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]
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]
The Mammal Species of the World (MSW) is a database of mammalian taxonomy. It is hoped that this database on the World Wide Web can be used as a convenient on-line reference for identifying or verifying recognized scientific names and for taxonomic research. The names are organized in a hierarchy that includes Order, Family, Subfamily, Genus and Species. ... [Information of the supplier]
Online Mendelian Inheritance in Animals (OMIA) is a database of genes, inherited disorders and traits in more than 135 animal species (other than human and mouse) authored by Professor Frank Nicholas of the University of Sydney, Australia, with help from many people over the years. The database contains textual information and references, as well as links to relevant PubMed and Gene records at the NCBI. ... [Information of the supplier]
At present, there are online zoology databases which detail all of the bird and mammal specimens in the collection. Electronic catalogues of a small collection of Charles Darwin's material, and the extinct and endangered species in the collections are also available. Work on the database of the human remanins in the collections is progressing. Currently there are approximately 500 records online. The database will be continuously updated. ... [Information of the supplier]
This educational Web site, designed to serve as a resource for students, teachers, and the general public interested in the biology and identification of mammals in North America, was developed by the External Affairs and Public Programs Division of the Smithsonian Institution's National Museum of Natural History. The resources we make available are derived from the Museum's unparalleled natural history collections, its scientific research, permanent and special exhibits, libraries, and through collaborations with other organizations and individuals with special resources to complement the site. This Web site includes detailed descriptions, images, and distribution ranges for more than 400 mammals native to the North American continent. The primary resources for the site have been based in the continental United States, but as the opportunity occurs, the site will be expanded to complete the species found in Canada and Mexico. ... [Information of the supplier]
SWISS-2DPAGE is an annotated two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) and SDS-PAGE database established in 1993 and maintained collaboratively by the Biomedical Proteomics Reasearch Group (BPRG) of the Geneva University and the Proteome Informatics Group of the Swiss Institute of Bioinformatics (SIB). The SWISS-2DPAGE database assembles data on proteins identified on various 2-D PAGE and SDS-PAGE maps. Each SWISS-2DPAGE entry contains textual data on one protein, including mapping procedures, physiological and pathological information, experimental data (isoelectric point, molecular weight, amino acid composition, peptide masses) and bibliographical references. In addition to this textual data, SWISS-2DPAGE provides several 2-D PAGE and SDS-PAGE images showing the experimentally determined location of the protein, as well as a theoretical region computed from the sequence protein, indicating where the protein might be found in the gel. Cross-references are provided to Medline and other federated databases. ... [Information of the supplier]
AACompIdent is a tool which allows the identification of a protein from its amino acid composition. It searches the Swiss-Prot and / or TrEMBL databases for proteins, whose amino acid compositions are closest to the amino acid composition given. [Information of the supplier]
This page allows you to test an antibody sequence against the Kabat sequence database. Any unusual residues (occurring in < 1% of chains in the database) will be reported to you. This allows the identification of potential cloning artifacts and sequencing errors. The current Kabat database contains 6014 light chains and 7895 heavy chains. ... [Information of the supplier]
CATH is a hierarchical classification of protein domain structures, which clusters proteins at four major levels, Class(C), Architecture(A), Topology(T) and Homologous superfamily (H).Class, derived from secondary structure content, is assigned for more than 90% of protein structures automatically. Architecture, which describes the gross orientation of secondary structures, independent of connectivities, is currently assigned manually. The topology level clusters structures into fold groups according to their topological connections and numbers of secondary structures. The homologous superfamilies cluster proteins with highly similar structures and functions. The assignments of structures to fold groups and homologous superfamilies are made by sequence and structure comparisons. The boundaries and assignments for each protein domain are determined using a combination of automated and manual procedures. These include computational techniques, empirical and statistical evidence, literature review and expert analysis. ... [Information of the supplier]