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A census of human soluble protein complexes |
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| Authors: | Pierre C Havugimana G Traver Hart Tamás Nepusz Haixuan Yang Andrei L Turinsky Zhihua Li Peggy I Wang Daniel R Boutz Vincent Fong Sadhna Phanse Mohan Babu Stephanie A Craig Pingzhao Hu Cuihong Wan James Vlasblom Vaqaar-Un-Nisa Dar Alexandr Bezginov Gregory W Clark Gabriel C Wu Shoshana J Wodak Elisabeth R M Tillier Alberto Paccanaro Edward M Marcotte Andrew Emili |
| Institution: | 1 Banting and Best Department of Medical Research, Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada 2 Department of Molecular Genetics, Medical Sciences Building, University of Toronto, Toronto, Ontario M5S 3E1, Canada 3 Department of Biochemistry, Medical Sciences Building, University of Toronto, Toronto, Ontario M5S 3E1, Canada 4 Department of Computer Science, Royal Holloway, University of London, Egham TW20 0EX, UK 5 Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada 6 Center for Systems and Synthetic Biology, Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA 7 Campbell Family Institute for Cancer Research, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario M5G 1L7, Canada |
| Abstract: | Cellular processes often depend on stable physical associations between proteins. Despite recent progress, knowledge of the composition of human protein complexes remains limited. To close this gap, we applied an integrative global proteomic profiling approach, based on chromatographic separation of cultured human cell extracts into more than one thousand biochemical fractions that were subsequently analyzed by quantitative tandem mass spectrometry, to systematically identify a network of 13,993 high-confidence physical interactions among 3,006 stably associated soluble human proteins. Most of the 622 putative protein complexes we report are linked to core biological processes and encompass both candidate disease genes and unannotated proteins to inform on mechanism. Strikingly, whereas larger multiprotein assemblies tend to be more extensively annotated and evolutionarily conserved, human protein complexes with five or fewer subunits are far more likely to be functionally unannotated or restricted to vertebrates, suggesting more recent functional innovations. |
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