About MutPred
MutPred is a web application tool developed to classify an amino acid substitution (AAS)
as disease-associated or neutral in human. In addition, it predicts molecular cause of
disease/deleterious AAS. MutPred is based upon SIFT [1] and a gain/loss of 14 different
structural and functional properties. For instance, gain of helical propensity or loss of
a phosphorylation site. It was trained using the deleterious mutations from the Human Gene
Mutation Database [2] and neutral polymorphisms from Swiss-Prot [3]. Current version of
MutPred is 1.2. The update consists of replacing SIFT score by a more stable version of
code that calculates evolutionary conservation. In addition, the I-mutant software was
replaced by a more stable MUpro [4], by the Baldi group. The training data set was updated
to contain 39,218 disease-associated mutations from HGMD and 26,439 putatively neutral
substitutions from Swiss-Prot.
How do I interpret the results?
The output of MutPred contains a general score (g), i.e., the probability that the
amino acid substitution is deleterious/disease-associated, and top 5 property scores
(p), where p is the P-value that certain structural and functional
properties are impacted.
Certain combinations of high values of general scores and low values of property scores
are referred to as hypotheses.
- Scores with g > 0.5 and p < 0.05 are referred to as actionable
hypotheses.
- Scores with g > 0.75 and p < 0.05 are referred to as confident
hypotheses.
- Scores with g > 0.75 and p < 0.01 are referred to as very
confident hypotheses.
MutPred is a collaborative effort between the Mooney group from the University of Washington
and the Radivojac group from the School of Informatics and Computing, Indiana
University.
We welcome any suggestions and comments.
Supported By
The work is funded by:
- NIH K22LM009135 (PI: Mooney)
- NIH 1R01LM009722 (PI: Mooney)
- NIH 5R01LM009722 (PI: Mooney)
- Indiana Genomics Initiative. The Indiana Genomics Initiative (INGEN) is supported in part by Lily Endowment.
- National Science Foundation, DBI‐0644017 (PI: Predrag Radivojac)
Citing This Web Site
Li B, Krishnan VG, Mort ME, Xin F, Kamati KK, Cooper DN, Mooney SD, Radivojac P. Automated inference of molecular mechanisms of disease from amino acid substitutions. Bioinformatics (2009) 25(21): 2744-2750.
References
- Ng, P.C. and Henikoff, S. (2003) SIFT: Predicting amino acid changes that affect
protein function, Nucleic Acids Res, 31, 3812-3814.
- Stenson, P.D., et al. (2009) The Human Gene Mutation Database: 2008 update,
Genome Med, 1, 13.
- Boeckmann, B., et al. (2003) The SWISS-PROT protein knowledgebase and its
supplement TrEMBL in 2003, Nucleic Acids Res, 31, 365-370.
- Cheng, J., Randall. A. and Baldi, P. (2006) Prediction of Protein Stability Changes
for Single-Site Mutations Using Support Vector Machines. Proteins: Structure, Function,
Bioinformatics, 62, 1125-1132.
Contact Us
Prof. Predrag Radivojac
Department of Computer Science and Informatics
Indiana University
150 S. Woodlawn Avenue
Bloomington, IN 47405
Tel: (812) 856-1851
Web:
www.cs.indiana.edu/~predrag
Prof. Sean Mooney
Department of Biomedical Informatics and Medical Education
Universiy of Washington
850 Republican Street
Seattle, WA 98109
Tel: (206) 685-0249
Web:
http://faculty.washington.edu/sdmooney
Disclaimer
The purpose of this resource is to distribute functional prediction of mutation
data. The data is meant to be used for basic research. Do not use this data to make
clinical decisions.
