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
HSPA4
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
In silico prediction of physical protein interactions and characterization of interactome orphans.
Protein-protein interactions (PPIs) are useful for understanding signaling cascades, predicting protein function, associating proteins with disease and fathoming drug mechanism of action. Currently, only ∼10% of human PPIs may be known, and about one-third of human proteins have no known interactions. We introduce FpClass, a data mining-based method for proteome-wide PPI prediction. At an estimated false discovery rate of 60%, ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EGFR HSPA4 | 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 | 727296 | |
| EGFR HSPA4 | 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 HSPA4 | 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 HSPA4 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - | |
| EGFR HSPA4 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | High | - | BioGRID | 1505996 |
Curated By
- BioGRID