CarbDisMut

CarbDisMut is a freely accessible database for human carbohydrate binding proteins mutation. It contains data on disease and neutral mutations retrieved from different mutation databases such as HumSavar, SwissVar, 1000 Genomes, COSMIC and ClinVar.

We have included missense, deletions and insertions in our database. Missense – is a non-synonymous mutation in which a single nucleotide change results in a codon that codes for a different amino acid Deletions - are mutations in which a section of DNA is lost, or deleted. Insertions - are mutations in which extra base pairs are inserted into a new place in the DNA.

Existing databases are on sequence/structural data and binding affinity from experimental techniques. Moreover, there is no specific mutation database for human carbohydrate binding proteins.

Sequence/structure based features are not available in most of the databases. Information given in the existing databases are not similar and several entries have ambiguous data. Moreover there is no database on disease causing and neutral mutations exclusively for membrane proteins. Further, there is no database for mutations and its ΔΔG (kcal/mol) on carbohydrate binding proteins.

The novelty of CarbDisMut is to provide information on nucleotide level mutation, location of the mutant, neighbouring residues of the mutant, origin of the mutation chromosome number, genomic position and disease class. Further, we have predicted ΔΔG (kcal/mol) for the mutations if structural information is available.

Proteins are linked to their accession numbers from UniProt, 3D structure from Protein Data Bank (PDB) and GlyGen databases, whereas carbohydrates are linked to Glycosciences.de database.

Please send us a request by sending the mail to the address available in the contact page.

Select the disease class from the search options and display options so that mutations related to particular disease class will be displayed.

There is a range of non-random pairing of residues in the neighboring positions and the pair preference is different for each of the amino acids in the primary structure of the proteins. This might play a vital role in short-range interactions, which accelerate the protein folding and stability.