Organs and organelles represent core biological systems in mammals, but the diversity in protein composition remains unclear. Here, we combine subcellular fractionation with exhaustive tandem mass spectrometry-based shotgun sequencing to examine the protein content of four major organellar compartments (cytosol, membranes [microsomes], mitochondria and nuclei) in six organs (brain, heart, kidney, liver, lung and placenta) of the laboratory mouse, Mus musculus. Using rigorous statistical filtering and machine-learning methods, the subcellular localization of 3274 of the 4768 proteins identified was determined with high-confidence, including 1503 previously uncharacterized factors, while tissue-selectivity was evaluated by comparison to previously reported mRNA expression patterns. This molecular compendium, fully accessible via a searchable web-browser interface, serves as a reliable reference of the expressed tissue and organelle proteomes of a leading model mammal. ... [Information of the supplier]
Organelle DB compiles protein localization data from organisms spanning the eukaryotic kingdom and presents an organized catalog of the known protein constituents of more than 50 organelles, subcellular structures, and protein complexes. The data sets in Organelle DB encompass 138 organisms with emphasis on the major model systems: S. cerevisiae, A. thaliana, D. melanogaster, C. elegans, M. musculus, and human proteins as well. In particular, Organelle DB is a central repository of yeast protein localization data, incorporating results from both previous and current (ongoing) large-scale studies of protein localization in Saccharomyces cerevisiae. In addition, we have manually curated several recent subcellular proteomic studies for incorporation in Organelle DB. In total, Organelle DB is a singular resource consolidating our knowledge of the protein composition of eukaryotic organelles and subcellular structures. ... [Information of the supplier]
PenBase provides comprehensive information about penaeidin properties, function, diversity and nomenclature. PenBase contains a Database section that lists all known penaeidins by subgroup or shrimp species. (...) Antimicrobial peptides are major components of innate immunity that have been conserved in evolution and found in different phyla of the plant and animal kingdom. Antimicrobial peptides are often small cationic molecules widely distributed in the whole living kingdom where they participate to host defence reactions against invading microorganisms. They are known to be involved in the innate immune response of vertebrate, invertebrate and plant species, and they are thought to be essential in organisms which lack adaptive immunity. Penaeidins are members of a family of antimicrobial peptides, originally isolated from the shrimp Litopenaeus vannamei, which present both Gram-positive antibacterial and antifungal activities (Destoumieux et al, 1997). Penaeidins appear to be a family of antimicrobial peptides ubiquitous among penaeid shrimps where they are major actors of the immune response (Bachère et al., 2004). ... [Information of the supplier]
Protein phosphorylation is a post-translational modification that regulates an astonishing number of critical biological processes in multicellular organisms. Cellular protein phosphorylation is an enormously complex dynamic system: over 510 distinct protein kinases and 100 phosphoprotein phosphatases are encoded in the human genome, and upwards of 40% of cellular proteins may be phosphorylated during some stage of growth and differentiation. Many proteins are multiply phosphorylated on scores of sites, making it likely that there are minimally 100,000 distinct phosphorylation sites in the mammalian proteome. It is the intention of the scientists who are designing and implementing PhosphoSite to provide an accurate and comprehensive source of information about mammalian protein phosphorylation sites. Our goal is to identify and organize information about all in vivo phosphorylation sites in human and mouse proteomes and to provide information and resources that will facilitate phosphorylation research. PhosphoSite is a curated, sequence-oriented protein database dedicated to in vivo phosphorylation sites. Information in PhosphoSite version 1.0 includes: (a) The phosphorylated residue and its surrounding sequence. We consider this information to be the central, organizing feature of PhosphoSite. (b) Orthologous sites in other species; this should assist investigators in determining if a phosphorylation site in species A might also be phosphorylated in species B. (c) The location within domains and motifs; this should assist investigators in inferring possible biological functions of phosphorylation sites. (d) Links to other online resources including the Alliance for Cell Signaling, the Protein Kinase Resource, and Scansite. Scansite predicts likely sites for protein phosphorylation by particular kinases and likely sites for interaction with other signaling proteins. This information, based upon vitro data, will be highly complimentary to that provided by PhosphoSite. (e) Literature references which demonstrate the in vivo nature and significance of the phosphorylation site. (...) Curated information will come from literature reports as well as from high-throughput phosphosite discovery programs. Information extracted from the public domain will be freely available for educational users. Proprietary information from phosphorylation site discovery programs may be available on a subscription basis. Corporations will need to pay a reasonable yearly fee to legally access PhosphoSite. ... [Information of the supplier, modified]
PHYTOPROT ist eine Datenbank von Clustern pflanzlicher Proteine. Alle Proteinsequenzen von Pflanzen (inklusive Arabidopsis thaliana), die bei SwissProt/ TrEMBL verfügbar sind, wurden einem gegenseitigen Vergleich unterzogen und aufgrund dessen in Cluster verwandter Proteine gruppiert. Innerhalb jedes Clusters wurden die Sequenzen einer pyramidalen Klassifikation unterzogen. ... [Information des Anbieters, übersetzt]
The PRIDE PRoteomics IDEntifications database is a centralized, standards compliant, public data repository for proteomics data. It has been developed to provide the proteomics community with a public repository for protein and peptide identifications together with the evidence supporting these identifications. [Information of the supplier]
PROSITE is a database of protein families and domains. It consists of biologically significant sites, patterns and profiles that help to reliably identify to which known protein family (if any) a new sequence belongs. [Information of the supplier]
Der ExPASy (Expert Protein Analysis System) Proteomics Server des Schweizerischen Instituts für Bioinformatik (SIB) widmet sich der Analyse von Protein-Sequenzen und -Strukturen sowie 2-D PAGE. [Information des Anbieters, übersetzt]
SNAPPI-DB ist eine objektorientierte Datenbank von Interaktionen zwischen Proteindomänen, die anhand von Strukturdaten festgestellt wurden. Die Strukturdaten stammen aus dem MSD Data Warehouse, denn die MSD liefert konsistente Daten mit zahlreichen Links zu verschiedenen Typen von Daten über Proteine und Aminosäuren. ... [Information des Anbieters, übersetzt]
Proteomik ist eine sehr junge Forschungsrichtung mit einer sehr viel älteren Wurzel: der Proteinanalytik. Diese befaßt sich mit der Aufklärung von molekularen Eigenschaften wie Aminosäuresequenz, dreidimensionale Struktur und biologische Aktivität individueller Proteine. Untersuchungsgegenstand der Proteomik ist demgegenüber die Gesamtheit aller Proteine in einer biologischen Probe im Moment der Untersuchung und bei den dafür gültigen Bedingungen. Dafür wurde vor etwa 7 Jahren der Begriff "Proteom" geprägt. Die DGPF versteht sich als Plattform, um die in Deutschland an verschiedenen Standorten und im Rahmen unterschiedlicher Programme angelaufenen Proteomik-Aktivitäten unter einem Dach zusammenzuführen und darüber hinaus die Proteomforschung durch national und international abgestimmte Initiativen voranzubringen. Durch eine übergreifende Koordination soll eine Bündelung und optimale Nutzung der nationalen Forschungs-kapazitäten herbeigeführt werden, um im weltweiten Wettbewerb an führender Stelle bestehen zu können. ... [Information des Anbieters]
