Ontology highlight
ABSTRACT:
SUBMITTER: Woodsmith J
PROVIDER: S-EPMC3591266 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Woodsmith Jonathan J Kamburov Atanas A Stelzl Ulrich U
PLoS computational biology 20130307 3
Post-translational modifications (PTMs) regulate protein activity, stability and interaction profiles and are critical for cellular functioning. Further regulation is gained through PTM interplay whereby modifications modulate the occurrence of other PTMs or act in combination. Integration of global acetylation, ubiquitination and tyrosine or serine/threonine phosphorylation datasets with protein interaction data identified hundreds of protein complexes that selectively accumulate each PTM, indi ...[more]