IUPred3

IUPred3 predicts intrinsic disorder in proteins and protein regions, producing per-residue disorder propensities and enabling evolutionary conservation analysis of IDPs/IDRs.

Key Features:

• Energy Estimation Approach: Extends the IUPred energy estimation approach to compute disorder propensities from amino acid sequences.
• Advanced Smoothing Functions: Applies smoothing functions to reduce noise and improve prediction accuracy.
• Experimentally Verified Annotations: Integrates a dataset of experimentally verified ordered/disordered regions with unambiguous annotations to ground predictions in empirical data.
• Context-Dependent Disorder Prediction: Accepts amino acid sequences or UniProt ID/accession numbers and predicts the likelihood of each amino acid being part of a disordered region with context-dependent options.
• Evolutionary Conservation Analysis: Performs sequence conservation analysis across model organisms to explore evolutionary dynamics associated with protein disorder.

Scientific Applications:

• Protein Disorder Annotation: Annotating proteins and protein regions with per-residue disorder propensities to identify IDRs.
• Functional Studies of IDRs: Investigating roles of intrinsically disordered proteins and regions in biological processes.
• Evolutionary Dynamics of Disorder: Analyzing evolutionary conservation and divergence of disorder across model organisms to study IDP/IDR evolution.

Methodology:

IUPred3 applies the IUPred energy estimation approach to compute per-residue disorder propensities from amino acid sequences or UniProt accessions, employs smoothing functions to reduce prediction noise, integrates experimentally validated ordered/disordered annotations, and performs sequence conservation analysis across model organisms.