DDX41 ubiquitination by TRIM21

Stable Identifier
Reaction [transition]
Homo sapiens
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TRIM21 (Ro52/SSA1) is a member of the TRIM (Tripartite Motif) family of E3 ligases. E3 activity of TRIM21 was found to be a RING domain-dependent and required E2-conjugating enzymes UBE2D1/2/3/4 and UBE2E1/2 (Espinosa A et al. 2011).

TRIM21 can form a complex with DDX41 leading to the K48-linked ubiquitination and degradation of DDX41 (Zhang Z et al. 2013).

Literature References
PubMed ID Title Journal Year
23222971 The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA

Yuan, B, Weng, L, Lu, N, Zhang, Z, Liu, YJ, Bao, M

Nat. Immunol. 2012
21862588 Anti-Ro52 autoantibodies from patients with Sjögren's syndrome inhibit the Ro52 E3 ligase activity by blocking the E3/E2 interface

Arrowsmith, CH, Sunnerhagen, M, Wahren-Herlenius, M, Sheng, Y, Ambrosi, A, Abelius, MS, Hennig, J, Espinosa, A, Anandapadmanaban, M, Nyberg, F

J. Biol. Chem. 2011
Catalyst Activity

ubiquitin-protein transferase activity of TRIM21 [cytosol]

Orthologous Events
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