CDH1
Gene Ontology Biological Process
- adherens junction organization [IMP, TAS]
- apoptotic process [TAS]
- cell junction assembly [TAS]
- cell-cell junction organization [TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- cellular response to indole-3-methanol [IDA]
- cellular response to lithium ion [IDA]
- establishment of protein localization to plasma membrane [IMP]
- extracellular matrix disassembly [TAS]
- extracellular matrix organization [TAS]
- homophilic cell adhesion via plasma membrane adhesion molecules [NAS]
- negative regulation of cell-cell adhesion [IMP]
- positive regulation of transcription factor import into nucleus [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- protein localization to plasma membrane [IDA]
- regulation of immune response [TAS]
- single organismal cell-cell adhesion [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- actin cytoskeleton [IDA]
- aggresome [IDA]
- apical junction complex [IDA]
- catenin complex [IDA]
- cell junction [IDA, TAS]
- cell-cell adherens junction [IDA]
- cytoplasm [IDA]
- cytoplasmic side of plasma membrane [IDA]
- extracellular region [TAS]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- integral component of membrane [IDA]
- lateral plasma membrane [IDA]
- perinuclear region of cytoplasm [IDA]
- plasma membrane [IDA, TAS]
- trans-Golgi network [IMP]
DDX39B
Gene Ontology Biological Process
- ATP catabolic process [IDA, TAS]
- RNA secondary structure unwinding [IDA]
- RNA splicing [IDA]
- mRNA export from nucleus [IDA, IGI]
- mRNA splicing, via spliceosome [IGI]
- negative regulation of DNA damage checkpoint [IMP]
- positive regulation of DNA-templated transcription, elongation [IMP]
- spliceosomal complex assembly [IDA]
- viral mRNA export from host cell nucleus [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
DDX39B K63-linked ubiquitination mediated by TRIM28 promotes NSCLC metastasis by enhancing ECAD lysosomal degradation.
Metastasis is a leading cause of treatment failure and high mortality in non-small cell lung cancer (NSCLC). Recently, we demonstrated that DEAD box helicase 39B (DDX39B) was upregulated and activated metabolic reprogramming in colorectal cancer and hepatocellular carcinoma. However, the function of DDX39B and the therapeutic potential for targeting DDX39B in NSCLC remain unclear. Herein, we discovered that DDX39B was ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| DDX39B CDH1 | Affinity Capture-MS 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. | High | - | BioGRID | 2472537 | |
| DDX39B CDH1 | Affinity Capture-MS 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. | High | - | BioGRID | - | |
| DDX39B CDH1 | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| CDH1 DDX39B | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| DDX39B CDH1 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - | |
| CDH1 DDX39B | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | - |
Curated By
- BioGRID