Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes

dc.contributor.authorVlastaridis, Panayotis
dc.contributor.authorKyriakidou, Pelagia
dc.contributor.authorChaliotis, Anargyros
dc.contributor.authorVan de Peer, Yves
dc.contributor.authorOliver, Stephen G.
dc.contributor.authorAmoutzias, Grigoris D.
dc.date.accessioned2017-09-04T08:04:09Z
dc.date.available2017-09-04T08:04:09Z
dc.date.issued2017
dc.description.abstractBACKGROUND : Phosphorylation is the most frequent post-translational modification made to proteins and may regulate protein activity as either a molecular digital switch or a rheostat. Despite the cornucopia of high-throughput (HTP) phosphoproteomic data in the last decade, it remains unclear how many proteins are phosphorylated and how many phosphorylation sites (p-sites) can exist in total within a eukaryotic proteome. We present the first reliable estimates of the total number of phosphoproteins and p-sites for four eukaryotes (human, mouse, Arabidopsis, and yeast). RESULTS : In all, 187 HTP phosphoproteomic datasets were filtered, compiled, and studied along with two low-throughput (LTP) compendia. Estimates of the number of phosphoproteins and p-sites were inferred by two METHODS : Capture-Recapture, and fitting the saturation curve of cumulative redundant vs. cumulative non-redundant phosphoproteins/p-sites. Estimates were also adjusted for different levels of noise within the individual datasets and other confounding factors. We estimate that in total, 13 000, 11 000, and 3000 phosphoproteins and 230 000, 156 000, and 40 000 p-sites exist in human, mouse, and yeast, respectively, whereas estimates for Arabidopsis were not as reliable. CONCLUSIONS : Most of the phosphoproteins have been discovered for human, mouse, and yeast, while the dataset for Arabidopsis is still far from complete. The datasets for p-sites are not as close to saturation as those for phosphoproteins. Integration of the LTP data suggests that current HTP phosphoproteomics appears to be capable of capturing 70% to 95% of total phosphoproteins, but only 40% to 60% of total p-sites.en_ZA
dc.description.departmentGeneticsen_ZA
dc.description.librarianam2017en_ZA
dc.description.sponsorshipGDA acknowledges financial support from the “ARISTEIA II” Action of the ”OPERATIONAL PROGRAMME EDUCATION AND LIFELONG LEARNING” that is co-funded by the European Social Fund and National Resources (code 4288 to GDA). GDA acknowledges additional support by research grants from the Postgraduate Programme ‘Toxicology’ of the Dept. of Biochemistry and Biotechnology, School of Health Sciences, University of Thessaly, Greece. YVdP acknowledges the Multidisciplinary Research Partnership “Bioinformatics: from nucleotides to networks” Project (no. 01MR0310W) of Ghent University. SGO acknowledges the University of Cambridge for granting him Sabbatical Leave to permit him to work with GDA in the University of Thessaly, Greece.en_ZA
dc.description.urihttps://academic.oup.com/gigascienceen_ZA
dc.identifier.citationVlastaridis, P., Kyriakidou, P., Chaliotis, A., Van de Peer, Y., Oliver, S.G. & Amoutzias, G.D. 2017, 'Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes', GigaScience, vol. 6, no. 2, pp. 1-11.en_ZA
dc.identifier.issn2047-217X (online)
dc.identifier.other10.1093/gigascience/giw015
dc.identifier.urihttp://hdl.handle.net/2263/62174
dc.language.isoenen_ZA
dc.publisherOxford University Pressen_ZA
dc.rights© The Author 2017. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution License.en_ZA
dc.subjectCapture-recaptureen_ZA
dc.subjectCurve-fittingen_ZA
dc.subjectPhosphoproteomicsen_ZA
dc.subjectTotal number of phosphoproteinsen_ZA
dc.subjectTotal number of phosphorylation sitesen_ZA
dc.subjectYeasten_ZA
dc.subjectHumanen_ZA
dc.subjectMouseen_ZA
dc.subjectArabidopsisen_ZA
dc.subjectHigh-throughput (HTP)en_ZA
dc.subjectLow-throughput (LTP)en_ZA
dc.titleEstimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomesen_ZA
dc.typeArticleen_ZA

Files

Original bundle

Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
Vlastaridis_Estimating_2017.pdf
Size:
1.66 MB
Format:
Adobe Portable Document Format
Description:
Article

License bundle

Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
license.txt
Size:
1.75 KB
Format:
Item-specific license agreed upon to submission
Description: