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

ABSTRACT:

Background

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 m

SUBMITTER: Vlastaridis P 

PROVIDER: S-EPMC5466708 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature