Tools   Select Another Resource Report Type

http://apps.cytoscape.org/apps/cytohubba

Software tool for identifying hub objects and sub-networks from complex interactome. Predicts and explore nodes and subnetworks in given network by several topological algorithms. Provides interface to analyze topology of protein-protein interaction networks, such as human, yeast, rat, mouse, fly etc. Plugin works with Cytoscape 2.6 or above, which requires Java 1.5 or above.

Proper citation: cytoHubba (RRID:SCR_017677) Copy   

•   Source: SciCrunch Registry

https://omictools.com/rnacompete-tool

Method for the systematic analysis of RNA binding specificities that uses a single binding reaction to determine the relative preferences of RBPs for short RNAs that contain a complete range of k-mers in structured and unstructured RNA contexts. RNAcompete identifies expected and previously unknown RNA binding preferences., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: RNAcompete (RRID:SCR_015900) Copy   

•   Source: SciCrunch Registry

http://apps.cytoscape.org/apps/cluepedia

Data analysis software and search tool for new markers potentially associated to pathways. CluePedia calculates linear and non-linear statistical dependencies from experimental data and investigates interrelations within each pathway to reveal associations through gene/protein/miRNA enrichments.

Proper citation: CluePedia Cytoscape plugin (RRID:SCR_015784) Copy   

•   Source: SciCrunch Registry

http://disulfind.dsi.unifi.it/

THIS RESOURCE IS NO LONGER IN SERVICE. Documented on February 28,2023, Software for predicting the disulfide bonding state of cysteines and their disulfide connectivity, starting from a protein sequence alone and may be useful in other genomic annotation tasks.

Proper citation: DISULFIND (RRID:SCR_016072) Copy   

•   Source: SciCrunch Registry

http://molevol.cmima.csic.es/castresana/Gblocks_server.html

Software that eliminates poorly aligned positions and divergent regions of a DNA or protein alignment so that it becomes more suitable for phylogenetic analysis., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: Gblocks (RRID:SCR_015945) Copy   

•   Source: SciCrunch Registry

http://emboss.sourceforge.net/apps/cvs/embassy/index.html#DOMALIGN

Software commands for Extra EMBOSS and protein domain alignment. The DOMALIGN programs were developed by Jon Ison and colleagues at MRC HGMP for their protein domain research. They are included as an EMBASSY package as a work in progress.

Proper citation: DOMALIGN (RRID:SCR_016085) Copy   

•   Source: SciCrunch Registry

https://github.com/osallou/cassiopee-c

Software to scan an input genomic sequence (dna/rna/protein). It searchs for a subsequence that has an exact match, substitutions (Hamming distance), and/or insertion/deletions with supporting alphabet ambiguity.

Proper citation: Cassiopee (RRID:SCR_016056) Copy   

•   Source: SciCrunch Registry

http://bioplex.hms.harvard.edu/

Database of cell lines with each expressing a tagged version of a protein from the ORFeome collection. The overarching project goal is to determine protein interactions for every member of the collection.

Proper citation: BioPlex (RRID:SCR_016144) Copy   

•   Source: SciCrunch Registry

https://mentha.uniroma2.it/

Software that archives evidence collected from different sources, then analyzes and presents these data. Its data come from manually curated protein-protein interaction databases that have adhered to the IMEx consortium.

Proper citation: mentha (RRID:SCR_016148) Copy   

•   Source: SciCrunch Registry

http://www.zucic.org/garlic/

Software application for visualization and editing of biomolecules. Used for the investigation of membrane proteins, visualization of other proteins and geometric objects, and analysis of protein sequences.

Proper citation: Garlic (RRID:SCR_016118) Copy   

•   Source: SciCrunch Registry

https://www.rapidnovor.com/antibody-sequencing-service/

Service for monoclonal antibody protein sequencing. It derives the sequences directly from the protein using mass spectrometry and without the need to access the cell line.

Proper citation: REmAb (RRID:SCR_016239) Copy   

•   Source: SciCrunch Registry

https://github.com/ihmwg/IHM-dictionary

Software resource for a data representation for integrative/hybrid methods of modeling macromolecular structures.

Proper citation: IHM-dictionary (RRID:SCR_016186) Copy   

•   Source: SciCrunch Registry

https://pdb-dev.wwpdb.org

Data repository for integrative/hybrid structural models of macromolecules and their assemblies. This includes atomistic models as well as multi-scale models consisting of different coarse-grained representations.

Proper citation: PDB-Dev (RRID:SCR_016185) Copy   

•   Source: SciCrunch Registry

http://caps.ncbs.res.in/gendis/home.html

Genomic Distribution of structural Superfamilies identifies and classifies evolutionary related proteins at the superfamily level in whole genome databases. GenDiS has been curated in direct correspondence with SCOP and represents 4001 highly resolved domains in 1194 structural superfamilies across protein sequence databases. Sequences showing reliable homology to entries in SCOP and PASS2 databases have been obtained from the non-redundant protein sequence database and aligned. Similar alignments of the superfamily members are provided in the genome level. GenDiS provides a platform for cross genome comparison at the superfamily level. GenDis relates proteins sequence information across all strata of taxonomy. One may navigate through the database to obtain structural homologues across different levels in taxonomic classification. The nomenclature of the various genomes and their hierarchy is in direct correspondence with the taxonomy database maintained at the NCBI. Sequence homologues for the various structural members are obtained from the non-redundant protein sequence database employing sensitive sequence search methods. Multiple approaches such as PSI-BLAST, HMMsearch of the HMMer suite and an interacting motif constrained PHI-BLAST have been employed to identify homologues in the sequence databases.

Proper citation: Genomic Distribution of structural Superfamilies (RRID:SCR_007670) Copy   

•   Source: SciCrunch Registry

http://mendel.gene.cwru.edu/adamslab/cgi-bin/paml/pbrowser.py

THIS RESOURCE IS NO LONGER IN SERVICE, documented on July 16, 2013. It provides access to the results of tests for positive selection in 14,000 human genes. Multiple alignments of protein-coding regions of genes from human and other mammals were extracted from whole-genome alignments available from UC-Santa Cruz. Each gene was analyzed using the maximum likelihood tests of selection using PAML. Branch, site, and branch+site tests were performed, each with at least one matching null model.

Proper citation: Human PAML Browser (RRID:SCR_007715) Copy   

•   Source: SciCrunch Registry

http://dbptm.mbc.nctu.edu.tw/

dbPTM is a database that compiles information on protein post-translational modifications (PTM) such as the modified sites, solvent accessibility of surrounding amino acids, protein secondary and tertiary structures, protein domains, and protein variations. The version 2.0 of dbPTM integrates the experimentally validated PTM sites with referable literatures from Swiss-Prot, Phospho.ELM, O-GLYCBASE, and UbiProt. In all of the collected PTM information, about 25 types of PTM with enough experimentally validated sites are trained the profile hidden Markov models (HMMs) to detect the potential PTM sites with 100% specificity against Swiss-Prot proteins. To help users investigating more detail in each type of PTM, the substrate peptide specificity such as positional amino acid frequency, solvent accessibility and secondary structure surrounding the modified sites are also provided. Moreover, the information of orthologous protein clusters is provided to users for analyzing whether the PTM sites located in the evolutionary conserved regions or not., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: dbPTM: An informational repository of proteins and post-translational modifications (RRID:SCR_007619) Copy   

•   Source: SciCrunch Registry

http://firedb.bioinfo.cnio.es/

A database of Protein Data Bank structures, ligands and annotated functional site residues. The database can be accessed by PDB codes or UniProt accession numbers as well as keywords. FireDB contains information on every chemical compound in the PDB, including their descriptions, the PDB structures in which the compounds are found and the amino acids that are in contact with the ligand.

Proper citation: FireDB (RRID:SCR_007655) Copy   

•   Source: SciCrunch Registry

http://cgl.imim.es/fcp/

FCP is a publicly accessible web tool dedicated to analyzing the current state and trends of available proteome structures along the classification schemes of enzymes and nuclear receptors. It offers both graphical and quantitative data on the degree of functional coverage in that portion of the proteome by existing structures and on the bias observed in the distribution of those structures among proteins. Users can choose to search the website based on structures or ligands, and can also sort by enzyme or receptor. Users can also view data based on structural and population (species) filters.

Proper citation: Functional Coverage of the Proteome (RRID:SCR_007654) Copy   

•   Source: SciCrunch Registry

http://caps.ncbs.res.in/imotdb/

Comprehensive collection of spatially interacting motifs in proteins. Interacting motif database lists interacting motifs that are identified for all structural entries in PDB. Conserved patterns or finger prints are identified for individual structural entries and also grouped together for reporting common motifs shared among all superfamily members.

Proper citation: Database of Spatially Interacting Motifs in Proteins (RRID:SCR_007735) Copy   

•   Source: SciCrunch Registry

http://pimp.starflr.info/

A database ofhuman disease-related mutated proteins identified by mass-spectrometry (MS). For achieving this goal, we collected human mutated sequences known to be related to diseases till now. After surveying mutated sequence sources: PMD, OMIM, SwissProt polymorphism, HGMD, etc, we found that currently HGMD contains the largest human gene mutation information. However, because, for academic users, HGMD does not provide with whole data download service, we decided to systematically extract and curate mutation information from PMD, OMIM, SwissProt, MSIPI database to form SysPIMP and provide it free for academic users.

Proper citation: Systematic Platform for Identifying Mutated Proteins (SysPIMP) (RRID:SCR_007954) Copy   

•   Source: SciCrunch Registry