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
CBLC
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation.
The Cbl family proteins Cbl, Cbl-b, and Cbl-c/Cbl-3 are thought to regulate signaling through protein-tyrosine kinases, positively as scaffold proteins and negatively as ubiquitin ligases. However, the precise signaling pathways and target proteins for each Cbl family member are not well understood. Here we show that Src is a preferential target of Cbl-c for degradation. Although exogenous expression of all ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CBLC 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 CBLC | 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 | 693382 | |
| CBLC SRC | Biochemical Activity Biochemical Activity 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. | Low | - | BioGRID | 946864 | |
| CBLC SRC | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| CBLC SRC | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | 693379 |
Curated By
- BioGRID