INSIG1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
VCP
Gene Ontology Biological Process
- DNA repair [NAS]
- ER-associated ubiquitin-dependent protein catabolic process [IDA, IMP, TAS]
- activation of cysteine-type endopeptidase activity involved in apoptotic process [ISS]
- cellular response to DNA damage stimulus [IDA]
- double-strand break repair [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- establishment of protein localization [TAS]
- positive regulation of Lys63-specific deubiquitinase activity [IDA]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of protein K63-linked deubiquitination [IDA]
- positive regulation of protein catabolic process [IDA]
- positive regulation of protein complex assembly [IDA]
- proteasome-mediated ubiquitin-dependent protein catabolic process [NAS]
- protein N-linked glycosylation via asparagine [IMP]
- protein ubiquitination [IDA, NAS]
- regulation of apoptotic process [TAS]
- retrograde protein transport, ER to cytosol [IDA]
- translesion synthesis [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Hrd1p ubiquitin ligase complex [IDA]
- cytoplasm [IDA]
- cytosol [IDA]
- endoplasmic reticulum [IDA]
- endoplasmic reticulum membrane [IDA]
- extracellular vesicular exosome [IDA]
- intracellular membrane-bounded organelle [ISS]
- lipid particle [IDA]
- nucleoplasm [IDA]
- nucleus [IDA, TAS]
- perinuclear region of cytoplasm [IDA]
- proteasome complex [IDA]
- site of double-strand break [IDA]
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Regulated endoplasmic reticulum-associated degradation of a polytopic protein: p97 recruits proteasomes to Insig-1 before extraction from membranes.
Polytopic membrane proteins subjected to endoplasmic reticulum (ER)-associated degradation are extracted from membranes and targeted to proteasomes for destruction. The extraction mechanism is poorly understood. One polytopic ER protein subjected to ER-associated degradation is Insig-1, a negative regulator of cholesterol synthesis. Insig-1 is rapidly degraded by proteasomes when cells are depleted of cholesterol, and its degradation is inhibited when sterols ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
INSIG1 VCP | 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 | - | |
INSIG1 VCP | 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 | - | |
INSIG1 VCP | 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 | 463600 |
Curated By
- BioGRID