Identification of Novel Phosphorylation Motifs Through an Integrative Computational and Experimental Analysis of the Human Phosphoproteome

• DOI: 10.4172/jpb.1000163
• Publication Date: 2011-02-23T01:41:20Z
• Authors: Ramars Amanchy
• Keywords: Phosphoserine; Sequence motif; Phosphorylation cascade; Proteome; Casein kinase 2; Structural motif

Protein phosphorylation occurs in certain sequence/structural contexts that are still incompletely understood. The amino acids surrounding the phosphorylated residues important determining binding of kinase to protein sequence. Upon these sequences also determine domains specifically bind sequences. Thus far, such 'motifs' have been identified through alignment a limited number well substrates. RESULTS: Experimentally determined sites from Human Reference Database were used identify 1,167 novel serine/threonine or tyrosine motifs using computational approach. We able statistically validate based on their enrichment known phosphopeptides datasets over phosphoserine/threonine/tyrosine peptides human proteome. There 299 found be significant. Several we computationally subsequently appeared large experimentally since initiated our analysis. Using peptide microarray platform, evaluated ability casein I phosphorylate subset discovered this study. Our results demonstrate it is feasible datasets. study establishes microarrays as platform for high throughput assays and validation consensus motifs. Finally, extended catalog should assist systematic networks signal transduction pathways.