BAIT
VCP
ALS14, HEL-220, HEL-S-70, IBMPFD, IBMPFD1, TERA, p97
valosin containing protein
GO Process (18)
GO Function (8)
GO Component (13)
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]
Homo sapiens
PREY
LZIC
leucine zipper and CTNNBIP1 domain containing
GO Process (0)
GO Function (0)
GO Component (0)
Homo sapiens
Affinity Capture-Luminescence
An interaction is inferred when a bait protein, tagged with luciferase, is enzymatically detected in immunoprecipitates of the prey protein as light emission. The prey protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag.
Publication
Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.
Interaction mapping is a powerful strategy to elucidate the biological function of protein assemblies and their regulators. Here, we report the generation of a quantitative interaction network, directly linking 14 human proteins to the AAA+ ATPase p97, an essential hexameric protein with multiple cellular functions. We show that the high-affinity interacting protein ASPL efficiently promotes p97 hexamer disassembly, resulting in ... [more]
Nat Commun Dec. 20, 2015; 7();13047 [Pubmed: 27762274]
Throughput
- Low Throughput
Additional Notes
- dual luminescence-based co-immunoprecipitation (DULIP) assay
Related interactions
Curated By
- BioGRID