Structural/functional types Functional classes Functional subclasses Detection methods

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 subclassDescription
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.
Molecular shield Entropic chain that forms a physical barrier around a target protein thereby reducing interactions that lead to aggregation, i.e. dessication tolerance provided by LEA proteins.
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-Biocrystal binding Protein binding to mineral to form biocrystals in the biomineralization process.
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-RNA binding Binds to RNA
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).
Sulfation Guides the addition of a sulfate group to a protein. Also called sulfonation.
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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