VIMP
Gene Ontology Biological Process
- ER overload response [IDA, IMP]
- ER-associated ubiquitin-dependent protein catabolic process [IDA]
- cell redox homeostasis [IDA]
- cellular response to insulin stimulus [TAS]
- cellular response to lipopolysaccharide [IMP]
- cellular response to oxidative stress [IMP]
- endoplasmic reticulum unfolded protein response [IDA]
- establishment of protein localization [TAS]
- negative regulation of acute inflammatory response to antigenic stimulus [IMP]
- negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [IMP]
- negative regulation of glucose import [TAS]
- negative regulation of glycogen biosynthetic process [TAS]
- negative regulation of inflammatory response [IC]
- negative regulation of interleukin-6 production [ISS]
- negative regulation of macrophage apoptotic process [IMP]
- negative regulation of nitric-oxide synthase biosynthetic process [IMP]
- negative regulation of tumor necrosis factor production [ISS]
- regulation of gluconeogenesis [TAS]
- regulation of nitric oxide metabolic process [IMP]
- response to glucose [IEP]
- response to redox state [IDA]
- retrograde protein transport, ER to cytosol [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HSPA4
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol.
Elimination of misfolded proteins from the endoplasmic reticulum (ER) by retro-translocation is an important physiological adaptation to ER stress. This process requires recognition of a substrate in the ER lumen and its subsequent movement through the membrane by the cytosolic p97 ATPase. Here we identify a p97-interacting membrane protein complex in the mammalian ER that links these two events. The ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID