Anti-DDX58抗体(ab111037)

Involved in innate immune defense against viruses. Upon interaction with intracellular dsRNA produced during viral replication, triggers a transduction cascade involving MAVS/IPS1, which results in the activation of NF-kappa-B, IRF3 and IRF7 and the induction of the expression of antiviral cytokines such as IFN-beta and RANTES (CCL5). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). Essential for the production of interferons in response to RNA viruses including paramyxoviruses, influenza viruses, Japanese encephalitis virus and HCV.

Present in vascular smooth cells (at protein level).

Belongs to the helicase family.
Contains 2 CARD domains.
Contains 1 helicase ATP-binding domain.
Contains 1 helicase C-terminal domain.

The repressor domain controls homomultimerization and interaction with MAVS.
The helicase domain is responsible for dsRNA recognition.
The 2 CARD domains are responsible for interaction with and signaling through MAVS.
The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination.

Isgylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation.
Ubiquitinated. Undergoes 'Lys-63'-linked ubiquitination. Lys-172 is the critical site for TRIM25-mediated ubiquitination, for MAVS binding and to induce anti-viral signal transduction. Lys-154, Lys-164 and Lys-172 are critical sites for RNF135-mediated ubiquitination. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains.

Cytoplasm. Colocalized with TRIM25 at cytoplasmic perinuclear bodies.