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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 an anaphase-promoting complex. A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Interacting selectively and non-covalently with the insulin receptor. Interacting selectively and non-covalently with a complex of G-protein beta/gamma subunits. Interacting selectively and non-covalently with a mismatch repair complex. Interacting selectively and non-covalently with any protein complex (a complex of two or more proteins that may include other nonprotein molecules). Interacting selectively and non-covalently with an intermediate filament, a distinct elongated structure, characteristically 10 nm in diameter, that occurs in the cytoplasm of higher eukaryotic cells. Intermediate filaments form a fibrous system, composed of chemically heterogeneous subunits and involved in mechanically integrating the various components of the cytoplasmic space. Interacting selectively and non-covalently with an inhibin complex, a dimer of one inhibin-alpha subunit and one inhibin-beta subunit. Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells. Interacting selectively and non-covalently with an integrin. Interacting selectively and non-covalently with a heterotrimeric G-protein. Interacting selectively and non-covalently with an immunoglobulin. Interacting selectively and non-covalently with activin, a dimer of inhibin-beta subunits. Interacting selectively and non-covalently with a dynein complex, a protein complex that contains two or three dynein heavy chains and several light chains, and has microtubule motor activity. The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. Interacting selectively and non-covalently with a proteasome, a large multisubunit protein complex that catalyzes protein degradation. Interacting selectively and non-covalently with fibrinogen, a highly soluble hexameric glycoprotein complex that is found in blood plasma and is converted to fibrin by thrombin in the coagulation cascade.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein complex binding
Acc: GO:0032403
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with any protein complex (a complex of two or more proteins that may include other nonprotein molecules).
Proteins in PDR annotated with:
   This term: 288 [Search]
   Term or descendants: 537 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0032403 - protein complex binding (interactive image map)
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