APID database: redefining protein-protein interaction experimental evidences and binary interactomes.
Diego Alonso-López, Francisco J Campos-Laborie, Miguel A Gutiérrez, Luke Lambourne, Michael A Calderwood, Marc Vidal, Javier De Las Rivas
Author Information
Diego Alonso-López: Cancer Research Center (CiC-IBMCC, CSIC/USAL/IBSAL), Consejo Superior de Investigaciones Científicas and University of Salamanca, Salamanca, Spain.
Francisco J Campos-Laborie: Cancer Research Center (CiC-IBMCC, CSIC/USAL/IBSAL), Consejo Superior de Investigaciones Científicas and University of Salamanca, Salamanca, Spain.
Miguel A Gutiérrez: Cancer Research Center (CiC-IBMCC, CSIC/USAL/IBSAL), Consejo Superior de Investigaciones Científicas and University of Salamanca, Salamanca, Spain.
Luke Lambourne: Center for Cancer Systems Biology, Department of Cancer Biology, Dana-Farber Cancer Institute and Department of Genetics, Harvard Medical School, Boston, MA, USA.
Michael A Calderwood: Center for Cancer Systems Biology, Department of Cancer Biology, Dana-Farber Cancer Institute and Department of Genetics, Harvard Medical School, Boston, MA, USA.
Marc Vidal: Center for Cancer Systems Biology, Department of Cancer Biology, Dana-Farber Cancer Institute and Department of Genetics, Harvard Medical School, Boston, MA, USA.
Javier De Las Rivas: Cancer Research Center (CiC-IBMCC, CSIC/USAL/IBSAL), Consejo Superior de Investigaciones Científicas and University of Salamanca, Salamanca, Spain.
The collection and integration of all the known protein-protein physical interactions within a proteome framework are critical to allow proper exploration of the protein interaction networks that drive biological processes in cells at molecular level. APID Interactomes is a public resource of biological data (http://apid.dep.usal.es) that provides a comprehensive and curated collection of `protein interactomes' for more than 1100 organisms, including 30 species with more than 500 interactions, derived from the integration of experimentally detected protein-to-protein physical interactions (PPIs). We have performed an update of APID database including a redefinition of several key properties of the PPIs to provide a more precise data integration and to avoid false duplicated records. This includes the unification of all the PPIs from five primary databases of molecular interactions (BioGRID, DIP, HPRD, IntAct and MINT), plus the information from two original systematic sources of human data and from experimentally resolved 3D structures (i.e. PDBs, Protein Data Bank files, where more than two distinct proteins have been identified). Thus, APID provides PPIs reported in published research articles (with traceable PMIDs) and detected by valid experimental interaction methods that give evidences about such protein interactions (following the `ontology and controlled vocabulary': www.ebi.ac.uk/ols/ontologies/mi; developed by `HUPO PSI-MI'). Within this data mining framework, all interaction detection methods have been grouped into two main types: (i) `binary' physical direct detection methods and (ii) `indirect' methods. As a result of these redefinitions, APID provides unified protein interactomes including the specific `experimental evidences' that support each PPI, indicating whether the interactions can be considered `binary' (i.e. supported by at least one binary detection method) or not.
