1. What is MutHTP?

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

2. What are the different types of mutations available in MutHTP?

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.

3. How does MutHTP differ from the existing databases?

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.

4. What are the novel features of the database?

The novelty of MutHTP is to provide information on nucleotide level mutation, location of the mutant with respect to the membrane protein topology, neighbouring residues of the mutant, origin of the mutation chromosome number, genomic position and disease class.

5. How can we get more information on proteins?

Proteins are linked to their accession numbers from UniProt and 3D structure from Protein Data Bank (PDB).

6. How to download the data?

Please send us a request by filling the form given on the download page.

7. How to retrieve disease specific mutations?

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

8. What is the importance of neighboring residues of the mutation site?

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.