Discovery of phosphorylation motif mixtures in phosphoproteomics data.

ABSTRACT:

Motivation

Modification of proteins via phosphorylation is a primary mechanism for signal transduction in cells. Phosphorylation sites on proteins are determined in part through particular patterns, or motifs, present in the amino acid sequence.

Results

We describe an algorithm that simultaneously discovers multiple motifs in a set of peptides that were phosphorylated by several different kinases. Such sets of peptides are routinely produced in proteomics experiments.Our motif-finding algorithm uses the principle of minimum description length to determine a mixture of sequence motifs that distinguish a foreground set of phosphopeptides from a background set of unphosphorylated peptides. We show that our algorithm outperforms existing motif-finding algorithms on synthetic dat

SUBMITTER: Ritz A 

PROVIDER: S-EPMC2638929 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature