ARFGAP1
Gene Ontology Biological Process
- COPI coating of Golgi vesicle [TAS]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- cellular protein metabolic process [TAS]
- endoplasmic reticulum unfolded protein response [TAS]
- membrane organization [TAS]
- positive regulation of GTPase activity [IDA]
- retrograde vesicle-mediated transport, Golgi to ER [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ARF1
Gene Ontology Biological Process
- COPI coating of Golgi vesicle [TAS]
- GTP catabolic process [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class II [TAS]
- cellular copper ion homeostasis [IMP]
- dendritic spine organization [ISS]
- long term synaptic depression [ISS]
- membrane organization [TAS]
- phosphatidylinositol biosynthetic process [TAS]
- phospholipid metabolic process [TAS]
- post-Golgi vesicle-mediated transport [TAS]
- regulation of Arp2/3 complex-mediated actin nucleation [ISS]
- regulation of defense response to virus by virus [TAS]
- regulation of receptor internalization [ISS]
- retrograde vesicle-mediated transport, Golgi to ER [TAS]
- small molecule metabolic process [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Mutational analysis of the Arf1*GTP/Arf GAP interface reveals an Arf1 mutant that selectively affects the Arf GAP ASAP1.
Arf1 is a GTP binding protein that functions at a number of cellular sites to control membrane traffic and actin remodeling. Arf1 is regulated by site-specific GTPase-activating proteins (GAPs). The combined results of crystallographic and biochemical studies have led to the proposal that Arf1 GAPs differ in the specific interface formed with Arf1. To test this hypothesis, we have used ... [more]
Throughput
- Low Throughput
Additional Notes
- species of origin for bait and hit is unclear
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ARF1 ARFGAP1 | 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. | High | 0.2199 | BioGRID | 1258724 | |
| ARF1 ARFGAP1 | 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 | 2381443 | |
| ARFGAP1 ARF1 | 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