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

Panayotis Vlastaridis | Zendy; Pelagia Kyriakidou | Zendy; Anargyros Chaliotis | Zendy; Yves Van de Peer | Zendy; Stephen G. Oliver | Zendy; Grigoris D. Amoutzias | Zendy

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

Author(s) -

Panayotis Vlastaridis,

Pelagia Kyriakidou,

Anargyros Chaliotis,

Yves Van de Peer,

Stephen G. Oliver,

Grigoris D. Amoutzias

Publication year - 2017

Publication title -

gigascience

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.947

H-Index - 54

ISSN - 2047-217X

DOI - 10.1093/gigascience/giw015

Subject(s) - phosphorylation , proteome , yeast , posttranslational modification , computational biology , arabidopsis , protein phosphorylation , biology , proteomics , microbiology and biotechnology , bioinformatics , chemistry , biochemistry , gene , enzyme , protein kinase a , mutant

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).

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