E3 ubiquitin-protein ligase TRAF7 (TRAF7)

E3 ubiquitin-protein ligase TRAF7 (TRAF7) is an atypical member of the tumor necrosis factor receptor-associated factor family, characterized by an N-terminal RING finger domain, multiple zinc-finger motifs, coiled-coil domain, and seven C-terminal WD40 repeats, which together mediate its activity as an E3 ubiquitin ligase and intracellular adaptor[1][4][5]. Unlike canonical TRAFs, TRAF7 interacts with signaling molecules (e.g., MEKK3, c-Myb) via its WD40 domain, and does not directly bind TNF receptors[5]. TRAF7 can mediate both ubiquitination and sumoylation, notably regulating proteins such as c-Myb, RelA/p65, NEMO, KLF4, and p53[1][2][5]. TRAF7 influences diverse biological processes, including apoptosis, immune response (by modulating NF-κB and type I interferon pathways), cell migration/invasion, and developmental events[3][4]. Dysregulation of TRAF7 is implicated in cancers (via promoting tumor growth, migration, and suppressing apoptosis), developmental defects, and potentially in inflammation and antiviral defense[2][3][4][6]. Disease-associated mutations are notably found in the WD40 and coiled-coil domains, impacting protein function and leading to pathologies[3].

Other names

RFWD1RNF119DKFZp586I021MGC7807RING finger and WD repeat-containing protein 1RING finger protein 119RING-type E3 ubiquitin transferase TRAF7TNF receptor-associated factor 7CAFDADD