Protein complexes conserved across species indicate processes that are core to cellular machinery (e.g. cell-cycle or DNA damage-repair complexes conserved across human and yeast). While numerous computational methods have been devised to identify complexes from the protein interaction (PPI) networks of individual species, these are severely limited by noise and errors (false positives) in currently available datasets. Our analysis using human and yeast PPI networks revealed that these methods missed several important complexes including those conserved between the two species (e.g. the MLH1-MSH2-PMS2-PCNA mismatch-repair complex). Here, we note that much of the functionalities of yeast complexes have been conserved in human complexes not only through sequence conservation of proteins but also of critical functional domains. Therefore, integrating information of domain conservation might throw further light on conservation patterns between yeast and human complexes.
Pubmed ID: 24564762 RIS Download
Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.
Open source database system and analysis tools for molecular interaction data. All interactions are derived from literature curation or direct user submissions. Direct user submissions of molecular interaction data are encouraged, which may be deposited prior to publication in a peer-reviewed journal. The IntAct Database contains (Jun. 2014): * 447368 Interactions * 33021 experiments * 12698 publications * 82745 Interactors IntAct provides a two-tiered view of the interaction data. The search interface allows the user to iteratively develop complex queries, exploiting the detailed annotation with hierarchical controlled vocabularies. Results are provided at any stage in a simplified, tabular view. Specialized views then allows "zooming in" on the full annotation of interactions, interactors and their properties. IntAct source code and data are freely available.
View all literature mentions