Skip to Content
MilliporeSigma

Initial characterization of the human central proteome.

BMC systems biology (2011-01-29)
Thomas R Burkard, Melanie Planyavsky, Ines Kaupe, Florian P Breitwieser, Tilmann Bürckstümmer, Keiryn L Bennett, Giulio Superti-Furga, Jacques Colinge
ABSTRACT

On the basis of large proteomics datasets measured from seven human cell lines we consider their intersection as an approximation of the human central proteome, which is the set of proteins ubiquitously expressed in all human cells. Composition and properties of the central proteome are investigated through bioinformatics analyses. We experimentally identify a central proteome comprising 1,124 proteins that are ubiquitously and abundantly expressed in human cells using state of the art mass spectrometry and protein identification bioinformatics. The main represented functions are proteostasis, primary metabolism and proliferation. We further characterize the central proteome considering gene structures, conservation, interaction networks, pathways, drug targets, and coordination of biological processes. Among other new findings, we show that the central proteome is encoded by exon-rich genes, indicating an increased regulatory flexibility through alternative splicing to adapt to multiple environments, and that the protein interaction network linking the central proteome is very efficient for synchronizing translation with other biological processes. Surprisingly, at least 10% of the central proteome has no or very limited functional annotation. Our data and analysis provide a new and deeper description of the human central proteome compared to previous results thereby extending and complementing our knowledge of commonly expressed human proteins. All the data are made publicly available to help other researchers who, for instance, need to compare or link focused datasets to a common background.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
β-Galactosidase from Escherichia coli, suitable for enzyme immunoassay, lyophilized, powder, ~140 U/mg
Sigma-Aldrich
Inosine Monophosphate Dehydrogenase Type II human, recombinant, expressed in E. coli
Sigma-Aldrich
Malic Dehydrogenase from porcine heart, ≥600 units/mg protein (biuret), ammonium sulfate suspension
Sigma-Aldrich
L-Lactic Dehydrogenase from bovine heart, 1000 units/mL
Sigma-Aldrich
Acyl-coenzyme A Synthetase from Pseudomonas sp., ≥2 units/mg protein
Sigma-Aldrich
Glutamic-Pyruvic Transaminase from porcine heart, ammonium sulfate suspension, ≥75 units/mg protein
Sigma-Aldrich
Phospholipase D from cabbage, Type IV, lyophilized powder, ≥100 units/mg solid
Supelco
GAPDH, standard for protein electrophoresis
Sigma-Aldrich
Pyruvate Kinase from rabbit muscle, Type VII, buffered aqueous glycerol solution, 350-600 units/mg protein
Sigma-Aldrich
Phosphorylase a from rabbit muscle, lyophilized powder, 20-30 units/mg protein
Sigma-Aldrich
α-Glycerophosphate Dehydrogenase from rabbit muscle, Type I, ammonium sulfate suspension, 100-300 units/mg protein
Sigma-Aldrich
Glucose-6-phosphate Dehydrogenase from baker′s yeast (S. cerevisiae), Type XV, lyophilized powder, 200-400 units/mg protein (modified Warburg-Christian)
Sigma-Aldrich
Uridine-5′-diphosphoglucose pyrophosphorylase from baker′s yeast, Type X, lyophilized powder, ≥40 units/mg protein
Sigma-Aldrich
Phosphatase, Acid from potato, lyophilized powder, ≥0.5 unit/mg solid
Sigma-Aldrich
Glucose-6-phosphate Dehydrogenase from baker′s yeast (S. cerevisiae), Type VII, ammonium sulfate suspension, ≥200 units/mg protein
Sigma-Aldrich
Glyceraldehyde-3-phosphate Dehydrogenase from rabbit muscle, lyophilized powder, ≥75 units/mg protein
Sigma-Aldrich
β-Galactosidase from bovine liver, Grade III, lyophilized powder, ≥0.15 units/mg protein
Sigma-Aldrich
Phosphoglucomutase from rabbit muscle, ammonium sulfate suspension, ≥100 units/mg protein
Sigma-Aldrich
Glucose-6-phosphate Dehydrogenase from baker′s yeast (S. cerevisiae), Type IX, lyophilized powder, 200-400 units/mg protein (modified Warburg-Christian)
Sigma-Aldrich
Phospholipase A2 from honey bee venom (Apis mellifera), salt-free, lyophilized powder, 600-2400 units/mg protein
Sigma-Aldrich
β-Galactosidase from Escherichia coli, lyophilized powder, ≥500 units/mg protein
Sigma-Aldrich
Enolase from baker′s yeast (S. cerevisiae), lyophilized powder, ≥50 units/mg protein
Sigma-Aldrich
β-Galactosidase from Escherichia coli, aqueous glycerol suspension, ≥500 units/mg protein (biuret)
Sigma-Aldrich
L-Lactic Dehydrogenase from bovine heart, Type XVII, buffered aqueous glycerol solution, ≥400 units/mg protein
Sigma-Aldrich
Creatine Phosphokinase from bovine heart, Type III, salt-free, lyophilized powder, ≥30 units/mg protein
Sigma-Aldrich
Adenosine 5′-Triphosphatase from porcine cerebral cortex, lyophilized powder, ≥0.3 units/mg protein, pH 7.8
Sigma-Aldrich
L-Glutamine Synthetase from Escherichia coli, lyophilized powder, 400-2,000 units/mg protein
Sigma-Aldrich
β-Hydroxybutyrate Dehydrogenase from Rhodopseudomonas sphaeroides, Type V, lyophilized powder, 250-750 units/mg protein
Sigma-Aldrich
Fumarase from porcine heart, ammonium sulfate suspension, ≥300 units/mg protein (biuret)
Sigma-Aldrich
Hexokinase from Saccharomyces cerevisiae, lyophilized powder, ≥350 units/mg protein, Protein ≥10 % by biuret