EGFR
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- MAPK cascade [NAS]
- activation of phospholipase A2 activity by calcium-mediated signaling [TAS]
- activation of phospholipase C activity [TAS]
- axon guidance [TAS]
- cell proliferation [IDA]
- cell surface receptor signaling pathway [IDA]
- cellular response to epidermal growth factor stimulus [ISS]
- cellular response to estradiol stimulus [IDA]
- epidermal growth factor receptor signaling pathway [IDA, TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [TAS]
- learning or memory [ISS]
- negative regulation of apoptotic process [IMP]
- negative regulation of epidermal growth factor receptor signaling pathway [TAS]
- negative regulation of protein catabolic process [IDA]
- neurotrophin TRK receptor signaling pathway [TAS]
- ossification [NAS]
- peptidyl-tyrosine phosphorylation [IDA, IMP, TAS]
- phosphatidylinositol-mediated signaling [TAS]
- positive regulation of DNA repair [IDA]
- positive regulation of DNA replication [IDA]
- positive regulation of ERK1 and ERK2 cascade [IDA]
- positive regulation of MAP kinase activity [IDA]
- positive regulation of catenin import into nucleus [IMP]
- positive regulation of cell migration [IMP]
- positive regulation of cell proliferation [IDA]
- positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [IDA]
- positive regulation of epithelial cell proliferation [IDA]
- positive regulation of nitric oxide biosynthetic process [IDA]
- positive regulation of phosphorylation [IDA]
- positive regulation of protein kinase B signaling [IMP]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein autophosphorylation [IMP]
- protein insertion into membrane [TAS]
- regulation of nitric-oxide synthase activity [IDA]
- regulation of peptidyl-tyrosine phosphorylation [IMP]
- response to UV-A [IDA]
- response to stress [NAS]
- signal transduction [IDA, TAS]
- single organismal cell-cell adhesion [IMP]
Gene Ontology Molecular Function- MAP kinase kinase kinase activity [NAS]
- actin filament binding [IDA]
- chromatin binding [IDA]
- double-stranded DNA binding [NAS]
- enzyme binding [IPI]
- epidermal growth factor-activated receptor activity [IDA, NAS]
- identical protein binding [IPI]
- nitric-oxide synthase regulator activity [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein phosphatase binding [IPI]
- protein tyrosine kinase activity [IDA, IMP, TAS]
- transmembrane receptor protein tyrosine kinase activity [TAS]
- transmembrane signaling receptor activity [IDA]
- ubiquitin protein ligase binding [IPI]
- MAP kinase kinase kinase activity [NAS]
- actin filament binding [IDA]
- chromatin binding [IDA]
- double-stranded DNA binding [NAS]
- enzyme binding [IPI]
- epidermal growth factor-activated receptor activity [IDA, NAS]
- identical protein binding [IPI]
- nitric-oxide synthase regulator activity [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein phosphatase binding [IPI]
- protein tyrosine kinase activity [IDA, IMP, TAS]
- transmembrane receptor protein tyrosine kinase activity [TAS]
- transmembrane signaling receptor activity [IDA]
- ubiquitin protein ligase binding [IPI]
Gene Ontology Cellular Component
CTNNA1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Positive Genetic
Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a less severe fitness defect than expected under a given condition. This term is reserved for high or low throughput studies with scores.
Publication
Genome-wide CRISPR screening reveals genetic modifiers of mutant EGFR dependence in human NSCLC.
EGFR-mutant NSCLCs frequently respond to EGFR tyrosine kinase inhibitors (TKIs). However, the responses are not durable, and the magnitude of tumor regression is variable, suggesting the existence of genetic modifiers of EGFR dependency. Here, we applied a genome-wide CRISPR-Cas9 screening to identify genetic determinants of EGFR TKI sensitivity and uncovered putative candidates. We show that knockout of RIC8A, essential for ... [more]
Throughput
- High Throughput
Ontology Terms
- growth abnormality (HP:0001507)
- viability (PATO:0000169)
Additional Notes
- CRISPR GI screen
- Cell Line: HCC-827
- Experimental Setup: Positive selection in response to EGFR TKI: erlotinib 1um
- GIST: A-phenotypic positive genetic interaction
- Library: CRISPRn (Cong, 2019)
- Significance Threshold: RSA<= -3 and Q3 z-score >=1
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EGFR CTNNA1 | 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 | 1517660 | |
| EGFR CTNNA1 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | High | - | BioGRID | 1504675 | |
| EGFR CTNNA1 | 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 | 0.01 | BioGRID | 3511124 | |
| CTNNA1 EGFR | 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. | Low | - | BioGRID | 3562771 |
Curated By
- BioGRID