Phosphorylation is a widespread post-translational modification that modulates the function of a large number of proteins. Here we show that a significant proportion of all the domains in the human proteome are significantly enriched or depleted in phosphorylation events. A substantial improvement in phosphosites prediction is achieved by leveraging this observation, which has not been tapped by existing methods. Phosphorylation sites are often not shared between multiple occurrences of the same domain in the proteome, even when the phosphoacceptor residue is conserved. This is partly due to different functional constraints acting on the same domain in different protein contexts. Moreover, by augmenting domain alignments with structural information, we were able to provide direct evidence that phosphosites in protein-protein interfaces need not be positionally conserved, likely because they can modulate interactions simply by sitting in the same general surface area.

Palmeri, A., Ausiello, G., Ferre, F., HELMER CITTERICH, M., Gherardini, P. (2014). A proteome-wide Domain-centric Perspective on Protein Phosphorylation. MOLECULAR & CELLULAR PROTEOMICS [10.1074/mcp.M114.039990].

A proteome-wide Domain-centric Perspective on Protein Phosphorylation

AUSIELLO, GABRIELE;HELMER CITTERICH, MANUELA;Gherardini, PF
2014-05-15

Abstract

Phosphorylation is a widespread post-translational modification that modulates the function of a large number of proteins. Here we show that a significant proportion of all the domains in the human proteome are significantly enriched or depleted in phosphorylation events. A substantial improvement in phosphosites prediction is achieved by leveraging this observation, which has not been tapped by existing methods. Phosphorylation sites are often not shared between multiple occurrences of the same domain in the proteome, even when the phosphoacceptor residue is conserved. This is partly due to different functional constraints acting on the same domain in different protein contexts. Moreover, by augmenting domain alignments with structural information, we were able to provide direct evidence that phosphosites in protein-protein interfaces need not be positionally conserved, likely because they can modulate interactions simply by sitting in the same general surface area.
15-mag-2014
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/11 - BIOLOGIA MOLECOLARE
English
Con Impact Factor ISI
Protein-Protein Interactions*; Post-translational modifications*; Phosphorylation; Phosphoproteome; Bioinformatics; Protein Domains
Palmeri, A., Ausiello, G., Ferre, F., HELMER CITTERICH, M., Gherardini, P. (2014). A proteome-wide Domain-centric Perspective on Protein Phosphorylation. MOLECULAR & CELLULAR PROTEOMICS [10.1074/mcp.M114.039990].
Palmeri, A; Ausiello, G; Ferre, F; HELMER CITTERICH, M; Gherardini, P
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/87935
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