Prediction of Intrinsically Unstructured Proteins

Intrinsically disordered proteins (IDPs) have no single well-defined tertiary structure under native conditions. IUPred3 is a combined web interface that allows to identify disordered protein regions using IUPred2 and disordered binding regions using ANCHOR2. IUPred3 is also capable of identifying protein regions that do or do not adopt a stable structure depending on the redox state of their environment. IUPred3 supersedes the previous IUPred and ANCHOR servers. For new features included in IUPred3, see the New features section. The IUPred3 web server can be accessed for free.

For a detailed description of how to run IUPred3 using various features and how to interpret the output, see the How to use and Examples sections. For a simple demonstration of how to input data, see the example 1 or example 2.

In order to see an example or our novel Disorder conservation tool click here!
Analysis type
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Primary citations

Gábor Erdős, Mátyás Pajkos, Zsuzsanna Dosztányi
IUPred3: prediction of protein disorder enhanced with unambiguous experimental annotation and visualization of evolutionary conservation
Nucleic Acids Research 2021;49(W1):W297-W303.

Bálint Mészáros, Gábor Erdős, Zsuzsanna Dosztányi
IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding
Nucleic Acids Research 2018;46(W1):W329-W337.

Gábor Erdős, Zsuzsanna Dosztányi
Analyzing Protein Disorder with IUPred2A
Current Protocols in Bioinformatics 2020;70(1):e99

Additional citations

Zsuzsanna Dosztányi
Prediction of protein disorder based on IUPred
Protein Science 2017;27:331-340.

Dosztányi Z, Csizmók V, Tompa P, Simon I.
The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
J Mol Biol. 2005;347:827-39.

Mészáros B, Simon I, Dosztányi Z.
Prediction of protein binding regions in disordered proteins
PLoS Comput Biol. 2009;5:e1000376.