PaxDb, a Database of Protein Abundance Averages Across All Three Domains of Life Wang, M. Weiss, M. Simonovic, M. Haertinger, G. Schrimpf, S. P. Hengartner, M. O. von Mering, C. Mol Cell Proteomics Technological Innovation and Resources Although protein expression is regulated both temporally and spatially, most proteins have an intrinsic, “typical” range of functionally effective abundance levels. These extend from a few molecules per cell for signaling proteins, to millions of molecules for structural proteins. When addressing fundamental questions related to protein evolution, translation and folding, but also in routine laboratory work, a simple rough estimate of the average wild type abundance of each detectable protein in an organism is often desirable. Here, we introduce a meta-resource dedicated to integrating information on absolute protein abundance levels; we place particular emphasis on deep coverage, consistent post-processing and comparability across different organisms. Publicly available experimental data are mapped onto a common namespace and, in the case of tandem mass spectrometry data, re-processed using a standardized spectral counting pipeline. By aggregating and averaging over the various samples, conditions and cell-types, the resulting integrated data set achieves increased coverage and a high dynamic range. We score and rank each contributing, individual data set by assessing its consistency against externally provided protein-network information, and demonstrate that our weighted integration exhibits more consistency than the data sets individually. The current PaxDb-release 2.1 (at http://pax-db.org/) presents whole-organism data as well as tissue-resolved data, and covers 85,000 proteins in 12 model organisms. All values can be seamlessly compared across organisms via pre-computed orthology relationships. The American Society for Biochemistry and Molecular Biology 2012-08 2012-04-24 /pmc/articles/PMC3412977/ /pubmed/22535208 http://dx.doi.org/10.1074/mcp.O111.014704 Text en © 2012 by The American Society for Biochemistry and Molecular Biology, Inc. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles
spellingShingle Technological Innovation and Resources
Wang, M.
Weiss, M.
Simonovic, M.
Haertinger, G.
Schrimpf, S. P.
Hengartner, M. O.
von Mering, C.
PaxDb, a Database of Protein Abundance Averages Across All Three Domains of Life
title PaxDb, a Database of Protein Abundance Averages Across All Three Domains of Life
title_full PaxDb, a Database of Protein Abundance Averages Across All Three Domains of Life
title_fullStr PaxDb, a Database of Protein Abundance Averages Across All Three Domains of Life
title_full_unstemmed PaxDb, a Database of Protein Abundance Averages Across All Three Domains of Life
title_short PaxDb, a Database of Protein Abundance Averages Across All Three Domains of Life
title_sort paxdb, a database of protein abundance averages across all three domains of life
topic Technological Innovation and Resources
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412977/
https://www.ncbi.nlm.nih.gov/pubmed/22535208
http://dx.doi.org/10.1074/mcp.O111.014704
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