ATG5
Gene Ontology Biological Process
- C-terminal protein lipidation [IBA]
- autophagic vacuole assembly [IMP]
- autophagy [IMP]
- blood vessel remodeling [IMP]
- cellular response to nitrogen starvation [IBA]
- heart contraction [IMP]
- mitochondrion degradation [IBA]
- negative regulation of apoptotic process [IMP]
- negative regulation of histone H4-K16 acetylation [IMP]
- negative regulation of protein ubiquitination [IMP]
- negative stranded viral RNA replication [IMP]
- nucleophagy [IBA]
- otolith development [IMP]
- positive regulation of mucus secretion [IMP]
- post-translational protein modification [IDA]
- regulation of cilium assembly [IMP]
- regulation of cytokine secretion involved in immune response [IMP]
- regulation of reactive oxygen species metabolic process [IMP]
- regulation of release of sequestered calcium ion into cytosol [IMP]
- response to drug [IMP]
- response to fungus [IMP]
- vasodilation [IMP]
- ventricular cardiac muscle cell development [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ATG12
Gene Ontology Biological Process
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
The ATG5 interactome links clathrin-mediated vesicular trafficking with the autophagosome assembly machinery.
Autophagosome formation involves the sequential actions of conserved ATG proteins to coordinate the lipidation of the ubiquitin-like modifier Atg8-family proteins at the nascent phagophore membrane. Although the molecular steps driving this process are well understood, the source of membranes for the expanding phagophore and their mode of delivery are only now beginning to be revealed. Here, we have used quantitative ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ATG5 ATG12 | 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 | 0.97 | BioGRID | 2666988 | |
| ATG12 ATG5 | Positive Genetic Positive Genetic Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a less severe fitness defect than expected under a given condition. This term is reserved for high or low throughput studies with scores. | Low | - | BioGRID | 2828218 | |
| ATG5 ATG12 | 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 | - | |
| ATG12 ATG5 | 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