Two highly detailed maps of the human proteome released at same time

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  • Published: May 29, 2014
  • Author: Steve Down
  • Channels: Raman / Infrared Spectroscopy / MRI Spectroscopy / UV/Vis Spectroscopy / Chemometrics & Informatics / Proteomics / Atomic / NMR Knowledge Base / X-ray Spectrometry / Base Peak

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Two independent research collaborations have released highly detailed maps of the human proteome in the same publication, identifying a high proportion of the proteins encoded by the human genome. They will help efforts worldwide in the search for new biomarkers of disease. Both methods relied on mass spectrometry to deliver the results, which have been released in public databases.

In the first report, 17 types of adult tissue, 7 foetal tissues and 6 samples of primary haematopoietic cells were analysed by high-resolution to produce 25 million tandem mass spectra from about 2000 runs. They led to the identification of proteins that are encoded by 17,294 genes, included 2861 protein isoforms, corresponding to 84% of the genome.

Around 16 million MS/MS spectra did not correspond to annotated proteins so they were examined by a unique process which uncovered 808 novel protein-coding regions of the genome.

The results are available online at the Human Proteome Map.

The second group collected 16,857 tandem mass spectra from human tissues, cell lines and body fluids and combined the results with data from colleagues and other repositories in a public database called ProteomicsDB. It held details of proteins for 18,097 of the 19,629 human genes in SwissProt and 19,376 of the 86,771 protein isoforms in UniProt.

The functional profiles of 27 tissues and body fluids were generated and a principal components analysis revealed that the proteomes from one tissue and its cell lines are largely equivalent, while being different to those of other tissue types. This finding supports the use of human cell lines as model systems.

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