Ontological visualization of protein-protein interactions.
BACKGROUND
Cellular processes require the interaction of many proteins across several cellular compartments. Determining the collective network of such interactions is an important aspect of understanding the role and regulation of individual proteins. The Gene Ontology (GO) is used by model organism databases and other bioinformatics resources to provide functional annotation of proteins. The annotation process provides a mechanism to document the binding of one protein with another. We have constructed protein interaction networks for mouse proteins utilizing the information encoded in the GO annotations. The work reported here presents a methodology for integrating and visualizing information on protein-protein interactions.


RESULTS
GO annotation at Mouse Genome Informatics (MGI) captures 1318 curated, documented interactions. These include 129 binary interactions and 125 interaction involving three or more gene products. Three networks involve over 30 partners, the largest involving 109 proteins. Several tools are available at MGI to visualize and analyze these data.


CONCLUSIONS
Curators at the MGI database annotate protein-protein interaction data from experimental reports from the literature. Integration of these data with the other types of data curated at MGI places protein binding data into the larger context of mouse biology and facilitates the generation of new biological hypotheses based on physical interactions among gene products.
Drabkin
Harold J
HJ
Mouse Genome Informatics, The Jackson Laboratory, Bar Harbor, ME, USA. hjd@informatics.jax.org
Hollenbeck
Christopher
C
Hill
David P
DP
Blake
Judith A
JA
D000818:Animals; D001665:Binding Sites; D003001:Cloning, Molecular; D019295:Computational Biology / Q000379:methods*; D030541:Databases, Genetic; D030562:Databases, Protein; D005796:Genes; D016678:Genome; D023281:Genomics; D006801:Humans; D016247:Information Storage and Retrieval; D051379:Mice; D008962:Models, Theoretical; D008967:Molecular Biology / Q000379:methods; D008968:Molecular Conformation; D010766:Phosphorylation; D011485:Protein Binding; D017510:Protein Folding; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry; D040901:Proteomics; D012984:Software
D011506:Proteins