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
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.
Publication
Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity.
RhoA/B/C and CDC42/Rac, which form two subgroups of the rho guanosine triphosphatase (GTPase) family, regulate various aspects of actin cytoskeleton organisation. In cytosol, guanosine diphosphate (GDP) dissociation inhibitor (GDI) interacts with and maintains rho GTPases in their inactive GDP-bound form. RhoGDI is a ubiquitously expressed GDI, whereas D4/LyGDI is hematopoietic cell-specific and 10-fold less potent than RhoGDI in binding to ... [more]
Throughput
- Low Throughput
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 | |
ARHGDIA RAC1 | 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 | 0.449 | BioGRID | 241766 | |
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 | - | |
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