The function of an IDP/IDR. Includes both active functions, i.e. performed on other proteins, and self-functions.
Targeting post-translational modification.
Guides the addition of a phosphate to the protein.
Guides the addition of an acetyl group to the protein.
Guides the addition of a methyl group to the protein.
Guides the addition of a sugar, such as a glycan, during chemical modification of the protein.
Guides the addition of a ubiquitin moiety for regulating the function and/or degradation of the protein.
Guides the addition of a fatty acyl group during chemical modification of the protein.
Guides the addition of a myristoyl group during chemical modification of the protein.
Guides the addition of a palmitoyl group during chemical modification of the protein.
Guides the regulatory cleavage of the polypeptide chain.
Guides the addition of ADP-ribose moietie(s) to a protein, in cell signaling, DNA repair, gene regulation and apoptosis.
The possible transitions occurring between different structural states.
Transition from a disordered state to an ordered state.
Transition from a disordered state to a molten globule state.
Transition from a disordered state to a pre-molten globule state.
Transition from a molten globule state to an ordered state.
Transition from a molten globule state to a pre-molten globule state.
Transition from a pre-molten globule state to an ordered state.
Transition from an ordered state to a disordered state.
Transition from an ordered state to a molten globule state.
Transition from an ordered state to a pre-molten globule state.
Transition from a pre-molten globule state to a disordered state.
Transition from a pre-molten globule state to a molten globule state.
Transition from a molten globule state to a disordered state.
The possible structural state populated by a given protein region.
A non-compact state in which atoms lack a fixed or ordered three-dimensional structure.
A compact state, with native secondary structure but lacking specific native tertiary interactions.
A condensed but not compact state, with residual secondary structure, describing many native and non-native conformations in rapid equilibrium.
A compact state in which atoms have a stable three-dimensional structure.
Functions directly associated with the disordered state of proteins that stem from their ability to shift between conformational states without becoming structured. Includes entropic bristles, clocks and springs.
Unstructured region connecting, providing separation and permitting movement between adjacent functional regions, e.g. structured domains or disordered motifs.
Intrinsically disordered region localized at the N-terminus of a protein.
Intrinsically disordered region localized at the C-terminus of a protein.
Protein interaction in cis that auto-regulates the protein function or its assembly.
Protein interaction in cis that auto-inhibits the protein function.
Protein interaction in cis that auto-activates the protein function.
Protein interaction in cis required for dimerization or oligomerization of a protein.