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Resource Name Proper Citation Abbreviations Resource Type Description Keywords Resource Relationships Related Condition Funding Defining Citation Availability Specification URL Alternate IDs Alternate URLs Old URLs Parent Organization Resource ID Synonyms Record Last Update Mentions Count
LPDB: Ligand-Protein DataBase
 
Resource Report
Resource Website
1+ mentions
LPDB: Ligand-Protein DataBase (RRID:SCR_008172) data or information resource, database The Ligand Protein Database is designed to allow the selection of complexes based on various properties of receptors and ligands for the design and parametrization of new scoring functions or to assess and improve existing ones. Moreover, for each complex, a continuum of ligand positions ranging from the crystallographic position to points on the surface of the protein receptor allows an assessment of the energetic behavior of particular scoring functions. Access to the database is password protected. To obtain access to the LPDB, complete a form, available online, have it signed by your research advisor, and fax the completed form back to the attention of Professor Charles L. Brooks III, (858) 784-8688. There is no fee for academic use of the LPDB. We are currently working out details for licensing to our colleagues in industry. Please contact Professor Brooks to obtain current information on access to the LPDB. complexes, ligand, protein, receptors has parent organization: University of Michigan; Ann Arbor; USA nif-0000-21245 SCR_008172 LPDB 2026-09-19 12:57:15 2
PHAROS
 
Resource Report
Resource Website
PHAROS (RRID:SCR_016258) TCRD data or information resource, database Database of ligands and diseases. Its goal is to develop a knowledge-base for the Druggable Genome (DG) in order to illuminate the uncharacterized and/or poorly annotated portion of the genome. DG, focusing on four of the most commonly drug-targeted protein families: G-protein-coupled receptors (GPCRs); nuclear receptors (NRs); ion channels (ICs); and kinases. protein, target, disease, ligand, phenotype, drug, medication, pharmacology, gpcr, nuclear, receptor, ion, channel, kinase NCATS ;
NCI CA189201;
NCI CA189205;
NCI U24 CA224370;
Novo Nordisk Foundation NNF14CC0001
PMID:27903890 Freely available, Free, Available for download SCR_016258 Target Central Resource Database 2026-09-19 12:57:35 0
p300db
 
Resource Report
Resource Website
1+ mentions
p300db (RRID:SCR_017063) data or information resource, database Data collection of CBP/p300 regulated acetylome, proteome, and transcriptome in murine embryonic fibroblasts. Composed of Symbol search for quantified acetylation sites, proteins and transcripts abundance in CBP/p300, Domain search for batch query of proteins by specific domain and Conserved sites for acetylation sites that are conserved between mouse and human, and their regulation in KATi treated cells. data, collection, CBP, p300, regulated, acetylome, proteome, transcriptome, murine, embryonic, fibroblast, domain, protein, acetylation, site, dataset is related to: Ensembl
is related to: UniProt
has parent organization: University of Copenhagen; Copenhagen; Denmark
Free, Available for download, Freely available SCR_017063 2026-09-19 12:57:36 1
MitoCarta
 
Resource Report
Resource Website
100+ mentions
MitoCarta (RRID:SCR_018165) data or information resource, database Collection of genes encoding proteins with strong support of mitochondrial localization. Inventory of genes encoding mitochondrial-localized proteins and their expression across 14 mouse tissues. Database is based on human and mouse RefSeq proteins that are mapped to NCBI Gene loci. MitoCarta 2.0 inventory provides molecular framework for system-level analysis of mammalian mitochondria. Gene, protein, mitochondrial protein, protein expression, data, human, mouse, RefSeq protein, analysis, mammalian mitochondra, FASEB list Australian NHMRC ;
Burroughs Wellcome Fund Career Award in the Biomedical Sciences ;
Charles E. Culpeper Scholarship in Medical Science ;
Howard Hughes Medical Institute ;
NIDDK DK43351;
NIDDK DK57521;
NIGMS GM0077465
PMID:26450961
PMID:18614015
Free, Freely available SCR_018165 MitoCarta2.0 2026-09-19 12:57:37 208
UniProtKB/Swiss-Prot
 
Resource Report
Resource Website
500+ mentions
UniProtKB/Swiss-Prot (RRID:SCR_021164) data or information resource, database Curated component of UniProtKB (produced by the UniProt consortium). It contains hundreds of thousands of protein descriptions, including function, domain structure, subcellular location, post-translational modifications and functionally characterized variants. protein descriptions, protein function, protein, domain structure, subcellular location, post-translational modifications, functionally characterized variants is related to: UniProtKB SIB Swiss Institute of Bioinformatics DOI:10.1093/nar/26.1.38 Free, Freely available r3d100010677 https://doi.org/10.17616/R33314 SCR_021164 Swiss-Prot, SwissProt 2026-09-19 12:57:38 658
Liver cell atlas
 
Resource Report
Resource Website
10+ mentions
Liver cell atlas (RRID:SCR_023627) atlas, data or information resource Portal to search liver single cell RNA-sequencing datasets. Datasets for expression of genes or proteins (when CITE-seq was performed). To search for gene enter the official gene name. To search for protein please click to see specific names to use for different markers included. liver single cell RNA-sequencing data, liver cell, RNA-sequencing data, gene expression, protein, dataset, has parent organization: Ghent University; Ghent; Belgium Free, Freely available SCR_023627 2026-09-19 12:57:39 41
AlphaFold Protein Structure Database
 
Resource Report
Resource Website
1000+ mentions
AlphaFold Protein Structure Database (RRID:SCR_023662) AlphaFold DB data or information resource, database Database of protein structure predictions by AlphaFold that are freely and openly available to global scientific community. Included are nearly all catalogued proteins known to science. Provides programmatic access to and interactive visualization of predicted atomic coordinates, per residue and pairwise model confidence estimates and predicted aligned errors. EMBL-EBI, protein structure predictions, AlphaFold, catalogued proteins, protein, programmatic access, interactive visualization, PMID:34791371 Free, Freely available r3d100013615 https://doi.org/10.17616/R31NJMZZ SCR_023662 2026-09-19 12:57:39 1771
UCL Biobank
 
Resource Report
Resource Website
UCL Biobank (RRID:SCR_000517) UCL Biobank biomaterial supply resource, material resource Two University College London (UCL) biobanks, one based at the Royal Free Hospital (RFH) Campus and the other based at Bloomsbury supporting Pathology and the Cancer Institute, will act as physical repositories for collections of biological samples and data from patients consented at UCLH, Partners Hospitals and external sources. This will incorporate collections of existing stored samples and new collections. UCL-RFH BioBank, the physical repository at the Royal Free, presents a unique opportunity to advance medical research through making access to research tissue easier, faster and much more efficient. The BioBank is both a physical repository, with capacity for up to 1 million cryogenically stored samples and a virtual repository for all tissue, cell, plasma, serum, DNA and RNA samples stored throughout UCLP. In particular, samples considered "relevant material", such as tissues and cells, that are licensed by the Human Tissue Authority, can be stored long term. Existing holdings of tissues and cells where appropriate can be transferred to the Physical BioBank at the Royal Free. UCL - Royal Free BioBank provides a flexible approach to banking, allowing the Depositor to pick and choose services that are tailored to fit their requirements. Collaborations arising from publicizing of the existence of the holdings are entirely at the discretion of the depositor, as the facility ensures that access to the deposits remains at the decision of the Depositor/User. UCL Biobank for studying Health and Disease (based at Pathology-Rockefeller building and the UCL-Cancer Institute will support projects principally involved in the study of human disease. The aim is to support primarily, research in the Pathology Department, UCLH and the UCL-Cancer Institute but it will also support other UCLH partners. The biobank will store normal and pathological specimens, surplus to diagnostic requirements, from relevant tissues and bodily fluids. Stored tissues will include; snap-frozen or cryopreserved tissue, formalin-fixed tissue, paraffin-embedded tissues, and slides prepared for histological examination. Tissues will include resection specimens obtained surgically or by needle core biopsy. Bodily fluids will include; whole blood, serum, plasma, urine, cerebrospinal fluid, milk, saliva and buccal smears and cytological specimens such as sputum and cervical smears. Fine needle aspirates obtained from tissues and bodily cavities (e.g. pleura and peritoneum) will also be collected. Where appropriate the biobank will also store separated cells, protein, DNA and RNA isolated from collected tissues and bodily fluids described above. Some of the tissue and aspirated samples will be stored in the diagnostic archive. tissue, cell, plasma, serum, dna, rna, blood, serum, plasma, urine, cerebral spinal fluid, milk, saliva, buccal smear, sputum, cervical smear, pleura, peritoneum, protein, body fluid, cryopreserved, frozen, snap-frozen, formalin-fixed, paraffin-embedded, slide, cancer, disease, normal is listed by: One Mind Biospecimen Bank Listing
has parent organization: University College London; London; United Kingdom
Cancer, Disease, Normal THIS RESOURCE IS NO LONGER IN SERVICE nlx_36620 SCR_000517 Biobanking at UCL 2026-09-19 12:57:41 0
Bio-Synthesis
 
Resource Report
Resource Website
100+ mentions
Bio-Synthesis (RRID:SCR_000820) biomaterial supply resource, material resource A commercial supplier of custom synthetic molecules. They specialize in peptides, oligonucleotides, bioconjugation, molecular biology services, proteins and specialty chemistry. antibody, synthetic molecule, peptides, oligonucleotide, bioconjugation, protein is listed by: ScienceExchange NIH 263-00050713-01 nlx_152297, SciEx_516 SCR_000820 Bio-Synthesis Inc. 2026-09-19 12:57:42 167
e-Driver
 
Resource Report
Resource Website
1+ mentions
e-Driver (RRID:SCR_002674) software application, software resource, standalone software Software tool to identify cancer driver genes based on linear annotations of biological regions such as protein domains.Uses information on three-dimensional structures of mutated proteins to identify specific structural features. Then algorithm analyzes whether these features are enriched in cancer somatic mutations and are candidate driver genes. Identify cancer driver genes, candidate driver genes, perl, protein, mutated proteins, cancer somatic mutations, bio.tools is listed by: OMICtools
is listed by: Debian
is listed by: bio.tools
Cancer PMID:25064568 Free, Available for download, Freely available biotools:e-Driver, OMICS_05288 https://bio.tools/e-Driver SCR_002674 2026-09-19 12:57:46 5
MapMan
 
Resource Report
Resource Website
1000+ mentions
MapMan (RRID:SCR_003543) MapMan software application, software resource Software tool that displays large genomics datasets (e.g. gene expression data from Arabidopsis Affymetrix arrays) onto diagrams of metabolic pathways or other biological processes. metabolic pathway, biological process, genomics, pathway, array, visualization, gene, transcript, protein, enzyme, metabolite is related to: GoMapMan
has parent organization: Max Planck Institute of Molecular Plant Physiology; Golm; Germany
PMID:19389052
PMID:14996223
PMID:16009995
PMID:16649112
nlx_157682 SCR_003543 MapMan Application Software 2026-09-19 12:57:47 1251
Protein Knots
 
Resource Report
Resource Website
1+ mentions
Protein Knots (RRID:SCR_008353) analysis service resource, data analysis service, production service resource, service resource The knot server allows the user to check PDB entries or uploaded structures for knots and to visualize them. The size of a knot is determined by deleting amino acids from both ends. This procedure is, however, not perfect and the resulting size should only be treated as a guideline. Mathematically, knots are only well defined in closed (circular) loops. However, both the N- and C-termini of open proteins are typically located close to the surface of the protein and can be connected unambiguously: We reduce the protein to its backbone and draw two lines outward starting at the termini in the direction of the connection line between the center of mass of the backbone and the respective ends. The two lines are joined by a big loop, and the structure is topologically classified by the determination of its Alexander polynomial. To determine an estimate for the size of the knotted core, we successively delete amino acids from the N-terminus until the protein becomes unknotted. The procedure is repeated at the C-terminus starting with the last N-terminal deletion structure that contained the original knot. For each deletion, the outward-pointing line through the new termini is parallel to the respective lines computed for the full structure. Unfortunately, the size of a knot is not always precisely determined by this procedure, so reported sizes should therefore only be treated as approximate. Sponsors: Knots is funded by MIT. amino acid, backbone, core, c-terminus, knot, n-terminus, protein, protein databank, protein folding, size, structural model, structure has parent organization: Massachusetts Institute of Technology; Massachusetts; USA; nif-0000-25217 SCR_008353 Knots 2026-09-19 12:57:17 3
Peroxisome Database
 
Resource Report
Resource Website
10+ mentions
Peroxisome Database (RRID:SCR_008352) data or information resource, database The aim of the PEROXISOME database (PeroxisomeDB) is to gather, organize and integrate curated information on peroxisomal genes, their encoded proteins, their molecular function and metabolic pathway they belong to, and their related disorders. PeroxisomeDB contains the complete peroxisomal proteome of Homo sapiens (encoded by 85 genes) and Saccharomyces cerevisiae (encoded by 61 genes). Now, we have included 34 new organism genomes with the acquisition of 2426 new peroxisomal homolog proteins. PeroxisomeDB 2.0 integrates the peroxisomal metabolome of whole microbody family by the new incorporation of the glycosome proteomes of trypanosomatids and the glyoxysome proteome of Arabidopsis thaliana. The site also provides a Peroxisome Metabolome of peroxisomal genes and proteins, their molecular interactions and metabolic pathways, tools for comparative genomics, predictive tools. Sponsors: Preoxisome Database is funded by Institut de Gntique et deBiologie Molculaire et Cellulaire. family, function, gene, arabidopsis thaliana, disorder, genome, genomic, glycosome, glyoxysome, homolog, homo sapiens, interaction, metabolic, metabolome, microbody, molecular, organism, pathway, peroxisome, protein, proteome, saccharomyces cerevisiae, trypanosomatid nif-0000-25216 SCR_008352 Preoxisomedb 2026-09-19 12:57:17 31
Structure modeling of 907 G protein coupled receptors in the human genome
 
Resource Report
Resource Website
1+ mentions
Structure modeling of 907 G protein coupled receptors in the human genome (RRID:SCR_008351) data or information resource, database THIS RESOURCE IS NO LONGER IN SERVICE, documented on August 19,2019.Database of tertiary structural modeling results of threading assembly refinement (TASSER) method for all 907 G protein-coupled receptors (GPCRs) in human genome. All sequences were collected from GPCR database http://www.gpcr.org/7tm/ and http://www.expasy.org/cgi-bin/lists?7tmrlist.txt. Unlike traditional homology modeling approaches, TASSER modeling does not require solved homologous template structures; moreover, it often refines the structures closer to native. G protein-coupled receptors (GPCRs), encoded by about 5% of human genes, comprise the largest family of integral membrane proteins and act as cell surface receptors responsible for the transduction of endogenous signal into a cellular response. Although tertiary structural information is crucial for function annotation and drug design, there are few experimentally determined GPCR structures. To address this issue, we employ the recently developed threading assembly refinement (TASSER) method to generate structure predictions for all 907 putative GPCRs in the human genome. Unlike traditional homology modeling approaches, TASSER modeling does not require solved homologous template structures; moreover, it often refines the structures closer to native. These features are essential for the comprehensive modeling of all human GPCRs when close homologous templates are absent. Based on a benchmarked confidence score, approximately 820 predicted models should have the correct folds. The majority of GPCR models share the characteristic seven-transmembrane helix topology, but 45 ORFs are predicted to have different structures. This is due to GPCR fragments that are predominantly from extracellular or intracellular domains as well as database annotation errors. Our preliminary validation includes the automated modeling of bovine rhodopsin, the only solved GPCR in the Protein Data Bank. With homologous templates excluded, the final model built by TASSER has a global C(alpha) root-mean-squared deviation from native of 4.6 angstroms, with a root-mean-squared deviation in the transmembrane helix region of 2.1 angstroms. Models of several representative GPCRs are compared with mutagenesis and affinity labeling data, and consistent agreement is demonstrated. Structure clustering of the predicted models shows that GPCRs with similar structures tend to belong to a similar functional class even when their sequences are diverse. These results demonstrate the usefulness and robustness of the in silico models for GPCR functional analysis. Sponsors: GPCR is funded by the University at Buffalo, Buffalo, New York. endogenous, extracellular, family, functional, gene, cellular, couple, genome, gpcr, g protein, helix, homology, human, membrane, model, modeling, orf, protein, receptor, response, signal, structural, structural model, structure, template, tertiary, topology, transduction, transmembrane has parent organization: Georgia Institute of Technology; Georgia; USA THIS RESOURCE IS NO LONGER IN SERVICE nif-0000-25215 SCR_008351 GPCR 2026-09-19 12:57:17 3
SVM based method for predicting beta hairpin structures in proteins
 
Resource Report
Resource Website
1+ mentions
SVM based method for predicting beta hairpin structures in proteins (RRID:SCR_008349) analysis service resource, data analysis service, production service resource, service resource Bhairpred server is based on machine learning technique SVM using single sequence information, evolutionary profile, predicted and observed secondary structure (as obtained using Psipred and DSSP), predicted and observed accessibility values (as obtainned from Netasa and DSSP). The methods were trained and tested on dataset of 2880 proteins and their performance was evaluated on dataset of 534 proteins used by Thornton (PNAS, 2002). Best prediction results were obtained with hybrid approach that combined prediction results from evolutionary profile, predicted secondary structure and accessibility. evolutionary, information, protein, protein structure prediction, secondary, sequence, single, svm, technique, bio.tools is listed by: bio.tools
is listed by: Debian
has parent organization: Institute of Microbial Technology; Chandigarh; India
Institute of Microbial Technology nif-0000-25213, biotools:bhairpred https://bio.tools/bhairpred SCR_008349 BhairPred 2026-09-19 12:57:17 2
MitoInteractome
 
Resource Report
Resource Website
MitoInteractome (RRID:SCR_010225) MitoInteractome data or information resource, database Database that gathers data on interactions in the mitochondrial proteome that has been used to construct a network for the aging process in humans and to identify interactions that influence this process, since mitochondria is a major source of cellular reactive oxygen species that accumulate during aging. It will: # aid in increasing our understanding of the molecular functions and interaction networks of mitochondrial proteins, # help in identifying new target proteins for experimental research using predicted protein-protein interaction information, and # help in identifying biomarkers for diagnosis and new molecular targets for drug development related to mitochondria. How is MitoInteractome different? * Provides protein-protein interaction information with graphical display. * Applies newly added new mitochondrial protein information by using BLAST incorporated in Mitointeractome * Shows correlation of mutation with their impact * Provides specific pathway information to aid study of their impact * Contains SNP Information interaction, mitochondrial proteome, mitochondria, protein-protein interaction, physico-chemical property, polymorphism, protein sequence, protein, disease, snp, pathway has parent organization: Korea Research Institute of Bioscience and Biotechnology; Daejeon; South Korea Aging PMID:19958484 nlx_156772 SCR_010225 MitoInteractome - Mitochondrial Protein Interactome Database 2026-09-19 12:57:21 0
UniPathway
 
Resource Report
Resource Website
10+ mentions
UniPathway (RRID:SCR_010513) UniPathway data or information resource, database A manually curated database of enzyme-catalyzed and spontaneous chemical reactions. It provides a hierarchical representation of metabolic pathways and a controlled vocabulary for pathway annotation in UniProtKB. UniPathway data are cross-linked to existing metabolic resources such as ChEBI/Rhea, KEGG and MetaCyc. Users may do a quick search, browse pathway, browse compound, or browse organism. metabolic pathway, pathway annotation, pathway, annotation, chemical reaction, protein, compound is related to: UniProtKB
has parent organization: PrabiG
has parent organization: SIB Swiss Institute of Bioinformatics
Swiss Federal Government ;
GIS-IBISA ;
European Union SISYPHE ;
European Union SLING 226073;
European Union Microme 222886-2;
French Government ANR MIRI BLAN08-1335497
PMID:22102589 nlx_16723 SCR_010513 UniPathway: a metabolic door to UniProtKB/Swiss-Prot, UniPathway: a resource for the exploration of metabolic pathways 2026-09-19 12:57:22 17
mCSM
 
Resource Report
Resource Website
50+ mentions
mCSM (RRID:SCR_010776) mCSM analysis service resource, data analysis service, production service resource, service resource Data analysis service to the study of missense mutations which relies on graph-based signatures. mutation, protein, protein stability, protein-protein, protein-dna, data set is listed by: OMICtools
has parent organization: University of Cambridge; Cambridge; United Kingdom
PMID:24281696 OMICS_00133 SCR_010776 mCSM: predicting the effect of mutations in proteins using graph-based signatures 2026-09-19 12:57:25 81
TBLASTN
 
Resource Report
Resource Website
5000+ mentions
TBLASTN (RRID:SCR_011822) TBLASTN analysis service resource, data analysis service, production service resource, service resource Tool to search translated nucleotide databases using a protein query. protein is listed by: OMICtools
is listed by: SoftCite
has parent organization: NCBI
OMICS_00999 SCR_011822 Translated BLAST: tblastn 2026-09-19 12:57:25 5696
HSLPred
 
Resource Report
Resource Website
HSLPred (RRID:SCR_011972) HSLPred analysis service resource, data analysis service, production service resource, service resource A support vector machine (SVM)-based method for the prediction of 4 major subcellular localization (cytoplasm, mitochondrial, nuclear and plasma membrane) of human proteins using various features such as i) amino acid composition, ii) dipeptide composition and iii) evolutionary information of proteins. subcellular localization, protein, support vector machine, bio.tools is listed by: OMICtools
is listed by: Debian
is listed by: bio.tools
has parent organization: Institute of Microbial Technology; Chandigarh; India
PMID:15647269 Acknowledgement requested biotools:hslpred, OMICS_01622 https://bio.tools/hslpred SCR_011972 HSLPred - A SVM-based Method for Subcellular Localization of Human Proteins 2026-09-19 12:57:26 0

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