The University of Southampton
University of Southampton Institutional Repository

Computational identification and analysis of protein short linear motifs

Davey, Norman E., Edwards, Richard J. and Shields, Denis C. (2010) Computational identification and analysis of protein short linear motifs Frontiers in Bioscience, 15, pp. 801-825.

Record type: Article


Short linear motifs (SLiMs) in proteins can act as targets for proteolytic cleavage, sites of post-translational modification, determinants of sub-cellular localization, and mediators of protein-protein interactions. Computational discovery of SLiMs involves assembling a group of proteins postulated to share a potential motif, masking out residues less likely to contain such a motif, down-weighting shared motifs arising through common evolutionary descent, and calculation of statistical probabilities allowing for the multiple testing of all possible motifs. Much of the challenge for motif discovery lies in the assembly and masking of datasets of proteins likely to share motifs, since the motifs are typically short (between 3 and 10 amino acids in length), so that potential signals can be easily swamped by the noise of stochastically recurring motifs. Focusing on disordered regions of proteins, where SLiMs are predominantly found, and masking out non-conserved residues can reduce the level of noise but more work is required to improve the quality of high-throughput experimental datasets (e.g. of physical protein interactions) as input for computational discovery.

PDF davey_edwards_shields_2010.pdf - Accepted Manuscript
Download (251kB)

More information

Published date: 1 June 2010


Local EPrints ID: 158235
ISSN: 1093-9946
PURE UUID: 753d61b3-d7c0-4cf9-8755-5d017e167083

Catalogue record

Date deposited: 16 Jun 2010 15:52
Last modified: 18 Jul 2017 12:39

Export record


Author: Norman E. Davey
Author: Richard J. Edwards
Author: Denis C. Shields

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton:

ePrints Soton supports OAI 2.0 with a base URL of

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.