RHOA
Gene Ontology Biological Process
- GTP catabolic process [TAS]
- Rho protein signal transduction [TAS]
- actin cytoskeleton organization [TAS]
- apical junction assembly [IMP]
- apolipoprotein A-I-mediated signaling pathway [IMP]
- axon guidance [TAS]
- blood coagulation [TAS]
- cleavage furrow formation [IDA]
- negative chemotaxis [IMP]
- negative regulation of axonogenesis [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- ossification involved in bone maturation [ISS]
- phosphatidylinositol-mediated signaling [TAS]
- platelet activation [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IEP]
- positive regulation of NF-kappaB import into nucleus [NAS]
- positive regulation of axonogenesis [TAS]
- positive regulation of cytokinesis [IMP]
- positive regulation of neuron differentiation [IMP]
- positive regulation of stress fiber assembly [IDA]
- regulation of axonogenesis [TAS]
- regulation of cell migration [IMP]
- regulation of osteoblast proliferation [ISS]
- regulation of small GTPase mediated signal transduction [TAS]
- small GTPase mediated signal transduction [TAS]
- spindle assembly involved in mitosis [IMP]
- substantia nigra development [IEP]
- trabecula morphogenesis [ISS]
- transforming growth factor beta receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RHOC
Gene Ontology Biological Process
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
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRASG13D.
Protein-protein-interaction networks (PPINs) organize fundamental biological processes, but how oncogenic mutations impact these interactions and their functions at a network-level scale is poorly understood. Here, we analyze how a common oncogenic KRAS mutation (KRASG13D) affects PPIN structure and function of the Epidermal Growth Factor Receptor (EGFR) network in colorectal cancer (CRC) cells. Mapping >6000 PPIs shows that this network is ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RHOC RHOA | 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. | Low | - | BioGRID | 3334370 | |
| RHOC RHOA | 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 | 3367302 | |
| RHOC RHOA | 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 | 1 | BioGRID | 2217013 | |
| RHOC RHOA | 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 | 1 | BioGRID | 3098608 | |
| RHOA RHOC | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | - |
Curated By
- BioGRID