Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP- induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3. Belongs to the ubiquitin-conjugating enzyme family. Note: This description may include information from UniProtKB.
Protein type: Ligase; EC 220.127.116.11; Ubiquitin conjugating system; Ubiquitin ligase
Cellular Component: protein complex; ubiquitin ligase complex
Molecular Function: protein binding; acid-amino acid ligase activity; nucleotide binding; ubiquitin-protein ligase activity; ATP binding; ligase activity
Biological Process: protein polyubiquitination; protein ubiquitination
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.