|Title||A million peptide motifs for the molecular biologist.|
|Publication Type||Journal Article|
|Year of Publication||2014|
|Authors||Tompa, P., N. E. Davey, T. J. Gibson, and M. M Babu|
|Date Published||2014 Jul 17|
|Keywords||Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Humans, Molecular Biology, Molecular Sequence Data, Protein Binding, Protein Interaction Domains and Motifs, Protein Processing, Post-Translational, Proteins|
A molecular description of functional modules in the cell is the focus of many high-throughput studies in the postgenomic era. A large portion of biomolecular interactions in virtually all cellular processes is mediated by compact interaction modules, referred to as peptide motifs. Such motifs are typically less than ten residues in length, occur within intrinsically disordered regions, and are recognized and/or posttranslationally modified by structured domains of the interacting partner. In this review, we suggest that there might be over a million instances of peptide motifs in the human proteome. While this staggering number suggests that peptide motifs are numerous and the most understudied functional module in the cell, it also holds great opportunities for new discoveries.
|Alternate Journal||Mol. Cell|
|Grant List||MC_U105185859 / / Medical Research Council / United Kingdom|
A million peptide motifs for the molecular biologist.