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A database for conveniently accessing the comprehensive information and relationships of spectra, peptides and proteins of single amino-acid polymorphisms (SAPs), as well as related genes, pathways, diseases and drug targets. dbSAP is a customized protein database that contained comprehensive variant proteins by integrating and annotating the human single nucleotide polymorphisms (SNPs) and mutations from eight distinct databases (UniProt, Protein Mutation Database, HPMD, MSIPI, MS-CanProVar, dbSNP, Ensembl and COSMIC). After a series of quality controls, a total of 16,854 SAP peptides involving in 439,537 spectra were identified with large scale mass spectrometry datasets from various human tissues and cell lines. dbSAP is freely available online.


Enables you to explore mutation hotspots identified in protein domains from more than 5000 patients across 22 cancer types. Using multiple sequence analysis, protein domain hotspots are identified by tallying missense mutations across analogous residues of domain-containing genes. By taking a domain-centric approach, we identify new mutation hotspots in domains of genes not previously associated with cancer and predict the functional role of many rare mutations. MutationAligner allows researchers to search, browse and analyze cancer mutations in the context of protein domains.


Stores and characterizes cancer-related alterations of single amino acid in the human proteome as well as variations detected in normal samples. CanProVar 2.0 allows users to retrieve protein-level annotations about a variation, such as the corresponding cancer samples, publications, and potential functional impact as suggested by analyses based on evolution conservation, protein expression, protein domains, and protein 3D interaction. It aims to provide a bridge between genomic data and proteomic studies, allowing users to explore molecular functional characteristics of crVARs and proteins bearing these variations, i.e., cancer-related proteins.


Collects information about von Hippel-Lindau protein (pVHL) interactors and mutation effects. VHLdb is both a manually and automatically curated repository that compiles more than 470 interactors and over 1000 pathogenic somatic or germline pVHL mutations. The platform allows users to browse data: (i) by interaction, providing an interactive and downloadable tree diagram; or (ii) by mutations by using a table interface that allows searches and filtering by several features such as variants, type or codon.

ProCMD / 3D Protein C Mutations Database

Consists in a 3D-structure oriented repository of protein C. ProCMD associates clinical and phenotypical descriptions with functional and structural data obtained by computational approaches. Users can retrieve entries by the position in the sequence of a mutated residue, by amino acidic substitution, and by domain localization. The database can be useful to assist in prediction of the effect of a mutation, clarification of the role of specific residues in protein function.