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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Main Authors: Kevin Drew, John B Wallingford, Edward M Marcotte
Format: Article
Language:English
Published: Wiley 2021-05-01
Series:Molecular Systems Biology
Subjects:
Online Access:https://doi.org/10.15252/msb.202010016
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spelling 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
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