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]
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]
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.
Publication
The role of the N-domain in the ATPase activity of the mammalian AAA ATPase p97/VCP.
p97/valosin-containing protein (VCP) is a type II ATPase associated with various cellular activities that forms a homohexamer with each protomer containing an N-terminal domain (N-domain); two ATPase domains, D1 and D2; and a disordered C-terminal region. Little is known about the role of the N-domain or the C-terminal region in the p97 ATPase cycle. In the p97-associated human disease inclusion ... [more]
Throughput
- Low Throughput
Additional Notes
- VCP forms a homohexamer that can be visualized by negative stain electron microscopy and cryo-EM
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
VCP 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. | High | - | BioGRID | 2534242 | |
VCP 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 | - | |
VCP 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. | High | - | BioGRID | 817427 | |
VCP 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 | - | |
VCP 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 | - | |
VCP 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 | 935310 | |
VCP 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 | - | |
VCP VCP | 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 | 2521313 | |
VCP VCP | 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 | 2484963 | |
VCP VCP | 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 | - | |
VCP VCP | 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 | - | |
VCP VCP | 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 | - | |
VCP VCP | 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 | - | |
VCP VCP | 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 | - | |
VCP VCP | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 722331 | |
VCP VCP | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VCP VCP | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 3308557 | |
VCP VCP | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - |
Curated By
- BioGRID