MINT focuses on experimentally verified protein-protein interactions mined from the scientific literature by expert curators

Database for molecular interaction information integrated with various other bio-entity information, including pathways, diseases, gene ontology (GO) terms, species and molecular types. The information is obtained from several manually curated databases and automatic extraction from literature. There are protein-protein interaction, gene/protein regulation and protein-small molecule interaction information stored in the database. The interaction information is linked with relevant GO terms, pathway, disease and species names. Interactions are also linked to the PubMed IDs of the corresponding abstracts the interactions were obtained from. Manually curated molecular interaction information was obtained from BioGRID, IntAct, NCBI Gene, and STITCH database. Pathway related information was obtained from KEGG database, Pathway Interaction database and Reactome. Disease information was obtained from PharmGKB and KEGG database. Gene ontology terms and related information was obtained from Gene Ontology database and GOA database.

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 are 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.

A database that focuses on experimentally verified protein-protein interactions mined from the scientific literature by expert curators. The curated data can be analyzed in the context of the high throughput data and viewed graphically with the MINT Viewer. This collection of molecular interaction databases 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. VirusMINT explores the interactions of viral proteins with human proteins. The MINT connect viewer allows you to enter a list of proteins (e.g. proteins in a pathway) to retrieve, display and download a network with all the interactions connecting them.

The microbial protein interaction database (MPIDB) provides physical microbial interaction data. The interactions are manually curated from the literature or imported from other databases, and are linked to supporting experimental evidence, as well as evidences based on interaction conservation, protein complex membership, and 3D domain contacts.

The Database is a research and analysis tool developed at the University of Washington, in the Department of Pharmaceutics. It contains in vitro and in vivo information on drug interactions in humans from the following sources: * 9648 peer-reviewed journal articles referenced in PubMed * 102 New Drug Applications (NDAs) * 411 excerpts of FDA Prescribing Information * In-depth analyses of drug-drug interactions in the context of 40 diseases / co-morbidities. In addition, the database also provides PK Profiles of drugs, QT Prolongation data, including results of TQT studies from recent NDAs, as well as Regulatory Guidances and Editorial Summaries/Syntheses relevant to advances in the field of drug interactions. Access to the Database is licensed by UW Center for Commercialization (C4C) to organizations interested in in-depth information on drug interactions. The Database is particularly useful to scientists/clinicians working in drug discovery and drug development. Database users can search for information using several families of pre-formulated queries based on drug name, enzyme name, transporter name, therapeutic area, and more.

The database NPIDB (Nucleic acid Protein Interaction DataBase) contains information derived from structures of DNA-protein and RNA-protein complexes extracted from Protein Data Bank (PDB) (1932 complexes in the end of 2007). It is equipped with a web-interface and a set of tools for extracting biologically meaningful characteristics of complexes. They are committed to satisfy all potential database users in order to: 1. Provide an essential information on structural features of DNA-protein and RNA-protein interaction for the users who need to get acquainted with the problem. 2. Give an effective access to the reasonably structured information about all DNA-protein and RNA-protein complexes containing in PDB. 3. Allow all visitors a quick access to our own research.

The MIPS mammalian protein-protein interaction database (MPPI) is a new resource of high-quality experimental protein interaction data in mammals. The content is based on published experimental evidence that has been processed by human expert curators. It is a collection of manually curated high-quality PPI data collected from the scientific literature by expert curators. We took great care to include only data from individually performed experiments since they usually provide the most reliable evidence for physical interactions. To suit different users needs we provide a variety of interfaces to search the database: -Expert interface Simple but powerful boolean query language. -PPI search form Easy to use PPI search -Protein search Just find proteins of interest in the database Sponsors: This work is funded by a grant from the German Federal Ministry of Education and Research.

The MHC-Peptide Interaction Database version T (MPID-T) is a new generation database for sequence-structure-function information on T cell receptor/peptide/MHC interactions. It contains all structures of TcR/pMHC and pMHC complexes, with emphasis on the structural characterization of these complexes. MPID-T will facilitate the development of algorithms to predict whether a peptide sequence will bind to a specific MHC allele. The database has been populated with the data from the Protein Data Bank(PDB). The data from the PDB is manually verified and classified, after which each structure is analysed for atomic interactions relevant to MHC-Peptide complex.

a database of modulators of protein-protein interactions. It contains exclusively small molecules and therefore no peptides. The data are retrieved from the literature either peer reviewed scientific articles or world patents. A large variety of data is stored within IPPI-DB: structural, pharmacological, binding and activity profile, pharmacokinetic and cytotoxicity when available, as well as some data about the PPI targets themselves.

THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 2,2022. It is a repository of interactions found by Entangle and compiled into various tables for use by the RNA community. This data does not have a user interface, but data can be accessed in tables. It contains raw Excel/Access Databases and data processed into useful Figures for people who don't want to wade through the primary data. At present it contains informations from 42 PDBs.

Protein-Protein, Genetic, and Chemical Interactions for Brandao MM (2010):AtPIN: Arabidopsis thaliana protein interaction network. curated by BioGRID (https://thebiogrid.org); ABSTRACT: BACKGROUND: Protein-protein interactions (PPIs) constitute one of the most crucial conditions to sustain life in living organisms. To study PPI in Arabidopsis thaliana we have developed AtPIN, a database and web interface for searching and building interaction networks based on publicly available protein-protein interaction datasets. DESCRIPTION: All interactions were divided into experimentally demonstrated or predicted. The PPIs in the AtPIN database present a cellular compartment classification (C3) which divides the PPI into 4 classes according to its interaction evidence and subcellular localization. It has been shown in the literature that a pair of genuine interacting proteins are generally expected to have a common cellular role and proteins that have common interaction partners have a high chance of sharing a common function. In AtPIN, due to its integrative profile, the reliability index for a reported PPI can be postulated in terms of the proportion of interaction partners that two proteins have in common. For this, we implement the Functional Similarity Weight (FSW) calculation for all first level interactions present in AtPIN database. In order to identify target proteins of cytosolic glutamyl-tRNA synthetase (Cyt-gluRS) (AT5G26710) we combined two approaches, AtPIN search and yeast two-hybrid screening. Interestingly, the proteins glutamine synthetase (AT5G35630), a disease resistance protein (AT3G50950) and a zinc finger protein (AT5G24930), which has been predicted as target proteins for Cyt-gluRS by AtPIN, were also detected in the experimental screening. CONCLUSIONS: AtPIN is a friendly and easy-to-use tool that aggregates information on Arabidopsis thaliana PPIs, ontology, and sub-cellular localization, and might be a useful and reliable strategy to map protein-protein interactions in Arabidopsis. AtPIN can be accessed at http://bioinfo.esalq.usp.br/atpin.

A database of interactions between HIV-1 and human proteins published in the peer-reviewed literature. The goal is to provide a concise, yet detailed, summary of all known interactions of HIV-1 proteins with host cell proteins, other HIV-1 proteins, or proteins from disease organisms associated with HIV/AIDS. For each HIV-1 human protein interaction the following information is provided: * NCBI Reference Sequence (RefSeq) protein accession numbers. * NCBI Entrez Gene ID numbers. * Amino acids from each protein that are known to be involved in the interaction. * Brief description of the protein-protein interaction. * Keywords to support searching for interactions. * PubMed identification numbers (PMIDs) for all journal articles describing the interaction. In addition, all protein-protein interactions documented in the database are integrated into Entrez Gene records and listed in the ''HIV-1 protein interactions'' section of Entrez Gene reports. The database is also tightly linked to other databases through Entrez Gene, enabling users to search for an abundance of information related to HIV pathogenesis and replication.

A publicly accessible web-based database through which the interactions between a variety of chelating groups and various central metal ions in the active site of metalloproteins can be explored in detail. Additional information can also be retrieved including protein and inhibitor names, the amino acid residues coordinated to the central metal ion, and the binding affinity of the inhibitor for the target metalloprotein.

ABSTRACT

It contains the data of drug targets (gene names), uniprot identifiers, secondary linked data sources (e.g., PharmGKB), market drug name, chembl identifier, and pubchem compound identifier obtained from DGIdb.

Instructions:

Data were cleaned and duplicates were removed. Data were all categorical features.

Inspiration:

This dataset uploaded to U-BRITE for "DRG_DEPOT" summer 2023 team project. It is used for constructing R2G dataset, which will map drugs to their drug targets (gene -> protein = drug target)

Acknowledgements

Freshour SL, Kiwala S, Cotto KC, Coffman AC, McMichael JF, Song JJ, Griffith M, Griffith OL, Wagner AH. Integration of the Drug-Gene Interaction Database (DGIdb 4.0) with open crowdsource efforts. Nucleic Acids Res. 2021 Jan 8;49(D1):D1144-D1151. doi: 10.1093/nar/gkaa1084. PMID: 33237278; PMCID: PMC7778926.

https://www.dgidb.org/

U-BRITE last update date: 06/09/2023

A database for protein-nucleic acid interaction that provides various features of protein-nucleic acid interfaces. There are 2333 protein-nucleic acid PDB complexes, 9547 SCOP domains, and 9633 domain-nucleic acid interfaces in BIPA. BIPA also provides a multiple structural alignment of representative structures at the SCOP family level using the program SALIGN, and the structural alignments were further annotated using the program JOY to detect local environments of amino acids.

The dataset is a subset of the expert curated PPI dataset based on the proteins with an association to Alzheimer’s disease available from IntAct molecular interaction database https://www.ebi.ac.uk/intact/. The confidence level of each interaction is characterised by IntAct MI score.Dataset was downloaded from IntAct database version 4.2.6.

This dataset Druggable Genome Comprehensive Drug Targets is a selection of supplementary data from "The Druggable Genome: Evaluation of Drug Targets in Clinical Trials Suggests Major Shifts in Molecular Class and Indication" (2013) [PMID:24016212]. The comprehensive list includes 461 targets of approved drugs.

Link Function: information

A web-based database of protein interaction sites. PiSITE provides not only information of interaction sites of a protein from single PDB entry, but also information of interaction sites of a protein from multiple PDB entries including similar proteins. PiSite also provides a list of sociable proteins, proteins with multiple binding states and multiple binding partners.In PiSITE, the identification of the binding sites of protein chains is performed by searching the same proteins with different binding states in PDB at first, and then mapping those binding sites onto the query proteins. The database PiSITE provides real interaction sites of proteins using the complex structures in PDB. According to the progress of several structural genomic projects, we have a large amount of structural data in PDB. Consequently, we can observe different binding states of proteins in atomic resolutions, and can analyze actual interaction sites of proteins. It will lead better understandings of protein interaction sites in near future. Usual practice to identify the interaction site has been done using a representative complex in PDB. However, for the proteins with multiple partners, non-interaction sites identified by using a single complex structure is not enough, because some part of the non-binding sites may be involved in the interaction sites with another proteins. Therefore, the real interaction sites should be obtained by using all of the binding states in PDB. For the purpose, the identifications of the binding site in PiSITE are done by searching the same proteins with different binding sites in PDB at first, and then mapping the binding sites onto the query proteins. PiSITE also provides the lists of transient hub proteins, which we call sociable proteins to clarify the different of so-called hub proteins. The sociable proteins are identified as the proteins with multiple binding states and multiple binding partners. On the other hand, so-called hub proteins have been identified as the proteins at the hub position in protein-protein interaction networks obtained by large-scale experiments, but the definition of the hub proteins cannot differentiate transient hub proteins from stable ones, although the differentiation is critically important for the better understanding of protein interaction networks. In addition, the usual definition of hub proteins can contain supermolecules as hub proteins. The supermolecules can be identified as the proteins with a single binding state and multiple binding partners, which we call stable hub proteins.