Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).

Interacting selectively and non-covalently with a G protein-coupled receptor.

Interacting selectively and non-covalently with any protease or peptidase.

A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. A third class occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.

A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. A third class occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.

Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.

Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.

Interacting selectively and non-covalently with any enzyme.

Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock.

Interacting selectively and non-covalently with denatured proteins.

Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.

Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.

Interacting selectively and non-covalently with the enzyme histone deacetylase.

Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) that contributes to the process of protein folding.

Interacting selectively and non-covalently with a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.

Interacting selectively and non-covalently with NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters.

Interacting selectively and non-covalently with an unfolded protein.

Interacting selectively and non-covalently with a C3HC4-type zinc finger domain of a protein. The C3HC4-type zinc finger is a variant of RING finger, is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C, where X is any amino acid. Many proteins containing a C3HC4-type RING finger play a key role in the ubiquitination pathway.

Interacting selectively and non-covalently with a disordered domain of a protein.