PP2A docking motifs

The specificity of enzymes controlling the post-translation modification state of eukaryotic proteins is a highly active field of research. Numerous mechanism have evolved to promote spatial and temporal colocalization of enzyme and substrate and thereby decrease the likelihood of off-target modification or demodification. In the case of the PP2A-B56 holoenzyme the B56 subunit recognises short peptide docking motif in the disordered regions of their substrates. This resource provides information about experimentally characterised B56 docking motifs, and a suite of tools to predict novel docking motifs in a protein or proteomes of interest based on the sequence determinant of these experimentally characterised instances. The resource is a collaboration between the Nilsson Lab at the Novo Nordisk Foundation Center for Protein Research at the University of Copenhagen and the Davey Lab at The Institute Of Cancer Research (ICR).

This website is a part of a project to characterise the binding specificity and targets of the B56 subunit of PP2A. This project is described in:

Thrane Hertz EP*, Kruse T*, Davey NE, López-Méndez B, Otti Sigurðsson J, Montoya G, Olsen JV, Nilsson J.
"A conserved binding motif provides substrate specificity to the PP2A-B56 phosphatase"
Mol Cell. 2016 Aug 18;63(4):686-95.

Protein phosphatase 2 regulatory subunit B56 coloured by conservation (red denotes conserved).