Mitochondria are far more than the ‘powerhouses’ of eukaryotic cells producing the adenosine triphosphate necessary for life. Their metabolism is dictated by their proteome, which is dynamic, responding to signals and the physiology of the cell, and their metabolic role includes supplying intermediates for anabolic pathways that produce essential metabolites, and catabolic pathways for disposal or recycling of excess or toxic metabolites. Their role in signalling is now evident and they participate in cellular growth, differentiation and death.
Provides information about human mitochondrial proteins. The MPA database contains 911 unique protein entries associated with experimentally validated and referenced mitochondrial localization. This database includes other information as experimentally validated and referenced information defining structure, function, interactions with other mitochondrial protein atlas (MPA) proteins, and involvement in pathologies. It supplies a prototype for other information sources allowing a distinction between what has been confirmed and what remains to be verified.
An inventory of genes encoding mitochondrial-localized proteins and their expression across 14 mouse tissues. Using the same strategy we have now reconstructed this inventory separately for human and for mouse based on (i) improved gene transcript models, (ii) updated literature curation, including results from proteomic analyses of mitochondrial sub-compartments, (iii) improved homology mapping and (iv) updated versions of all seven original data sets. The updated human MitoCarta2.0 consists of 1158 human genes, including 918 genes in the original inventory as well as 240 additional genes. The updated mouse MitoCarta2.0 consists of 1158 genes, including 967 genes in the original inventory plus 191 additional genes. The improved MitoCarta 2.0 inventory provides a molecular framework for system-level analysis of mammalian mitochondria.
Provides information on the predicted and experimentally confirmed protein complement of mitochondria from the model plant Arabidopsis thaliana. AMPDB contains more than 29 100 proteins obtained from 17 public resources and represent about 500 unique identifications. It can be queried with a series of mitochondrial-specific characteristics such as targeting pre-sequence predictions, and orthology to yeast, human mitochondrial proteins and the mitochondrial progenitor Rickettsia.
An object-relational database of human mitochondrial protein sequences generated from information obtained from a comprehensive curation of public databases as well as from direct experimental evidence. Users may browse and search MitoProteome, and access a complete compilation of data relevant to each protein of interest, cross-linked to external databases.
Provides searchable information on the protein import apparatus of plant and non-plant mitochondria. An in silico analysis was carried out, comparing the mitochondrial protein import apparatus from 24 species representing various lineages from Saccharomyces cerevisiae (yeast) and algae to Homo sapiens (human) and higher plants, including Arabidopsis thaliana (Arabidopsis), Oryza sativa (rice) and other more recently sequenced plant species. Each of these species was extensively searched and manually assembled for analysis in the MPIC DB. The database presents an interactive diagram in a user-friendly manner, allowing users to select their import component of interest.
Provides a comprehensive knowledgebase for mitochondrial proteome, interactome and human diseases. MitProNet features a user-friendly graphic visualization interface to present functional analysis of linkage networks. As an up-to-date database and analysis platform, MitProNet should be particularly helpful in comprehensive studies of complicated biological mechanisms underlying mitochondrial functions and human mitochondrial diseases.
A large-scale relational database that is automatically updated to keep pace with advances in mitochondrial proteomics and is curated to assure that the designation of proteins as mitochondrial reflects gene ontology (GO) annotations supported by high-quality evidence codes. A set of postulates is proposed to help define which proteins are authentic components of mitochondria. A web interface is provided to permit members of the mitochondrial research community to suggest modifications in protein annotations or mitochondrial status.