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. 2000 Jan 1;28(1):155-8.
doi: 10.1093/nar/28.1.155.

MITOP, the mitochondrial proteome database: 2000 update

C Scharfe  1 , P Zaccaria, K Hoertnagel, M Jaksch, T Klopstock, M Dembowski, R Lill, H Prokisch, K D Gerbitz, W Neupert, H W Mewes, T Meitinger
Affiliations

MITOP, the mitochondrial proteome database: 2000 update

C Scharfe et al. Nucleic Acids Res. .

Abstract

MITOP (http://www.mips.biochem.mpg.de/proj/medgen/mitop/) is a comprehensive database for genetic and functional information on both nuclear- and mitochondrial-encoded proteins and their genes. The five species files--Saccharomyces cerevisiae, Mus musculus, Caenorhabditis elegans, Neurospora crassa and Homo sapiens--include annotated data derived from a variety of online resources and the literature. A wide spectrum of search facilities is given in the overlapping sections 'Gene catalogues', 'Protein catalogues', 'Homologies', 'Pathways and metabolism' and 'Human disease catalogue' including extensive references and hyperlinks to other databases. Central features are the results of various homology searches, which should facilitate the investigations into interspecies relationships. Precomputed FASTA searches using all the MITOP yeast protein entries and a list of the best human EST hits with graphical cluster alignments related to the yeast reference sequence are presented. The orthologue tables with cross-listings to all the protein entries for each species in MITOP have been expanded by adding the genomes of Rickettsia prowazeckii and Escherichia coli. To find new mitochondrial proteins the complete yeast genome has been analyzed using the MITOPROT program which identifies mitochondrial targeting sequences. The 'Human disease catalogue' contains tables with a total of 110 human diseases related to mitochondrial protein abnormalities, sorted by clinical criteria and age of onset. MITOP should contribute to the systematic genetic characterization of the mitochondrial proteome in relation to human disease.

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Figures

Figure 1
Figure 1
Estimated number of mitochondria-related proteins in human and yeast, current and candidate protein entries in MITOP.
Figure 2
Figure 2
In silico approach for identification of nuclear gene defects in human mitochondriopathies. The human SURF1 protein is highly homologous to the yeast SHY1 protein which is necessary for the maintenance of cytochrome-c-oxidase activity and respiration.
See this image and copyright information in PMC

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