ubiquitin protein ligase binding

Definition

Target type: molecularfunction

Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. [GOC:vp]

Ubiquitin protein ligase binding is a molecular function that describes the interaction of a protein with a ubiquitin protein ligase (E3). E3 ligases are enzymes that catalyze the attachment of ubiquitin, a small protein, to other proteins. This process, known as ubiquitination, is a highly regulated post-translational modification that can regulate a wide range of cellular processes, including protein degradation, signal transduction, DNA repair, and immune responses. The binding of an E3 ligase to a target protein is typically mediated by specific protein-protein interactions. These interactions can involve various domains and motifs, such as RING fingers, HECT domains, and U-box domains, which are commonly found in E3 ligases. The interaction between an E3 ligase and its target protein is often regulated by factors such as phosphorylation, cellular localization, and other signaling pathways. The precise nature of the interaction between an E3 ligase and its target protein can vary depending on the specific proteins involved. However, the general outcome of this interaction is the transfer of ubiquitin from a ubiquitin-conjugating enzyme (E2) to the target protein, leading to its ubiquitination. The attachment of ubiquitin can modify the target protein's activity, localization, or stability. This process is crucial for maintaining cellular homeostasis and for orchestrating cellular responses to various stimuli. Ubiquitin protein ligase binding is a critical regulatory mechanism involved in a multitude of cellular processes.'
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Proteins (89)

Compounds (3,400)