background:
Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). The first step in the ubiquitination process requires the ATP-dependent activation of the ubiquitin SLCterminus and the assembly of multi-ubiquitin chains by the E1 enzyme. The ubiquitin chain is then conjugated to the E2 enzyme to generate an intermediate ubiquitin-E2 complex. The E3 enzyme then catalyzes the transfer of ubiquitin from E2 to the appropriate protein substrate, thereby targeting that substrate for degradation. A wide range of enzymes facilitate this proteolytic ubiquitin pathway, one of which is UBE2E2 (also known as UBCH8 in human), which functions as an E2 enzyme and catalyzes the ATP-dependent covalent attachment of ubiquitin to target proteins, thereby playing an important role in protein degradation.
Function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination.
Similarity:
Belongs to the ubiquitin-conjugating enzyme family.
Database links:
UniProtKB/Swiss-Prot: Q96LR5.1
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
|
|
