Welcome to Missense variant to proteIn StruCture Analysis web SuiTe



MISCAST is an online resource developed at the Stanley Center in the Broad Institute of MIT and Harvard, by a combined effort from the Genetics and Therapeutics group. The goal of MISCAST is to interpret single amino-acid-altering missense variants on protein 3-dimensional structure and to thereby forecast their biological impact.

The dataset provided on this website spans 1,330 human genes, including 406,449 population variants from gnomAD (release 2.1.1), 54,137 pathogenic variants and disease mutations from the ClinVar (February, 2019 release) and HGMD, (Professional release 2018.4) databases, respectively, and >14k molecularly-solved human protein 3D structures from the Protein Data Bank (PDB). The website provides two separate tracks. The Variant Summary Reports track provides an amino-acid-wise report, summarizing its pathogenic and population variant-associated protein features. The Variant Analysis Suite provides a platform for detailed exploration, analysis, and visualization of protein features and missense variants on 1D, 2D and 3D protein structure space.

Disclaimer: Please note that all content on this website is provided for academic and research purposes only. It has not undergone clinical validation, and should not be used for medical advice, diagnosis, or treatment. For best experience, please open Variant Analysis Suite on a laptop/desktop instead of any smaller screen.


Copyright © Broad Institute. All rights reserved.

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   Disclaimer: Please note that all content on this website is provided for academic and research purposes only. It has not undergone clinical validation, and should not be used for medical advice, diagnosis, or treatment.

Explore Protein Features of Missense Variants by Gene and Protein class







  3-class Secondary Structure


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  8-class Secondary Structure


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  Accessible Surface Area


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  Twenty Amino Acids and Physiochemical Property


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  Protein-protein Interaction types

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  Distance to Post-translational Modification (PTM) Types


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  UniProt-based Functional Features

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  3-class Secondary Structure

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  8-class Secondary Structure

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  Acessible Surface Area/Residue Exposure

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  Amino Acids and Physiochemical Property

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  Protein-protein Interactions

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  Post-translational Modifications (PTMs)

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  UniProt-based Functional Features

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