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
GRIN2B
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Phosphorylation)
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
Epidermal growth factor receptor promotes glioma progression by regulating xCT and GluN2B-containing N-methyl-d-aspartate-sensitive glutamate receptor signaling.
Autocrine and paracrine factors, including glutamate and epidermal growth factor (EGF), are potent inducers of brain tumor cell invasion, a pathological hallmark of malignant gliomas. System xc(-) consists of xCT and CD98hc subunits and functions as a plasma membrane antiporter for the uptake of extracellular cystine in exchange for intracellular glutamate. We previously showed that the EGF receptor (EGFR) interacts ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EGFR GRIN2B | 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 | - | |
| EGFR GRIN2B | 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