Abstract
CORUM is a database that provides a manually curated repository of experimentally characterized protein complexes from mammalian organisms, mainly human (67%), mouse (15%) and rat (10%). Given the vital functions of these macromolecular machines, their identification and functional characterization is foundational to our understanding of normal and disease biology. The new CORUM 3.0 release encompasses 4274 protein complexes offering the largest and most comprehensive publicly available dataset of mammalian protein complexes. The CORUM dataset is built from 4473 different genes, representing 22% of the protein coding genes in humans. Protein complexes are described by a protein complex name, subunit composition, cellular functions as well as the literature references. Information about stoichiometry of subunits depends on availability of experimental data. Recent developments include a graphical tool displaying known interactions between subunits. This allows the prediction of structural interconnections within protein complexes of unknown structure. In addition, we present a set of 58 protein complexes with alternatively spliced subunits. Those were found to affect cellular functions such as regulation of apoptotic activity, protein complex assembly or define cellular localization. CORUM is freely accessible at http://mips.helmholtz-muenchen.de/corum/.
Highlights
Understanding biological processes at cellular and system levels is an important task in all living organisms
For functional annotation of protein complexes, we offer a mapping to Gene Ontology (GO) terms since CORUM 2.0
In articles used for CORUM, we found only 288 protein complexes with stoichiometry data
Summary
Understanding biological processes at cellular and system levels is an important task in all living organisms. Protein complexes play critical roles in an array of biological processes, including protein synthesis, signaling and cellular degradation processes. There are no reliable estimates about the total number of protein complexes in cells (complexome), but data from single cell organisms provide evidence that more than half of the gene products are involved in the formation of protein complexes [1]. According to estimates from Berggard et al [2], even more than 80% of proteins work in complexes. Many proteins are subunits of more than one complex, which extends the number of potential protein complexes. The RING-box protein 1 (RBX1), that was present in 35 protein complexes in the 2009 release of CORUM [3], is found in 65 protein complexes
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