hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assemblies
Abstract A general principle of biology is the self‐assembly of proteins into functional complexes. Characterizing their composition is, therefore, required for our understanding of cellular functions. Unfortunately, we lack knowledge of the comprehensive set of identities of protein complexes in hu...
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Online Access: | https://doi.org/10.15252/msb.202010016 |
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doaj-8e1225f55bc0460da7ca3851b9582e1a2021-08-02T23:52:02ZengWileyMolecular Systems Biology1744-42922021-05-01175n/an/a10.15252/msb.202010016hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assembliesKevin Drew0John B Wallingford1Edward M Marcotte2Department of Molecular Biosciences Center for Systems and Synthetic Biology University of Texas Austin TX USADepartment of Molecular Biosciences Center for Systems and Synthetic Biology University of Texas Austin TX USADepartment of Molecular Biosciences Center for Systems and Synthetic Biology University of Texas Austin TX USAAbstract A general principle of biology is the self‐assembly of proteins into functional complexes. Characterizing their composition is, therefore, required for our understanding of cellular functions. Unfortunately, we lack knowledge of the comprehensive set of identities of protein complexes in human cells. To address this gap, we developed a machine learning framework to identify protein complexes in over 15,000 mass spectrometry experiments which resulted in the identification of nearly 7,000 physical assemblies. We show our resource, hu.MAP 2.0, is more accurate and comprehensive than previous state of the art high‐throughput protein complex resources and gives rise to many new hypotheses, including for 274 completely uncharacterized proteins. Further, we identify 253 promiscuous proteins that participate in multiple complexes pointing to possible moonlighting roles. We have made hu.MAP 2.0 easily searchable in a web interface (http://humap2.proteincomplexes.org/), which will be a valuable resource for researchers across a broad range of interests including systems biology, structural biology, and molecular explanations of disease.https://doi.org/10.15252/msb.202010016data integrationhuman protein complexesmass spectrometrymoonlighting proteins |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Kevin Drew John B Wallingford Edward M Marcotte |
spellingShingle |
Kevin Drew John B Wallingford Edward M Marcotte hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assemblies Molecular Systems Biology data integration human protein complexes mass spectrometry moonlighting proteins |
author_facet |
Kevin Drew John B Wallingford Edward M Marcotte |
author_sort |
Kevin Drew |
title |
hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assemblies |
title_short |
hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assemblies |
title_full |
hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assemblies |
title_fullStr |
hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assemblies |
title_full_unstemmed |
hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assemblies |
title_sort |
hu.map 2.0: integration of over 15,000 proteomic experiments builds a global compendium of human multiprotein assemblies |
publisher |
Wiley |
series |
Molecular Systems Biology |
issn |
1744-4292 |
publishDate |
2021-05-01 |
description |
Abstract A general principle of biology is the self‐assembly of proteins into functional complexes. Characterizing their composition is, therefore, required for our understanding of cellular functions. Unfortunately, we lack knowledge of the comprehensive set of identities of protein complexes in human cells. To address this gap, we developed a machine learning framework to identify protein complexes in over 15,000 mass spectrometry experiments which resulted in the identification of nearly 7,000 physical assemblies. We show our resource, hu.MAP 2.0, is more accurate and comprehensive than previous state of the art high‐throughput protein complex resources and gives rise to many new hypotheses, including for 274 completely uncharacterized proteins. Further, we identify 253 promiscuous proteins that participate in multiple complexes pointing to possible moonlighting roles. We have made hu.MAP 2.0 easily searchable in a web interface (http://humap2.proteincomplexes.org/), which will be a valuable resource for researchers across a broad range of interests including systems biology, structural biology, and molecular explanations of disease. |
topic |
data integration human protein complexes mass spectrometry moonlighting proteins |
url |
https://doi.org/10.15252/msb.202010016 |
work_keys_str_mv |
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1721225300084260864 |