UniProtKB XML Format
How to cite this record FAIRsharing.org: UniProtKB XML Format; UniProtKB XML Format; DOI: https://doi.org/10.25504/FAIRsharing.zj850n; Last edited: Jan. 8, 2019, 1:37 p.m.; Last accessed: Aug 01 2021 11:38 p.m.
Record updated: March 15, 2018, 10:19 a.m. by The FAIRsharing Team.
Edits to 'https://fairsharing.org/FAIRsharing.zj850n' by 'The FAIRsharing Team' at 10:19, 15 Mar 2018 (approved): 'miriam_url' has been modified: Before: None After:
Edits to 'https://fairsharing.org/FAIRsharing.zj850n' by 'The FAIRsharing Team' at 21:32, 23 Oct 2016 (approved): 'description' has been modified: Before: "UniProtKB XML Format" is a standard, specialising in the fields described under "scope and data types", below. Until this entry is claimed, more information on this project can be found at http://www.uniprot.org/docs/uniprot.xsd. This text was generated automatically. If you work on the project responsible for "UniProtKB XML Format" then please consider helping us by claiming this record and updating it appropriately. After: XML Schema definition for the UniProtKB XML format.
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The Bacterial protein tYrosine Kinase database (BYKdb) contains computer-annotated BY-kinase sequences. The database web interface allows static and dynamic queries and provides integrated analysis tools including sequence annotation.
Dragon Antimicrobial Peptide Database
Dragon Antimicrobial Peptide Database is a manually curated database of known and putative antimicrobial peptides (AMPs). It covers both prokaryotes and eukaryotes organisms.
Eukaryotic Linear Motifs
This computational biology resource mainly focuses on annotation and detection of eukaryotic linear motifs (ELMs) by providing both a repository of annotated motif data and an exploratory tool for motif prediction. ELMs, or short linear motifs (SLiMs), are compact protein interaction sites composed of short stretches of adjacent amino acids.
Major Intrinsic Proteins Modification Database
This is a database of comparative protein structure models of the MIP (Major Intrinsic Protein) family of proteins. The MIPs have been identified from the completed genome sequence of organisms available at NCBI.
Protein-Chemical Structural Interactions
Protein-Chemical Structural Interactions provides information on the 3-dimensional chemical structures of protein interactions with low molecular weight.
UniPathway is a manually curated resource of metabolic pathways for the UniProtKB/Swiss-Prot knowledgebase. It provides a structured controlled vocabulary to describe the role of a protein in a metabolic pathway.
The UniProt Knowledgebase (UniProtKB) is the central hub for the collection of functional information on proteins, with accurate, consistent and rich annotation. In addition to capturing the core data mandatory for each UniProtKB entry (mainly, the amino acid sequence, protein name or description, taxonomic data and citation information), as much annotation information as possible is added. This includes widely accepted biological ontologies, classifications and cross-references, and clear indications of the quality of annotation in the form of evidence attribution of experimental and computational data. The UniProt Knowledgebase consists of two sections: a reviewed section containing manually-annotated records with information extracted from literature and curator-evaluated computational analysis (aka "UniProtKB/Swiss-Prot"), and an unreviewed section with computationally analyzed records that await full manual annotation (aka "UniProtKB/TrEMBL").
FlyMine is an integrated database of genomic, expression and protein data for Drosophila, Anopheles and C. elegans. Its main focus is genomic and proteomics data for Drosophila and other insects. It provides access to integrated data at a number of different levels, from browsing to construction of complex queries, which can be executed on either single items or lists.
MobiDB is a database of intrinsically disordered regions (IDRs) and related features from various sources and prediction tools. Different levels of reliability and different features are reported as different and independent annotations. The database features three levels of annotation: manually curated, indirect and predicted. MobiDB annotates the binding modes of disordered proteins, whether they undergo disorder-to-order transitions or remain disordered in the bound state. In addition, disordered regions undergoing liquid-liquid phase separation or post-translational modifications are defined.
InterMine was formed in 2002 at the University of Cambridge, originally as a Drosophila-dedicated resource, before expanding to become organism-agnostic, enabling a large range of organisations around the world to create their own InterMines. There are many instances of InterMine installations, relating to particular model organisms. These can be searched individually or via a cross-Mine search function.
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UniProt Consortium (Consortium)