ATG5
Gene Ontology Biological Process
- C-terminal protein lipidation [IBA]
- autophagic vacuole assembly [IBA, ISS]
- autophagy [ISS]
- cellular response to nitrogen starvation [IBA]
- innate immune response [TAS]
- mitochondrion degradation [IBA]
- negative regulation of type I interferon production [TAS]
- nucleophagy [IBA]
- post-translational protein modification [ISS]
- regulation of cilium assembly [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
GNB2L1
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- negative regulation of Wnt signaling pathway [ISS]
- negative regulation of cell growth [IDA]
- negative regulation of gene expression [IMP]
- negative regulation of hydrogen peroxide-induced neuron death [IGI]
- negative regulation of phagocytosis [IMP]
- negative regulation of protein kinase B signaling [IMP]
- negative regulation of protein tyrosine kinase activity [IDA]
- negative regulation of translation [ISS]
- positive regulation of GTPase activity [IDA]
- positive regulation of apoptotic process [IDA, IMP]
- positive regulation of cAMP catabolic process [IMP]
- positive regulation of cell migration [IDA]
- positive regulation of cyclic-nucleotide phosphodiesterase activity [IMP]
- positive regulation of gastrulation [ISS]
- positive regulation of intrinsic apoptotic signaling pathway [IMP]
- positive regulation of mitochondrial depolarization [IMP]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of protein homooligomerization [IDA, IMP]
- positive regulation of protein phosphorylation [IDA]
- regulation of cell cycle [IDA]
- regulation of cell division [ISS]
- regulation of establishment of cell polarity [ISS]
- regulation of protein localization [ISS]
Gene Ontology Molecular Function- SH2 domain binding [IDA]
- cysteine-type endopeptidase activator activity involved in apoptotic process [IMP]
- enzyme binding [IPI]
- ion channel inhibitor activity [ISS]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein complex scaffold [TAS]
- protein homodimerization activity [IDA]
- protein kinase C binding [IDA]
- protein phosphatase binding [IPI]
- protein tyrosine kinase inhibitor activity [IDA]
- receptor binding [NAS]
- receptor tyrosine kinase binding [IDA]
- SH2 domain binding [IDA]
- cysteine-type endopeptidase activator activity involved in apoptotic process [IMP]
- enzyme binding [IPI]
- ion channel inhibitor activity [ISS]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein complex scaffold [TAS]
- protein homodimerization activity [IDA]
- protein kinase C binding [IDA]
- protein phosphatase binding [IPI]
- protein tyrosine kinase inhibitor activity [IDA]
- receptor binding [NAS]
- receptor tyrosine kinase binding [IDA]
Gene Ontology Cellular Component
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
ATG5 provides host protection acting as a switch in the atg8ylation cascade between autophagy and secretion.
ATG5 is a part of the E3 ligase directing lipidation of ATG8 proteins, a process central to membrane atg8ylation and canonical autophagy. Loss of Atg5 in myeloid cells causes early mortality in murine models of tuberculosis. This in vivo phenotype is specific to ATG5. Here, we show using human cell lines that absence of ATG5, but not of other ATGs directing ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ATG5 GNB2L1 | 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 | - | |
| ATG5 GNB2L1 | 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 | - | |
| GNB2L1 ATG5 | 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 | - | |
| ATG5 GNB2L1 | 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