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| Structural/functional types | Functional classes | Functional subclasses | Detection methods |
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List of all functional subclasses
This functional classification scheme was based on: Dunker AK, Brown CJ, Lawson JD, Iakoucheva LM, Obradovic Z. "Intrinsic disorder and protein function." Biochemistry. 2002 41(21):6573-82.
| Function subclass | Description |
|---|---|
| Acetylation | Guides the addition of an acetyl group during chemical modification of the protein. |
| ADP-ribosylation | Regulates vesicle biogenesis in intracellular traffic; may modulate vesicle budding and uncoating within the Golgi apparatus; is involved in protein trafficking. |
| Apoptosis Regulation | Regulation of cell fate. |
| Autoregulatory | Involved in the regulation of protein function/activity. |
| Cofactor/heme binding | Binds to the appropriate cofactor(s) and/or heme(s). |
| Disordered region is not essential for protein function | Region has been shown experimentally to perform no function. |
| DNA bending | Mediates DNA bending. |
| DNA unwinding | Promotes the unwinding of DNA. |
| Electron transfer | Participates in the electron transfer. |
| Entropic bristle | A disordered region that creates a zone of exclusion by its entropic movement. |
| Entropic clock | Provide a timing mechanism arising from random searches such as those observed in the ball-and-chain model for closure of voltage-gated ion channels. |
| Entropic spring | Provides a restoring force resulting from randomization of bond torsion angles that become restricted upon stretching. |
| Fatty acylation (myristolation and palmitoylation) | Guides the addition of a fatty acyl group during chemical modification of the protein. |
| Flexible linkers/spacers | Provides separation and permits movement between adjacent domains. |
| Glycosylation | Guides the addition of a sugar, such as a glycan, during chemical modification of the protein. |
| Intraprotein interaction | Directs the binding of the disordered region to another location within the parent protein. |
| Metal binding | Binds to metal ions. |
| Methylation | Guides the addition of a methyl group during chemical modification of the protein. |
| Nuclear localization | Acts as a tag on the protein surface to confine the protein to the cell nucleus through the nuclear pore complex. |
| Phosphorylation | Guides the addition of a phosphate to the protein. |
| Polymerization | Facilitates polymerization. |
| Protein detergent | Binds to hydrophobic groups, thus making them more soluble. |
| Protein-DNA binding | Binds to DNA. |
| Protein-genomic RNA binding | Binds to genomic RNA. |
| Protein inhibitor | Binds to a protein and decreases the protein's activity. |
| Protein-lipid interaction | Located at the interface of the protein and its lipid partner. |
| Protein-mRNA binding | Binds to mRNA. |
| Protein-protein binding | Binds to interacting protein partner(s). |
| Protein-rRNA binding | Binds to rRNA. |
| Protein-tRNA binding | Binds to tRNA. |
| Regulation of proteolysis in vivo | Directs protein lysis under physiological conditions within the cell. |
| Self-transport through channel | Allows movement of proteins through membrane channels. |
| Structural mortar | Ribosomal proteins that fill the gaps and cracks of rRNA. |
| Substrate/ligand binding | Binds to substrate(s) and/or ligand(s). |
| Transactivation (transcriptional activation) | Mediates transcriptional activation. |
| Unknown | No experimental evidence supporting or disproving the role of the region in protein function. |
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