PAK1
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- MAPK cascade [IDA]
- T cell costimulation [TAS]
- T cell receptor signaling pathway [TAS]
- actin cytoskeleton reorganization [IDA, IMP]
- axon guidance [TAS]
- branching morphogenesis of an epithelial tube [IMP]
- innate immune response [TAS]
- mitotic cell cycle [IBA]
- negative regulation of cell proliferation involved in contact inhibition [IMP]
- neuron projection morphogenesis [ISS]
- positive regulation of JUN kinase activity [IMP]
- positive regulation of intracellular estrogen receptor signaling pathway [IDA]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- positive regulation of protein phosphorylation [IMP]
- positive regulation of stress fiber assembly [IMP]
- protein autophosphorylation [IDA]
- protein phosphorylation [IDA]
- signal transduction by phosphorylation [IBA]
- wound healing [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PAK1
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- MAPK cascade [IDA]
- T cell costimulation [TAS]
- T cell receptor signaling pathway [TAS]
- actin cytoskeleton reorganization [IDA, IMP]
- axon guidance [TAS]
- branching morphogenesis of an epithelial tube [IMP]
- innate immune response [TAS]
- mitotic cell cycle [IBA]
- negative regulation of cell proliferation involved in contact inhibition [IMP]
- neuron projection morphogenesis [ISS]
- positive regulation of JUN kinase activity [IMP]
- positive regulation of intracellular estrogen receptor signaling pathway [IDA]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- positive regulation of protein phosphorylation [IMP]
- positive regulation of stress fiber assembly [IMP]
- protein autophosphorylation [IDA]
- protein phosphorylation [IDA]
- signal transduction by phosphorylation [IBA]
- wound healing [IMP]
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 |
---|---|---|---|---|---|---|
PAK1 PAK1 | 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 | - | |
PAK1 PAK1 | 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 | 2327651 | |
PAK1 PAK1 | 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 | 317168 | |
PAK1 PAK1 | 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 | 740069 | |
PAK1 PAK1 | 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 | - | |
PAK1 PAK1 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | Low | - | BioGRID | - |
Curated By
- BioGRID