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Found 12 result(s)

ProteomeXchange

PX

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The ProteomeXchange consortium has been set up to provide a single point of submission of MS proteomics data to the main existing proteomics repositories, and to encourage the data exchange between them for optimal data dissemination. Current members accepting submissions are: The PRIDE PRoteomics IDEntifications database at the European Bioinformatics Institute focusing mainly on shotgun mass spectrometry proteomics data PeptideAtlas/PASSEL focusing on SRM/MRM datasets.

Top Down Proteomics Repository

TDPR

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This database will provide a central location for scientists to browse uniquely observed proteoforms and to contribute their own datasets. Top-down proteomics is a method of protein identification that uses an ion trapping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry analysis.

cropPAL

Compendium of crop Proteins with Annotated Locations

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<<<!!!<<<This repository is no longer available>>>!!!>>>

Mass Spectrometry Interactive Virtual Environment

MassIVE

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MassIVE is a community resource developed by the NIH-funded Center for Computational Mass Spectrometry to promote the global, free exchange of mass spectrometry data. MassIVE datasets can be assigned ProteomeXchange accessions to satisfy publication requirements.

UniParc

UniProt Archive

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The UniProt Archive (UniParc) is a comprehensive and non-redundant database that contains most of the publicly available protein sequences in the world.

The Comprehensive Resource of Mammalian protein complexes

CORUM

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CORUM is a manually curated dataset of mammalian protein complexes. Annotation of protein complexes includes protein complex composition and other valuable information such as method of purification, cellular function of complexes or involvement in diseases.

UniMES

UniProt Metagenomic and Environmental Sequences

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<<<!!!<<< Retirement of UniProt Metagenomic and Environmental Sequences (UniMES): UniProt has retired UniMES as there is now a resource at the EBI that is dedicated to serving metagenomic researchers. Henceforth, we recommend using the EBI Metagenomics portal instead https://www.ebi.ac.uk/metagenomics/ . In addition to providing a repository of metagenomics sequence data, EBI Metagenomics allows you to view functional and taxonomic analyses and to submit your own samples for analysis. >>>!!!>>> The UniProt Metagenomic and Environmental Sequences (UniMES) database is a repository specifically developed for metagenomic and environmental data. We provide UniMES clusters in order to obtain complete coverage of sequence space at different resolutions.

PeptideAtlas

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The PeptideAtlas validates expressed proteins to provide eukaryotic genome data. Peptide Atlas provides data to advance biological discoveries in humans. The PeptideAtlas accepts proteomic data from high-throughput processes and encourages data submission.

Molecular INTeraction Database

MINT

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Starting September 2013, MINT uses the IntAct database infrastructure to limit the duplication of efforts and to optimise future software development. Data manually curated by the MINT curators can now be accessed from the IntAct homepage at the EBI. Data maintenance and release, MINT PSICQUIC and IMEx services are under the responsibility of the IntAct team, while curation effort will be carried by both groups. The MINT development team now focuses on two new developments: mentha that integrates protein interaction information curated by IMEx databases and SIGNOR a database of logic relationships between human proteins. MINT is a public repository for molecular interactions reported in peer-reviewed journals.IT is a collection of molecular interaction databases that can be used to search for, analyze and graphically display molecular interaction networks and pathways from a wide variety of species. MINT is comprised of separate database components. HomoMINT, is an inferred human protein interatction database. Domino, is database of domain peptide interactions. A new component has been added called VirusMINT that explores the interactions of viral proteins with human proteins.

CyberCell Database

CCDB

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The CyberCell database (CCDB) is a comprehensive collection of detailed enzymatic, biological, chemical, genetic, and molecular biological data about E. coli (strain K12, MG1655). It is intended to provide sufficient information and querying capacity for biologists and computer scientists to use computers or detailed mathematical models to simulate all or part of a bacterial cell at a nanoscopic (10-9 m), mesoscopic (10-8 m).The CyberCell database CCDB actually consists of 4 browsable databases: 1) the main CyberCell database (CCDB - containing gene and protein information), 2) the 3D structure database (CC3D – containing information for structural proteomics), 3) the RNA database (CCRD – containing tRNA and rRNA information), and 4) the metabolite database (CCMD – containing metabolite information). Each of these databases is accessible through hyperlinked buttons located at the top of the CCDB homepage. All CCDB sub-databases are fully web enabled, permitting a wide variety of interactive browsing, search and display operations. and microscopic (10-6 m) level.

Influenza Research Database

IRD

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<<<!!!<<< The migration of the data, tools, and services from the legacy IRD and ViPR applications to BV-BRC is now complete. All web traffic from the IRD and ViPR resources is also being forwarded to the BV-BRC home page https://www.re3data.org/repository/r3d100014100 >>>!!!>>>

DEPOD

DEPhOsphorylation Database

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DEPOD - the human DEPhOsphorylation Database (version 1.1) is a manually curated database collecting human active phosphatases, their experimentally verified protein and non-protein substrates and dephosphorylation site information, and pathways in which they are involved. It also provides links to popular kinase databases and protein-protein interaction databases for these phosphatases and substrates. DEPOD aims to be a valuable resource for studying human phosphatases and their substrate specificities and molecular mechanisms; phosphatase-targeted drug discovery and development; connecting phosphatases with kinases through their common substrates; completing the human phosphorylation/dephosphorylation network.