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NONCODE is an integrated knowledge database dedicated to non-coding RNAs (excluding tRNAs and rRNAs). Now, there are 16 species in NONCODE(human, mouse, cow, rat, chicken, fruitfly, zebrafish, celegans, yeast, Arabidopsis, chimpanzee, gorilla, orangutan, rhesus macaque, opossum and platypus).The source of NONCODE includes literature and other public databases. We searched PubMed using key words ‘ncrna’, ‘noncoding’, ‘non-coding’,‘no code’, ‘non-code’, ‘lncrna’ or ‘lincrna. We retrieved the new identified lncRNAs and their annotation from the Supplementary Material or web site of these articles. Together with the newest data from Ensembl , RefSeq, lncRNAdb and GENCODE were processed through a standard pipeline for each species.
RDP provides quality-controlled, aligned and annotated Bacterial and Archaeal 16S rRNA sequences, and Fungal 28S rRNA sequences, and a suite of analysis tools to the scientific community.
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BRENDA is the main collection of enzyme functional data available to the scientific community worldwide. The enzymes are classified according to the Enzyme Commission list of enzymes. It is available free of charge for via the internet (http://www.brenda-enzymes.org/) and as an in-house database for commercial users (requests to our distributor Biobase). The enzymes are classified according to the Enzyme Commission list of enzymes. Some 5000 "different" enzymes are covered. Frequently enzymes with very different properties are included under the same EC number. BRENDA includes biochemical and molecular information on classification, nomenclature, reaction, specificity, functional parameters, occurrence, enzyme structure, application, engineering, stability, disease, isolation, and preparation. The database also provides additional information on ligands, which function as natural or in vitro substrates/products, inhibitors, activating compounds, cofactors, bound metals, and other attributes.
The PRIDE PRoteomics IDEntifications database is a centralized, standards compliant, public data repository for proteomics data, including protein and peptide identifications, post-translational modifications and supporting spectral evidence. PRIDE encourages and welcomes direct user submissions of mass spectrometry data to be published in peer-reviewed publications.
The DIP database catalogs experimentally determined interactions between proteins. It combines information from a variety of sources to create a single, consistent set of protein-protein interactions. The data stored within the DIP database were curated, both, manually by expert curators and also automatically using computational approaches that utilize the the knowledge about the protein-protein interaction networks extracted from the most reliable, core subset of the DIP data. Please, check the reference page to find articles describing the DIP database in greater detail. The Database of Ligand-Receptor Partners (DLRP) is a subset of DIP (Database of Interacting Proteins). The DLRP is a database of protein ligand and protein receptor pairs that are known to interact with each other. By interact we mean that the ligand and receptor are members of a ligand-receptor complex and, unless otherwise noted, transduce a signal. In some instances the ligand and/or receptor may form a heterocomplex with other ligands/receptors in order to be functional. We have entered the majority of interactions in DLRP as full DIP entries, with links to references and additional information
MatrixDB is a freely available database focused on interactions established by extracellular proteins and polysaccharides. MatrixDB takes into account the multimetric nature of the extracellular proteins (e.g. collagens, laminins and thrombospondins are multimers). MatrixDB includes interaction data extracted from the literature by manual curation in our lab, and offers access to relevant data involving extracellular proteins provided by our IMEx partner databases through the PSICQUIC webservice, as well as data from the Human Protein Reference Database. MatrixDB is in charge of the curation of papers published in Matrix Biology since January 2009