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| Resource Name | Proper Citation | Abbreviations | Resource Type |
Description |
Keywords | Resource Relationships | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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A Classification of Mobile genetic Elements Resource Report Resource Website 10+ mentions |
A Classification of Mobile genetic Elements (RRID:SCR_001694) | ACLAME | data or information resource, database | A database dedicated to the collection and classification of mobile genetic elements (MGEs) from various sources, comprising all known phage genomes, plasmids and transposons. In addition to provide information on the full genomes and genetic entities, it aims at building a comprehensive classification of the functional modules of MGE's at the protein, gene, and higher levels. Prophinder, a tool dedicated to the detection of prophages in sequenced bacterial genomes, is available on ACLAME. | mobile genetic element, phage genome, plasmid, virus, prophage, transposon, protein, gene, classification, data analysis service, prophage prediction, bio.tools, FASEB list |
is listed by: OMICtools is listed by: bio.tools is listed by: Debian has parent organization: Free University of Brussels; Brussels; Belgium is parent organization of: MeGO |
ESTEC contract ESTEC 16370/02/NL/CK | PMID:19933762 PMID:14681355 |
THIS RESOURCE IS NO LONGER IN SERVICE | nif-0000-02533, OMICS_01528, biotools:aclame | https://bio.tools/aclame | SCR_001694 | ACLAME: A CLAssification of Mobile genetic Elements | 2026-09-19 12:56:31 | 33 | ||||
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GlycoMod Resource Report Resource Website 100+ mentions |
GlycoMod (RRID:SCR_001602) | GlycoMod | analysis service resource, data analysis service, production service resource, service resource | A tool that can predict the possible oligosaccharide structures that occur on proteins from their experimentally determined masses. This is done by comparing the mass of the glycan to a list of pre-computed masses of glycan compositions. The program can be used with free or derivatised glycans and for glycopeptides where the peptide mass or protein is known. Compositional constraints can be applied to the output. Note: You can use GlycanMass to calculate the mass of an oligosaccharide structure from its oligosaccharide composition. | predict, oligosaccharide structure, protein, mass, oligosaccharide, glycopeptide, glycoprotein, oligosaccharide composition, mass spectrometry, glycosylation, composition, glycan, structure, n-linked oligosaccharide, o-linked oligosaccharide, monosaccharide residue | has parent organization: ExPASy Bioinformatics Resource Portal | PMID:11680880 | Free, Freely available | nlx_153859 | SCR_001602 | GlycoMod Tool | 2026-09-19 12:56:31 | 117 | ||||||
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GlyProt Resource Report Resource Website 10+ mentions |
GlyProt (RRID:SCR_001560) | GlyProt | analysis service resource, data analysis service, production service resource, service resource | Web-based tool that enables meaningful N-glycan conformations to be attached to all the spatially accessible potential N-glycosylation sites of a known three-dimensional (3D) protein structure. The 3D structure of protein is required as input. Potential N-glysylations site are automatically detected. The attached glycan are constructed with SWEET-II, http://www.glycosciences.de/modeling/sweet2/doc/index.php | glycosylation, protein, in silico, 3d structure, protein structure, glycan, n-glycan, glycoprotein, bio.tools |
is listed by: bio.tools is listed by: Debian is related to: Research Collaboratory for Structural Bioinformatics Protein Data Bank (RCSB PDB) is related to: SWEET-DB has parent organization: glycosciences.de |
DFG | PMID:15980456 | THIS RESOURCE IS NO LONGER IN SERVICE | biotools:glyprot, nlx_152875 | https://bio.tools/glyprot | http://www.glycosciences.de/glyprot/ | SCR_001560 | GlyProt - In Silico Glycosylation of Proteins | 2026-09-19 12:56:30 | 39 | |||
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MitoMiner Resource Report Resource Website 50+ mentions |
MitoMiner (RRID:SCR_001368) | data or information resource, database | A database of mitochondrial proteomics data. It includes two sets of proteins: the MitoMiner Reference Set, which has 10477 proteins from 12 species; and MitoCarta, which has 2909 proteins from mouse and human mitochondrial proteins. MitoMiner provides annotation from the Gene Ontology (GO) and UniProt databases. This reference set contains all proteins that are annotated by either of these resources as mitochondrial in any of the species included in MitoMiner. MitoMiner data via is available via Application Programming Interface (API). The client libraries are provided in Perl, Python, Ruby and Java. | mitochondrion, proteomics, function, homolog, proteome, protein expression, mass-spectrometry, protein, metabolism, green fluorescent protein tag, ortholog, FASEB list |
uses: HomoloGene uses: UniProt uses: KEGG uses: OMIM uses: The Human Protein Atlas uses: Gene Ontology |
MRC | PMID:22121219 PMID:19208617 |
Public, Acknowledgement requested, Code: | nlx_152504 | SCR_001368 | MitoMiner - A database of the mitochondrial proteome | 2026-09-19 12:56:30 | 78 | ||||||
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big-PI Predictor Resource Report Resource Website 50+ mentions |
big-PI Predictor (RRID:SCR_001599) | big-PI Predictor | analysis service resource, data analysis service, production service resource, service resource | Prediction tool locating potential GPI-modification sites in precursor sequences applied for large-scale protein sequence database searches. The composite prediction function (with separate parametrization for metazoan and protozoan proteins) consists of terms evaluating both amino acid type preferences at sequence positions near a supposed omega-site as well as the concordance with general physical properties encoded in multi-residue correlation within the motif sequence. The latter terms are especially successful in rejecting non-appropriate sequences from consideration. The algorithm has been validated with a self-consistency and two jack-knife tests for the learning set of fully annotated sequences from the SWISS-PROT database as well as with a newly created database big-Pi (more than 300 GPI-motif mutations extracted from original literature sources). The accuracy of predicting the effect of mutations in the GPI sequence motif was above 83 %. | prediction, glycoprotein, protein, glycosylphosphatidylinositol, genome annotation, target selection, FASEB list | has parent organization: University of Vienna; Vienna; Austria | PMID:10497036 PMID:10871885 |
Free, Freely available | nlx_153855 | http://www.embl.de/beisenha/gpi/gpi_p%20rediction.html | SCR_001599 | big-PI Predictor: GPI Modification Site Prediction | 2026-09-19 12:56:30 | 59 | |||||
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CORUM Resource Report Resource Website 100+ mentions |
CORUM (RRID:SCR_002254) | CORUM | data or information resource, database |
Database of manually annotated protein complexes from mammalian organisms. Annotation includes protein complex function, localization, subunit composition, literature references and more. All information is obtained from individual experiments published in scientific articles, but data from high-throughput experiments is excluded. The majority of protein complexes in CORUM originates from man (65%), followed by mouse (14%) and rat (14%)., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025. |
mammalian protein, protein, protein complex, protein function, FASEB list |
is listed by: OMICtools is related to: Interaction Reference Index is related to: ConsensusPathDB has parent organization: Institute of Bioinformatics and Systems Biology; Neuherberg; Germany |
BMBF 031U212C | PMID:19884131 PMID:17965090 |
THIS RESOURCE IS NO LONGER IN SERVICE | nif-0000-02688, OMICS_01904, r3d100011272 | http://mips.gsf.de/genre/proj/corum | SCR_002254 | CORUM the Comprehensive Resource of Mammalian protein complexes, CORUM - the Comprehensive Resource of Mammalian protein complexes | 2026-09-19 12:56:34 | 164 | ||||
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Spliceosome Database Resource Report Resource Website 10+ mentions |
Spliceosome Database (RRID:SCR_002097) | Spliceosome Database | data or information resource, database | A database of proteins and RNAs that have been identified in various purified splicing complexes. Various names, orthologs and gene identifiers of spliceosome proteins have been cataloged to navigate the complex nomenclature of spliceosome proteins. Links to gene and protein records are also provided for the spliceosome components in other databases. To navigate spliceosome assembly dynamics, tools were created to compare the association of spliceosome proteins with complexes that form at specific stages of spliceosome assembly based on a compendium of mass spectrometry experiments that identified proteins in purified splicing complexes. | splicing, mass spectrometry, protein, rna, complex, spliceosome, small nuclear rna, structure, dynamics, ortholog, gene |
is listed by: OMICtools has parent organization: University of California at Santa Cruz; California; USA |
PMID:23118483 | Free, Freely available | OMICS_01891 | SCR_002097 | Spliceosome Database - A source of information for the SLPICEOSOME: The large ribonucleoprotein complex responsible for pre-mRNA splicing, Spliceosome Component Database | 2026-09-19 12:56:33 | 15 | ||||||
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PTMcode Resource Report Resource Website 10+ mentions |
PTMcode (RRID:SCR_002046) | PTMCode | data or information resource, database | Database of known and predicted functional associations between protein posttranslational modifications (PTMs) within proteins. In its first release it contains 13 different PTM types. PTM types are abbreviated in a two letter code as: Ph (phosphorylation), NG (N-linked glycosylation), Ac (acetylation), OG (O-linked glycosylation), Ub (ubiquitination), Me (methylation), SM (SUMOylation), Hy (hydroxylation), Ca (carboxylation), Pa (palmitoylation), Su (sulfation), Ni (nitrosylation) and CG (C-linked glycosylation). These PTMs are present in 25,765 proteins of 8 different eukaryotes. The database is focused on the exploration of the global post-translational regulation of proteins, not only by describing the set of its modifications, but by identifying the functional associations among the PTMs present in the protein. To do that, they combine five different evidence channels based on a literature survey, the modified residue co-evolution, their structural proximity, their competition for the same residue and the location within PTM highly-enriched protein regions (hotspots) and show the functional associations within the context of the protein architecture. | protein posttranslational modification, protein, function, phosphorylation, n-linked glycosylation, acetylation, o-linked glycosylation, ubiquitination, methylation, sumoylation, hydroxylation, carboxylation, palmitoylation, sulfation, nitrosylation, c-linked glycosylation |
is listed by: OMICtools has parent organization: European Molecular Biology Laboratory |
PMID:23193284 | Free, Freely available | OMICS_01915 | SCR_002046 | 2026-09-19 12:56:32 | 13 | |||||||
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WD repeat Family of Proteins Resource Report Resource Website |
WD repeat Family of Proteins (RRID:SCR_002160) | data or information resource, database | THIS RESOURCE IS NO LONGER IN SERVICE, documented on August 26, 2016. This website contains a library of WD-repeat containing proteins in which the repeats appear as multi-aligned sets. WD-repeat-containing proteins are those that contain 4 or more copies of the WD-repeat (tryptophan-aspartate repeat), a sequence motif approximately 31 amino acids long, that encodes a structural repeat. This repeat is described by the following profile, where x is ANY amino acid. By clicking on each high-lighted character you will obtain the distribution of amino acids found at that position of the repeat among an aligned set of WD-repeat containing proteins. The tertiary structure of only one member of this family has been determined, that of the G protein beta subunit, which contains 7 WD-repeats. Each of the 7 repeats folds into a small antiparallel beta-sheet. The over-lines above indicate the position of these strands, with a being the strand closest to the central pore and d at the external surface of the folded protein. These sheets are arranged around a central pseudosymmetry axis into a beta propeller. The WD-repeat-containing proteins form a very large family that is diverse in both its function and domain structure. Within all these proteins the WD-repeat domains are thought to have two common features: the domain folds into a beta propeller; and the domains form a platform without any catalytic activity on which multiple protein complexes assemble reversibly. The fact that these proteins play such key roles in the formation of protein-protein complexes in nearly all the major pathways and organelles unique to eukaryotic cells has two important implications. It supports both their ancient and proto eukaryotic origins and supports a likely association with many genetic diseases. | eukaryotic, function, genetic, align, amino acid, ancient, antiparallel, aspartate, beta, cell, disease, domain, g protein, multi-aligned, organelle, origin, pathway, propeller, protein, proto, pseudosymmetry, sheet, structural, tertiary, tryptophan, wd-repeat | THIS RESOURCE IS NO LONGER IN SERVICE | nif-0000-20949 | SCR_002160 | WD repeat Family of Proteins | 2026-09-19 12:56:34 | 0 | |||||||||
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TcoF Resource Report Resource Website 10+ mentions |
TcoF (RRID:SCR_002158) | TcoF | data or information resource, database | Database that facilitates the exploration of proteins involved in the regulation of transcription in humans by binding to regulatory DNA regions (transcription factors) and proteins involved in the regulation of transcription in humans by interacting with transcription factors and not binding to regulatory DNA regions (transcription co-factors). | protein, regulation, transcription, transcription factor, transcription co-factor, bio.tools |
is listed by: OMICtools is listed by: bio.tools is listed by: Debian has parent organization: King Abdullah University of Science and Technology; Makkah Province; Saudi Arabia |
PMID:20965969 | THIS RESOURCE IS NO LONGER IN SERVICE | biotools:tcof-db, OMICS_01865 | https://bio.tools/tcof-db | SCR_002158 | Dragon Database for Human Transcription Co-Factors and Transcription Factor Interacting Proteins, TcoF-DB, TcoF - Dragon database of transcription co-factors and transcription factor interacting proteins | 2026-09-19 12:56:34 | 10 | |||||
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Genome Network Platform Resource Report Resource Website 10+ mentions |
Genome Network Platform (RRID:SCR_001737) | GNP | data or information resource, database | THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 23,2022. Integrated database of experiment data generated by participating research institutes and public databases relating to: 1) transcription starting position of human genes in the human genome, 2) conjunction to control region on transcriptional factors and the human genome 3) protein-protein interaction with a central focus on transcription factors organized for use in genome level research. Gene Search is the function to search the integrated database by using keywords and public IDs. The search results can be visualized by: * Genome Explorer : provides annotation of landmarks (genes, transcription start sites, etc.) aligned in accordance with their genome locations. * PPI Network : provides a graphical view of protein-protein interaction (PPI) network from the experimental data generated under the project and the public datasets. * Expression Profile : clusters genes by expression pattern and display the result with heatmap. The function provides genes which have relation of coregulation and anti-coregulation. * Comparison Viewer : This function gives the view to compare the genomic regions between human and mouse homologous genes. The viewer shows the distribution of transcription start sites (TSS) as the way of separable by tissues or time points with other landmarks on genome region. * Gene Stock : This is the function to save the gene list that you are interested until the session is closed. | gene, genome, chip, human, interaction, micro array, protein, protein-protein interaction, qrt-pcr, rat, rna, sequence, short rna, tiling array, transcription, transcription control, transcription factor, transcription starting position, yeast two hybrid, data set, cage, data analysis service |
is listed by: 3DVC has parent organization: National Institute of Genetics; Shizuoka; Japan |
PMID:24927841 | Free, Freely Available | nif-0000-10237 | http://genomenetwork.nig.ac.jp/index_e.html | SCR_001737 | 2026-09-19 12:56:31 | 20 | ||||||
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ASPicDB Resource Report Resource Website 1+ mentions |
ASPicDB (RRID:SCR_002102) | ASPicDB | data or information resource, database | A database to access reliable annotations of the alternative splicing pattern of human genes, obtained by ASPic algorithm (Castrignano et al. 2006), and to the functional annotation of predicted isoforms. Users may select and extract specific sets of data related to genes, transcripts and introns fulfilling a combination of user-defined criteria. Several tabular and graphical views of the results are presented, providing a comprehensive assessment of the functional implication of alternative splicing in the gene set under investigation. ASPicDB also includes information on tissue-specific splicing patterns of normal and cancer cells, based on available EST data and their library source annotation. | annotation, splicing pattern, gene, transcript, intron, protein, variant, alternative splicing, splicing, blast, exon, u2, u12, isoform |
is listed by: OMICtools is listed by: SoftCite has parent organization: University of Bari; Bari; Italy |
Normal, Cancer | PMID:21051348 PMID:18388144 |
Free, Freely available | OMICS_01882 | http://srv00.ibbe.cnr.it/ASPicDB/ | SCR_002102 | Alternative Splicing Prediction Data Base, ASPicDB - A Database tool for alternative splicing analysis | 2026-09-19 12:56:33 | 8 | ||||
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AutoPSI database of predicted SCOP classifications Resource Report Resource Website |
AutoPSI database of predicted SCOP classifications (RRID:SCR_001923) | data or information resource, database | Searchable database for predicted protein sequences and structures. It has the ability to search through PDB ID, UniProt ID, and descriptive classifiers. | protein, structure, sequence, database, search, uniprot | has parent organization: Ludwig-Maximilians-University; Munich; Germany | Ludwig Maximilians Universitat Munchen | PMID:17932066 | THIS RESOURCE IS NO LONGER IN SERVICE | nif-0000-02588 | SCR_001923 | Automated Protein Structure Identification (AutoPSI) database, AutoPSI, AutoPSI Database, Automated Protein Structure Identification database | 2026-09-19 12:56:32 | 0 | ||||||
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TissueNet - The Database of Human Tissue Protein-Protein Interactions Resource Report Resource Website 10+ mentions |
TissueNet - The Database of Human Tissue Protein-Protein Interactions (RRID:SCR_002052) | TissueNet | data or information resource, database | Database of human tissue protein-protein interactions (PPIs) that associates each interaction with human tissues that express both pair mates. This was achieved by integrating current data of experimentally detected PPIs with extensive data of gene and protein expression across 16 main human tissues. Users can query TissueNet using a protein and retrieve its PPI partners per tissue, or using a PPI and retrieve the tissues expressing both pair mates. The graphical representation of the output highlights tissue-specific and tissue-wide PPIs. Thus, TissueNet provides a unique platform for assessing the roles of human proteins and their interactions across tissues. | protein-protein interaction, protein, tissue, adipose, adrenal, brain, breast, colon, heart, kidney, liver, lung, lymph node, ovary, prostate, skeletal muscle, testis, thyroid, white blood cell, protein expression, dna-microarray |
is listed by: OMICtools is related to: Biological General Repository for Interaction Datasets (BioGRID) is related to: Database of Interacting Proteins (DIP) is related to: IntAct is related to: MINT has parent organization: Ben-Gurion University of the Negev; Beer-Sheva; Israel |
PMID:23193266 | THIS RESOURCE IS NO LONGER IN SERVICE | OMICS_01913 | SCR_002052 | 2026-09-19 12:56:32 | 27 | |||||||
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Arabidopsis Nucleolar Protein Database Resource Report Resource Website 1+ mentions |
Arabidopsis Nucleolar Protein Database (RRID:SCR_001793) | AtNoPDB | data or information resource, database, image | Database of proteins found in the nucleoli of Arabidopsis, identified through proteomic analysis. The Arabidopsis Nucleolar Protein database (AtNoPDB) provides information on the plant proteins in comparison to human and yeast proteins, and images of cellular localizations for over a third of the proteins. A proteomic analysis was carried out of nucleoli purified from Arabidopsis cell cultures and to date 217 proteins have been identified. Many proteins were known nucleolar proteins or proteins involved in ribosome biogenesis. Some proteins, such as spliceosomal and snRNP proteins, and translation factors, were unexpected. In addition, proteins of unknown function which were either plant-specific or conserved between human and plant, and proteins with differential localizations were identified. | image, plant protein, plant, protein, homologue, blast, human proteome, orthologue, human, yeast, cell culture, blast, nucleolar protein | has parent organization: James Hutton Institute; Scotland; United Kingdom | Scottish Executive Environment and Rural Affairs Department ; BBSRC |
PMID:15608277 | THIS RESOURCE IS NO LONGER IN SERVICE | nif-0000-02562 | SCR_001793 | AtNoPDB Database | 2026-09-19 12:56:31 | 7 | |||||
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Interaction Reference Index Resource Report Resource Website 10+ mentions |
Interaction Reference Index (RRID:SCR_002085) | iRefIndex | data or information resource, database | An index of protein interactions available in a number of primary interaction databases including BIND, BioGRID, CORUM, DIP, HPRD, IntAct, MINT, MPact, MPPI and OPHID. This index includes multiple interaction types including physical and genetic (mapped to their corresponding protein products) as determined by a multitude of methods. This index allows the user to search for a protein and retrieve a non-redundant list of interactors for that protein. iRefIndex uses the Sequence Global Unique Identifier (SEGUID) to group proteins and interactions into redundant groups. This method allows users to integrate their own data with the iRefIndex in a way that ensures proteins with the exact same sequence will be represented only once. iRefIndex project has three long term objectives: # to facilitate exchange of interaction data between interaction databases. # to consolidate interaction data from multiple sources. # to provide feedback to source interaction databases. iRefIndex is made available in a number of formats: MITAB tab-delimited text files, iRefWeb interface, iRefScape plugin for Cytoscape, PSICQUIC Web services, and an interface for the R programming language environment. | genetic, interaction, protein, protein interaction, protein-protein interaction |
is related to: BIND is related to: Biological General Repository for Interaction Datasets (BioGRID) is related to: CORUM is related to: Database of Interacting Proteins (DIP) is related to: HPRD - Human Protein Reference Database is related to: InnateDB is related to: IntAct is related to: MatrixDB is related to: MINT is related to: MPact: Representation of Interaction Data at MIPS is related to: MPIDB is related to: MIPS Mammalian Protein-Protein Interaction Database is related to: I2D is related to: IMEx - The International Molecular Exchange Consortium is related to: PSICQUIC Registry |
PMID:18823568 | THIS RESOURCE IS NO LONGER IN SERVICE | nif-0000-20860 | http://irefindex.uio.no | SCR_002085 | 2026-09-19 12:56:33 | 22 | ||||||
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SpliceAid-F Resource Report Resource Website 10+ mentions |
SpliceAid-F (RRID:SCR_002082) | SpliceAid-F | data or information resource, database | A database of human splicing factors and their RNA - binding sites. For each splicing factor (SF) the database reports its functional domains and its protein and chemical interactors. Furthermore, experimentally validated RNA-SF interactions are collected, including relevant information on the RNA binding sites such as the genes where these sites lie, their genomic coordinates, the splicing effects, experimental procedures, as well as the corresponding bibliographic references. Information from experiments showing no RNA-SF binding is also collected, at least in the assayed conditions. SpliceAid-F contains 4227 interactions, 2622 RNA binding sites and 1170 no-binding sites, including information on binding and no-binding specificity in different cellular contexts. SpliceAid-F can provide significant information to explain an observed splicing pattern as well as the effect of mutations in functional regulatory elements. | splicing, protein, rna, splicing factor, interaction, binding site, no-binding site, splicing pattern, mutation, regulatory element, splicing factor |
is listed by: OMICtools has parent organization: University of Bari; Bari; Italy |
PMID:23118479 | Free, Freely Available | OMICS_01893 | http://srv00.ibbe.cnr.it/SpliceAidF/ | SCR_002082 | SpliceAid-F: a database of human splicing factors and their binding sites | 2026-09-19 12:56:33 | 11 | |||||
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Protein Interactions by Structural Matching Resource Report Resource Website 1+ mentions |
Protein Interactions by Structural Matching (RRID:SCR_002116) | P.R.I.S.M. | data or information resource, database | It is a web-server that can be used to explore protein interfaces and predict protein-protein interactions. It is a website for protein interface analysis and prediction of putative protein-protein interactions. It is composed of a database holding protein interface structures derived from the Protein Data Bank (PDB). The server also includes summary information about related proteins and an interactive protein interface viewer. A list of putative protein-protein interactions obtained by running our prediction algorithm can also be accessed. These results are applied to a set of protein structures obtained from the PDB at the time of algorithm execution. Users can browse through the non-redundant dataset of representative interfaces on which the prediction algorithm depends, retrieve the list of similar structures to these interfaces or see the results of interaction predictions for a particular protein. Another service provided is interactive prediction. This is done by running the algorithm for user input structures. | interaction, protein, structure | PMID:15991339 PMID:21886100 |
THIS RESOURCE IS NO LONGER IN SERVICE | nif-0000-20901 | SCR_002116 | Protein Interactions by Structural Matching | 2026-09-19 12:56:33 | 2 | |||||||
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Database of the Human Proteotheque Initiative Resource Report Resource Website |
Database of the Human Proteotheque Initiative (RRID:SCR_002076) | data or information resource, database | The Human Proteotheque Initiative is a multidisciplinary project aimed at building a repertoire of comprehensive maps of human protein interaction networks. The information contained in the Proteotheque is made publicly available through an interactive web site that can be consulted to visualize some of the fundamental molecular connections formed in human cells and to determine putative functions of previously uncharacterized proteins based on guilt by association. The process governing the evolution of HuPI towards becoming a repository of accurate and complete protein interaction maps is described. | function, cell, human, interaction, protein | PMID:18443628 | THIS RESOURCE IS NO LONGER IN SERVICE | nif-0000-20836 | http://hupi.ircm.qc.ca/hupi/index.jsp | SCR_002076 | HuPI | 2026-09-19 12:56:32 | 0 | |||||||
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MPIDB Resource Report Resource Website 1+ mentions |
MPIDB (RRID:SCR_001898) | MPIDB | data or information resource, database | Database that collects and provides all known physical microbial interactions. Currently, 24,295 experimentally determined interactions among proteins of 250 bacterial species/strains can be browsed and downloaded. These microbial interactions have been manually curated from the literature or imported from other databases (IntAct, DIP, BIND, MINT) and are linked to 26,578 experimental evidences (PubMed ID, PSI-MI methods). In contrast to these databases, interactions in MPIDB are further supported by 68,346 additional evidences based on interaction conservation, co-purification, and 3D domain contacts (iPfam, 3did). (spoke/matrix) binary interactions inferred from pull-down experiments are not included. | 3d domain, conservation, co-purification, interaction, microbial, protein, microbial interaction, protein interaction, interaction conservation, interaction co-purification, 3d domain contact, protein-protein interaction, microbial protein, microbiology |
is listed by: re3data.org is related to: IMEx - The International Molecular Exchange Consortium is related to: IntAct is related to: Database of Interacting Proteins (DIP) is related to: BIND is related to: MINT is related to: Interaction Reference Index is related to: IMEx - The International Molecular Exchange Consortium is related to: PSICQUIC Registry has parent organization: J. Craig Venter Institute |
J. Craig Venter Institute ; Indgen Life Technologies ; NIH ; NIMH R01GM79710 |
PMID:18556668 | THIS RESOURCE IS NO LONGER IN SERVICE | r3d100010673, nif-0000-10467 | http://jcvi.org/mpidb/ | SCR_001898 | The Microbial Protein Interaction Database, Microbial Protein Interaction Database | 2026-09-19 12:56:32 | 5 |
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