SQSTM1
Gene Ontology Biological Process
- apoptotic signaling pathway [TAS]
- autophagy [IMP, TAS]
- endosomal transport [TAS]
- intracellular signal transduction [TAS]
- macroautophagy [ISS]
- negative regulation of apoptotic process [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- positive regulation of apoptotic process [TAS]
- positive regulation of macroautophagy [IMP]
- positive regulation of transcription from RNA polymerase II promoter [TAS]
- protein localization [TAS]
- protein phosphorylation [NAS]
- regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- regulation of Ras protein signal transduction [NAS]
- response to stress [TAS]
- ubiquitin-dependent protein catabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HSPA5
Gene Ontology Biological Process
- ATP catabolic process [ISS]
- ER-associated ubiquitin-dependent protein catabolic process [TAS]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- blood coagulation [TAS]
- cellular protein metabolic process [TAS]
- cellular response to glucose starvation [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- maintenance of protein localization in endoplasmic reticulum [IMP]
- negative regulation of apoptotic process [IMP, TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of cell migration [IMP]
- regulation of protein folding in endoplasmic reticulum [TAS]
- substantia nigra development [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- COP9 signalosome [IDA]
- endoplasmic reticulum [IDA, IMP, TAS]
- endoplasmic reticulum chaperone complex [IDA]
- endoplasmic reticulum lumen [TAS]
- endoplasmic reticulum membrane [TAS]
- endoplasmic reticulum-Golgi intermediate compartment [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- integral component of endoplasmic reticulum membrane [IDA]
- membrane [IDA]
- midbody [IDA]
- nucleus [IDA, IMP]
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.
Publication
Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding.
We show that ATE1-encoded Arg-transfer RNA transferase (R-transferase) of the N-end rule pathway mediates N-terminal arginylation of multiple endoplasmic reticulum (ER)-residing chaperones, leading to their cytosolic relocalization and turnover. N-terminal arginylation of BiP (also known as GRP78), protein disulphide isomerase and calreticulin is co-induced with autophagy during innate immune responses to cytosolic foreign DNA or proteasomal inhibition, associated with increased ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HSPA5 SQSTM1 | 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 | - | |
| SQSTM1 HSPA5 | 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 | - | |
| HSPA5 SQSTM1 | 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 | - | |
| SQSTM1 HSPA5 | 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 | - | |
| HSPA5 SQSTM1 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| HSPA5 SQSTM1 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | 2756558 | |
| HSPA5 SQSTM1 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| SQSTM1 HSPA5 | 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 | 2595629 |
Curated By
- BioGRID