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
CKAP4
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
Valosin-containing protein-interacting membrane protein (VIMP) links the endoplasmic reticulum with microtubules in concert with cytoskeleton-linking membrane protein (CLIMP)-63.
The distribution and morphology of the endoplasmic reticulum (ER) in mammalian cells depend on both dynamic and static interactions of ER membrane proteins with microtubules (MTs). Cytoskeleton-linking membrane protein (CLIMP)-63 is exclusively localized in sheet-like ER membranes, typical structures of the rough ER, and plays a pivotal role in the static interaction with MTs. Our previous study showed that the ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
VIMP CKAP4 | 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. | Low | - | BioGRID | - | |
CKAP4 VIMP | Proximity Label-MS 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. | High | 25 | BioGRID | 2983354 |
Curated By
- BioGRID