title: A million peptide motifs for the molecular biologist.
abstract: 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.
authors.affiliation: VIB Structural Biology Research Center (SBRC), Vrije Universiteit Brussel, Brussels 1050, Belgium; Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest 1519, Hungary. Electronic address: ptompa@vub.ac.be.
authors.forename: Peter
authors.initials: P
authors.lastname: Tompa
authors.affiliation: Department of Physiology, University of California, San Francisco, San Francisco, CA 94158, USA.
authors.forename: Norman E
authors.initials: NE
authors.lastname: Davey
authors.affiliation: Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
authors.forename: Toby J
authors.initials: TJ
authors.lastname: Gibson
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: madanm@mrc-lmb.cam.ac.uk.
authors.forename: M Madan
authors.initials: MM
authors.lastname: Babu
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D006801:Humans; D008967:Molecular Biology; D008969:Molecular Sequence Data; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins