ARHGDIA
Gene Ontology Biological Process
- cellular component movement [TAS]
- negative regulation of apoptotic process [TAS]
- negative regulation of axonogenesis [TAS]
- negative regulation of cell adhesion [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- positive regulation of axonogenesis [TAS]
- regulation of axonogenesis [TAS]
- regulation of small GTPase mediated signal transduction [TAS]
- semaphorin-plexin signaling pathway [ISS]
- small GTPase mediated signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RAC1
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- GTP catabolic process [TAS]
- T cell costimulation [TAS]
- actin cytoskeleton organization [IGI]
- actin filament polymerization [TAS]
- anatomical structure morphogenesis [TAS]
- apoptotic signaling pathway [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell adhesion [TAS]
- cell motility [IDA]
- cell-matrix adhesion [NAS]
- cellular component movement [TAS]
- inflammatory response [TAS]
- innate immune response [TAS]
- intracellular signal transduction [TAS]
- lamellipodium assembly [IMP]
- localization within membrane [IMP]
- negative regulation of interleukin-23 production [IDA]
- negative regulation of receptor-mediated endocytosis [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- platelet activation [TAS]
- positive regulation of Rho protein signal transduction [TAS]
- positive regulation of apoptotic process [TAS]
- positive regulation of cell-substrate adhesion [IGI]
- positive regulation of focal adhesion assembly [IDA]
- positive regulation of lamellipodium assembly [IDA, IMP]
- positive regulation of neutrophil chemotaxis [IMP]
- positive regulation of protein phosphorylation [IMP]
- positive regulation of stress fiber assembly [IDA]
- positive regulation of substrate adhesion-dependent cell spreading [IDA]
- regulation of cell migration [IMP]
- regulation of defense response to virus by virus [TAS]
- regulation of hydrogen peroxide metabolic process [TAS]
- regulation of respiratory burst [IDA]
- response to wounding [TAS]
- ruffle organization [IDA, TAS]
- semaphorin-plexin signaling pathway [ISS]
- substrate adhesion-dependent cell spreading [IMP]
- viral process [TAS]
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
Large-scale mapping of human protein-protein interactions by mass spectrometry.
Mapping protein-protein interactions is an invaluable tool for understanding protein function. Here, we report the first large-scale study of protein-protein interactions in human cells using a mass spectrometry-based approach. The study maps protein interactions for 338 bait proteins that were selected based on known or suspected disease and functional associations. Large-scale immunoprecipitation of Flag-tagged versions of these proteins followed by ... [more]
Quantitative Score
- 0.449 [Confidence Score]
Throughput
- High Throughput
Ontology Terms
- cell line: hek-293 cell (BTO:0000007)
Additional Notes
- Exogenous expression of bait
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RAC1 ARHGDIA | 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 | 3326581 | |
| RAC1 ARHGDIA | 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 | - | |
| RAC1 ARHGDIA | 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 | 3365809 | |
| RAC1 ARHGDIA | 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 | - | |
| RAC1 ARHGDIA | 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 | 1103901 | |
| RAC1 ARHGDIA | 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 | - | |
| RAC1 ARHGDIA | 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 | - | |
| ARHGDIA RAC1 | 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 | 305959 | |
| RAC1 ARHGDIA | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - | |
| ARHGDIA RAC1 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - | |
| RAC1 ARHGDIA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| RAC1 ARHGDIA | Two-hybrid 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. | Low | - | BioGRID | - | |
| ARHGDIA RAC1 | Two-hybrid 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. | Low | - | BioGRID | - | |
| RAC1 ARHGDIA | Two-hybrid 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. | High | - | BioGRID | - |
Curated By
- BioGRID