TRIM7
SRC
Gene Ontology Biological Process
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- Ras protein signal transduction [TAS]
- T cell costimulation [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- bone resorption [IBA, ISS]
- cell adhesion [IBA]
- cellular response to peptide hormone stimulus [IBA]
- cellular response to progesterone stimulus [ISS]
- central nervous system development [IBA]
- epidermal growth factor receptor signaling pathway [IBA, TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [IBA, TAS]
- integrin-mediated signaling pathway [IMP]
- intracellular estrogen receptor signaling pathway [IBA]
- intracellular signal transduction [IDA]
- leukocyte migration [TAS]
- membrane organization [TAS]
- negative regulation of anoikis [IMP]
- negative regulation of apoptotic process [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- negative regulation of extrinsic apoptotic signaling pathway [IMP]
- negative regulation of focal adhesion assembly [ISS]
- negative regulation of intrinsic apoptotic signaling pathway [IMP]
- negative regulation of mitochondrial depolarization [IMP]
- negative regulation of protein homooligomerization [IMP]
- neurotrophin TRK receptor signaling pathway [TAS]
- osteoclast development [IBA]
- peptidyl-tyrosine autophosphorylation [IBA]
- peptidyl-tyrosine phosphorylation [IDA]
- platelet activation [TAS]
- platelet-derived growth factor receptor signaling pathway [IBA]
- positive regulation of integrin activation [TAS]
- positive regulation of protein kinase B signaling [IMP]
- progesterone receptor signaling pathway [IBA, ISS]
- protein autophosphorylation [IDA]
- regulation of bone resorption [TAS]
- regulation of caveolin-mediated endocytosis [IMP]
- regulation of cell cycle [IBA]
- regulation of cell proliferation [IBA]
- regulation of cell-cell adhesion [IMP]
- regulation of early endosome to late endosome transport [IMP]
- regulation of epithelial cell migration [IMP]
- regulation of podosome assembly [IBA]
- regulation of vascular permeability [TAS]
- response to interleukin-1 [IMP]
- signal complex assembly [TAS]
- signal transduction [TAS]
- stress fiber assembly [IMP]
- transforming growth factor beta receptor signaling pathway [IMP]
Gene Ontology Molecular Function- SH2 domain binding [IPI]
- SH3/SH2 adaptor activity [TAS]
- enzyme binding [IPI]
- ephrin receptor binding [IPI]
- growth factor receptor binding [IPI]
- heme binding [IDA]
- hormone receptor binding [IBA]
- integrin binding [TAS]
- ion channel binding [IPI]
- kinase activity [TAS]
- non-membrane spanning protein tyrosine kinase activity [IBA, TAS]
- phosphoprotein binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA, TAS]
- protein tyrosine kinase activity [EXP, IDA, TAS]
- receptor binding [IPI]
- scaffold protein binding [IPI]
- SH2 domain binding [IPI]
- SH3/SH2 adaptor activity [TAS]
- enzyme binding [IPI]
- ephrin receptor binding [IPI]
- growth factor receptor binding [IPI]
- heme binding [IDA]
- hormone receptor binding [IBA]
- integrin binding [TAS]
- ion channel binding [IPI]
- kinase activity [TAS]
- non-membrane spanning protein tyrosine kinase activity [IBA, TAS]
- phosphoprotein binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA, TAS]
- protein tyrosine kinase activity [EXP, IDA, TAS]
- receptor binding [IPI]
- scaffold protein binding [IPI]
Gene Ontology Cellular Component
Biochemical Activity (Ubiquitination)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
The E3 ubiquitin ligase TRIM7 suppressed hepatocellular carcinoma progression by directly targeting Src protein.
Aberrant Src kinase activity is known to be involved in a variety of human malignancies, whereas the regulatory mechanism of Src has not been completely clarified. Here, we demonstrated that tripartite motif containing 7 (TRIM7) directly interacted with Src, induced Lys48-linked polyubiquitination of Src and reduced the abundance of Src protein in hepatocellular carcinoma (HCC) cells. We further identified TRIM7 ... [more]
Throughput
- Low Throughput
Additional Notes
- E2: UbcH5a/UBE2D1
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM7 SRC | 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 | - | |
| SRC TRIM7 | 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 | - | |
| TRIM7 SRC | Reconstituted Complex 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. | Low | - | BioGRID | - |
Curated By
- BioGRID