The Relationship between the UniProt Knowledgebase (UniProtKB) and the IntAct Molecular Interaction Databases

IntAct provides a freely available, open source database system and analysis tools for protein interaction data. All interactions are derived from literature curation or direct user submission and all experimental information relating to binary protein-protein
interactions is entered into the IntAct database by curators, via a web-based editor. Interaction information is added to the SUBUNIT comment and the RP line of the relevant publication within the UniProtKB entry. There may be a single INTERACTION comment present within a UniProtKB entry, which conveys information relevant to binary protein-protein interactions. This is automatically derived from the IntAct database and is updated on a triweekly basis. Interactions can be derived by any appropriate experimental method but must be confirmed by a second interaction if resulting from a single yeast2hybrid experiment. For large-scale experiments, interactions are considered if a high confidence score is assigned by the authors. The INTERACTION line contains a direct link to IntAct that provides detailed information for the experimental support. These lines are not changed manually and any discrepancy is reported to IntAct for updates. There is also a database crossreference line within the UniProtKB entry i.e.: DR IntAct _UniProtKB AC, which directs the user to additional interaction data for that molecule. 
UniProt is supported by grants from the National Institutes of Health, European Commission, Swiss Federal Government and PATRIC BRC.
IntAct is funded by the European Commission under FELICS, contract number 021902 (RII3) within the Research Infrastructure Action of the FP6 "Structuring the European Research Area" Programme

The Relationship between the UniProt Knowledgebase (UniProtKB) and the IntAct Molecular Interaction Databases

IntAct provides a freely available, open source database system and analysis tools for protein interaction data. All interactions are derived from literature curation or direct user submission and all experimental information relating to binary protein-protein
interactions is entered into the IntAct database by curators, via a web-based editor. Interaction information is added to the SUBUNIT comment and the RP line of the relevant publication within the UniProtKB entry. There may be a single INTERACTION comment present within a UniProtKB entry, which conveys information relevant to binary protein-protein interactions. This is automatically derived from the IntAct database and is updated on a triweekly basis. Interactions can be derived by any appropriate experimental method but must be confirmed by a second interaction if resulting from a single yeast2hybrid experiment. For large-scale experiments, interactions are considered if a high confidence score is assigned by the authors. The INTERACTION line contains a direct link to IntAct that provides detailed information for the experimental support. These lines are not changed manually and any discrepancy is reported to IntAct for updates. There is also a database crossreference line within the UniProtKB entry i.e.: DR IntAct _UniProtKB AC, which directs the user to additional interaction data for that molecule. 
UniProt is supported by grants from the National Institutes of Health, European Commission, Swiss Federal Government and PATRIC BRC.
IntAct is funded by the European Commission under FELICS, contract number 021902 (RII3) within the Research Infrastructure Action of the FP6 "Structuring the European Research Area" Programme

Integration of Biological Sources: Exploring the Case of Protein Homology

Data integration is a key issue in the domain of bioin- formatics, which deals with huge amounts of heteroge- neous biological data that grows and changes rapidly. This paper serves as an introduction in the field of bioinformatics and the biological concepts it deals with, and an exploration of the integration problems a bioinformatics scientist faces. We examine ProGMap, an integrated protein homology system used by bioin- formatics scientists at Wageningen University, and several use cases related to protein homology. A key issue we identify is the huge manual effort required to unify source databases into a single resource. Un- certain databases are able to contain several possi- ble worlds, and it has been proposed that they can be used to significantly reduce initial integration efforts. We propose several directions for future work where uncertain databases can be applied to bioinformatics, with the goal of furthering the cause of bioinformatics integration

MODBASE, a database of annotated comparative protein structure models and associated resources.

MODBASE (http://salilab.org/modbase) is a database of annotated comparative protein structure models. The models are calculated by MODPIPE, an automated modeling pipeline that relies primarily on MODELLER for fold assignment, sequence-structure alignment, model building and model assessment (http:/salilab.org/modeller). MODBASE currently contains 5,152,695 reliable models for domains in 1,593,209 unique protein sequences; only models based on statistically significant alignments and/or models assessed to have the correct fold are included. MODBASE also allows users to calculate comparative models on demand, through an interface to the MODWEB modeling server (http://salilab.org/modweb). Other resources integrated with MODBASE include databases of multiple protein structure alignments (DBAli), structurally defined ligand binding sites (LIGBASE), predicted ligand binding sites (AnnoLyze), structurally defined binary domain interfaces (PIBASE) and annotated single nucleotide polymorphisms and somatic mutations found in human proteins (LS-SNP, LS-Mut). MODBASE models are also available through the Protein Model Portal (http://www.proteinmodelportal.org/)

An integrated approach to the interpretation of Single Amino Acid Polymorphisms within the framework of CATH and Gene3D

Background: The phenotypic effects of sequence variations in protein-coding regions come about primarily via their effects on the resulting structures, for example by disrupting active sites or affecting structural stability. In order better to understand the mechanisms behind known mutant phenotypes, and predict the effects of novel variations, biologists need tools to gauge the impacts of DNA mutations in terms of their structural manifestation. Although many mutations occur within domains whose structure has been solved, many more occur within genes whose protein products have not been structurally characterized.Results: Here we present 3DSim (3D Structural Implication of Mutations), a database and web application facilitating the localization and visualization of single amino acid polymorphisms (SAAPs) mapped to protein structures even where the structure of the protein of interest is unknown. The server displays information on 6514 point mutations, 4865 of them known to be associated with disease. These polymorphisms are drawn from SAAPdb, which aggregates data from various sources including dbSNP and several pathogenic mutation databases. While the SAAPdb interface displays mutations on known structures, 3DSim projects mutations onto known sequence domains in Gene3D. This resource contains sequences annotated with domains predicted to belong to structural families in the CATH database. Mappings between domain sequences in Gene3D and known structures in CATH are obtained using a MUSCLE alignment. 1210 three-dimensional structures corresponding to CATH structural domains are currently included in 3DSim; these domains are distributed across 396 CATH superfamilies, and provide a comprehensive overview of the distribution of mutations in structural space.Conclusion: The server is publicly available at http://3DSim.bioinfo.cnio.es/. In addition, the database containing the mapping between SAAPdb, Gene3D and CATH is available on request and most of the functionality is available through programmatic web service access

A Linked Data Approach to Sharing Workflows and Workflow Results

A bioinformatics analysis pipeline is often highly elaborate, due to the inherent complexity of biological systems and the variety and size of datasets. A digital equivalent of the ‘Materials and Methods’ section in wet laboratory publications would be highly beneficial to bioinformatics, for evaluating evidence and examining data across related experiments, while introducing the potential to find associated resources and integrate them as data and services. We present initial steps towards preserving bioinformatics ‘materials and methods’ by exploiting the workflow paradigm for capturing the design of a data analysis pipeline, and RDF to link the workflow, its component services, run-time provenance, and a personalized biological interpretation of the results. An example shows the reproduction of the unique graph of an analysis procedure, its results, provenance, and personal interpretation of a text mining experiment. It links data from Taverna, myExperiment.org, BioCatalogue.org, and ConceptWiki.org. The approach is relatively ‘light-weight’ and unobtrusive to bioinformatics users