Search results for DDX58

Showing 20 results out of 59

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Protein (4 results from a total of 5)

Identifier: R-HSA-168917
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: O95786
Identifier: R-HSA-6782770
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: DDX58: O95786
Identifier: R-HSA-918191
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: DDX58: O95786
Identifier: R-HSA-3080568
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: DDX58: O95786

Interactor (1 results from a total of 1)

Identifier: O95786-1
Species: Homo sapiens
Primary external reference: UniProt: O95786-1

Reaction (4 results from a total of 17)

Identifier: R-HSA-936563
Species: Homo sapiens
Compartment: cytosol
ISG15 is an ubiquitin (Ub)-like protein which is conjugated to intracellular proteins via an isopeptide bond. Similar to ubiquitination, the conjugation of ISG15 (ISGylation) requires a three-step process, involving an E1 activating enzyme (UBE1L), an E2 conjugating enzyme (UbcM8/H8), and HERC5/Ceb1 an IFN-inducible ISG15-specific E3 ligase. ISG15 conjugation may play an important regulatory role in IFN-mediated antiviral responses. IFN induces ISG15 conjugation to DDX58 negatively regulating DDX58-mediated antiviral signaling. ISGylated DDX58 becomes subject to an irreversible biochemical process, such as proteolysis or proteasomeal degradation.
Identifier: R-HSA-168935
Species: Homo sapiens
Compartment: cytosol
Probable ATP-dependent RNA helicase DDX58 (DDX58, RIG-I, RIG-1) has two caspase recruitment domains (CARD) in its N-terminus, a DExD/H helicase domain with an ATP binding motif in the middle and a repressor domain (RD) in the C-terminus. In the absence of appropriate stimulation, DDX58 is in a 'closed' conformation in which the repressor domain phyically interacts with the helicase domain masking CARD. Upon viral infection, the free triphosphate structure at the 5' end of viral RNAs activates DDX58 by binding to its RNA helicase domain. This provokes a change in DDX58 conformation exposing the CARD leading to DDX58 dimerization, allowing it to interact with Mitochondrial antiviral-signaling protein (MAVS, IPS-1).
Identifier: R-HSA-918224
Species: Homo sapiens
Compartment: cytosol
On viral infection antiviral innate immune response receptor RIG-I (RIG‑I, also known as probable ATP-dependent RNA helicase DDX58 or DEAD box protein 58) undergoes robust ubiquitination at its N-terminal Caspase activation and recruitment domain (CARD) region. E3 ubiquitin/ISG15 ligase TRIM25 (TRIM25), a member of the tripartite motif (TRIM) protein family and E3 ubiquitin-protein ligase RNF135 (RNF135, REUL) are the E3 ligases involved in K63-linked polyubiquitination (K63polyUb) of DDX58. TRIM25 contains a cluster of domains including a RING-finger domain, a B box/coiled-coil domain and a SPRY domain. The interaction is mediated by the SPRY domain of TRIM25 and the N-terminal CARDs of DDX58. The polyubiquitin chains added by TRIM25 are unanchored. The lysine-172 (K172) residue of DDX58 is critical for efficient TRIM25-mediated ubiquitination and for binding of Mitochondrial Antiviral-Signaling protein (MAVS, IPS-1), as well as the ability of DDX58 to induce antiviral signal transduction. RNF135 associates with DDX58 through its PRY and SPRY domains. The K154, K164, and K172 residues of the DDX58 CARD domain are critical for efficient RNF135-mediated ubiquitination and for the ability of DDX58 to induce antiviral signal transduction. (Michaela et al. Goa et al. 2009).

The severe acute respiratory syndrome coronavirus type 1 (SARS-CoV-1) N protein was found to inhibit TRIM25-mediated DDX58 ubiquitination upon coexpression in HEK293T cells in a dose-dependent manner (Hu Y et al. 2017).

Identifier: R-HSA-8985153
Species: Homo sapiens
Compartment: cytosol
Interferon-dependent antiviral mechanisms trigger activation of 5'-triphosphorylated 2'-5'oligoadenylate synthetase (OAS) proteins which bind double-stranded RNA and catalyze the synthesis of 5'-triphosphorylated 2'-5' oligoadenylates from ATP (Kristiansen et al. 2011). The p59 protein encoded by the OAS-like (OASL) gene is an atypical member of the OAS family in the sense that it lacks the characteristic 2'-5' oligoadenylate synthetase activity (Hartmann et al. 1998; Rebouillat et al. 1998). Furthermore, OASL contains two tandem ubiquitin-like domains (UBL) in the C-terminus, which are absent in other OAS proteins (Hartmann et al. 1998; Rebouillat et al. 1998). OASL is rapidly induced by virus infection via interferon regulatory factor 3 (IRF3) as well as by IFN signaling and has been shown to have antiviral activities, which requires the UBL domain (Melchjorsen et al. 2009; Sarkar and Sen 2004; Marques et al. 2008; Schoggins et al. 2011). OASL is thought to interact with and enhance RIG1 (DDX58) signaling through its C-terminal ubiquitin-like domain (UBL) by mimicking polyubiquitin (Zhu J et al. 2014). Loss of OASL expression reduced DDX58 signaling and enhanced virus replication in human cells. Conversely, OASL expression suppressed replication of a number of viruses in a DDX58-dependent manner and enhanced DDX58-mediated IFN induction (Zhu J et al. 2014).

Set (4 results from a total of 8)

Identifier: R-HSA-5690188
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-936436
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-983460
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-5696897
Species: Homo sapiens
Compartment: cytosol

Complex (4 results from a total of 25)

Identifier: R-HSA-168906
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-6782841
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-936557
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-6782844
Species: Homo sapiens
Compartment: cytosol

Pathway (2 results from a total of 2)

Identifier: R-HSA-936440
Species: Homo sapiens
As with other cytokine systems, production of type I IFN is a transient process, and can be hazardous to the host if unregulated, resulting in chronic cellular toxicity or inflammatory and autoimmune diseases. RIG-I-mediated production of IFN can, in turn, increase the transcription of RIG-I itself, thus setting into motion an IFN amplification loop, which if left unchecked, could become deleterious to the host. This module mainly focuses on the endogenous negative regulation of the RIG-I-like receptor (RLR) family proteins RIG-I and MDA5.
Identifier: R-HSA-168928
Species: Homo sapiens
Compartment: mitochondrial outer membrane
RIG-I-like helicases (RLHs) the retinoic acid inducible gene-I (RIG-I) and melanoma differentiation associated gene 5 (MDA5) are RNA helicases that recognize viral RNA present within the cytoplasm. Functionally RIG-I and MDA5 positively regulate the IFN genes in a similar fashion, however they differ in their response to different viral species. RIG-I is essential for detecting influenza virus, Sendai virus, VSV and Japanese encephalitis virus (JEV), whereas MDA5 is essential in sensing encephalomyocarditis virus (EMCV), Mengo virus and Theiler's virus, all of which belong to the picornavirus family. RIG-I and MDA5 signalling results in the activation of IKK epsilon and (TKK binding kinase 1) TBK1, two serine/threonine kinases that phosphorylate interferon regulatory factor 3 and 7 (IRF3 and IRF7). Upon phosphorylation, IRF3 and IRF7 translocate to the nucleus and subsequently induce interferon alpha (IFNA) and interferon beta (IFNB) gene transcription.

Icon (1 results from a total of 1)

Species: Homo sapiens
Curator: Steve Jupe
Designer: Cristoffer Sevilla
DDX58 icon
Probable ATP-dependent RNA helicase
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