FHOD1
Gene Ontology Biological Process
Gene Ontology Molecular Function
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-localization
Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.
Publication
The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation.
Formins induce the nucleation and polymerization of unbranched actin filaments. They share three homology domains required for profilin binding, actin polymerization, and regulation. Diaphanous-related formins (DRFs) are activated by GTPases of the Rho/Rac family, whose interaction with the N-terminal formin domain is thought to displace a C-terminal Diaphanous-autoregulatory domain (DAD). We have determined the structure of the N-terminal domains of ... [more]
Throughput
- Low Throughput
Additional Notes
- Source of RAC1 not clear
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RAC1 FHOD1 | 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 FHOD1 | 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