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A census of human soluble protein complexes.

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.

Pubmed ID: 22939629

Authors

  • Havugimana PC
  • Hart GT
  • Nepusz T
  • Yang H
  • Turinsky AL
  • Li Z
  • Wang PI
  • Boutz DR
  • Fong V
  • Phanse S
  • Babu M
  • Craig SA
  • Hu P
  • Wan C
  • Vlasblom J
  • Dar VU
  • Bezginov A
  • Clark GW
  • Wu GC
  • Wodak SJ
  • Tillier ER
  • Paccanaro A
  • Marcotte EM
  • Emili A

Journal

Cell

Publication Data

August 31, 2012

Associated Grants

  • Agency: Biotechnology and Biological Sciences Research Council, Id: BB/F00964X/1
  • Agency: Biotechnology and Biological Sciences Research Council, Id: BB/K004131/1
  • Agency: NIGMS NIH HHS, Id: DP1 GM106408
  • Agency: Canadian Institutes of Health Research, Id: MOP 82940
  • Agency: NIGMS NIH HHS, Id: R01 GM067779
  • Agency: NIGMS NIH HHS, Id: R01 GM076536
  • Agency: NIGMS NIH HHS, Id: R01 GM088624

Mesh Terms

  • Humans
  • Multiprotein Complexes
  • Protein Interaction Maps
  • Proteins
  • Proteomics
  • Tandem Mass Spectrometry