DDX3X
Gene Ontology Biological Process
- ATP catabolic process [IDA, TAS]
- DNA duplex unwinding [IDA]
- RNA secondary structure unwinding [IDA]
- cellular response to arsenic-containing substance [IDA]
- cellular response to osmotic stress [IDA]
- chromosome segregation [IMP]
- extrinsic apoptotic signaling pathway via death domain receptors [IMP]
- innate immune response [IMP]
- intracellular signal transduction [IDA]
- intrinsic apoptotic signaling pathway [IMP]
- mature ribosome assembly [IMP]
- negative regulation of apoptotic process [IMP]
- negative regulation of cell growth [IDA]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- negative regulation of intrinsic apoptotic signaling pathway [IMP]
- negative regulation of protein complex assembly [IDA]
- negative regulation of translation [IMP]
- positive regulation of G1/S transition of mitotic cell cycle [IMP]
- positive regulation of apoptotic process [IMP]
- positive regulation of cell growth [IMP]
- positive regulation of chemokine (C-C motif) ligand 5 production [TAS]
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- positive regulation of interferon-beta production [TAS]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of translation [IDA]
- positive regulation of translational initiation [IMP]
- positive regulation of viral genome replication [IMP]
- response to virus [IDA]
- stress granule assembly [IDA]
Gene Ontology Molecular Function- ATP-dependent DNA helicase activity [IDA]
- ATP-dependent RNA helicase activity [IDA]
- ATPase activity [IDA]
- DNA binding [IDA]
- RNA binding [IDA]
- RNA stem-loop binding [IDA]
- eukaryotic initiation factor 4E binding [IDA]
- mRNA 5'-UTR binding [IDA]
- poly(A) RNA binding [IDA]
- poly(A) binding [IDA]
- protein binding [IPI]
- ribosomal small subunit binding [IDA]
- transcription factor binding [IDA]
- translation initiation factor binding [IDA]
- ATP-dependent DNA helicase activity [IDA]
- ATP-dependent RNA helicase activity [IDA]
- ATPase activity [IDA]
- DNA binding [IDA]
- RNA binding [IDA]
- RNA stem-loop binding [IDA]
- eukaryotic initiation factor 4E binding [IDA]
- mRNA 5'-UTR binding [IDA]
- poly(A) RNA binding [IDA]
- poly(A) binding [IDA]
- protein binding [IPI]
- ribosomal small subunit binding [IDA]
- transcription factor binding [IDA]
- translation initiation factor binding [IDA]
Gene Ontology Cellular Component
RPL4
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- cellular protein metabolic process [TAS]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- translation [NAS, TAS]
- translational elongation [TAS]
- translational initiation [TAS]
- translational termination [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral transcription [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
TRIM25 and DEAD-Box RNA Helicase DDX3X Cooperate to Regulate RIG-I-Mediated Antiviral Immunity.
The cytoplasmic retinoic acid-inducible gene-I (RIG-I)-like receptors (RLRs) initiate interferon (IFN) production and antiviral gene expression in response to RNA virus infection. Consequently, RLR signalling is tightly regulated by both host and viral factors. Tripartite motif protein 25 (TRIM25) is an E3 ligase that ubiquitinates multiple substrates within the RLR signalling cascade, playing both ubiquitination-dependent and -independent roles in RIG-I-mediated ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| DDX3X RPL4 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | - | BioGRID | 3430276 |
Curated By
- BioGRID