BAIT
AHSA1
AHA1, C14orf3, p38, HSPC322
AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast)
GO Process (1)
GO Function (3)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
HSPA5
BIP, GRP78, HEL-S-89n, MIF2
heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
GO Process (14)
GO Function (10)
GO Component (12)
Gene Ontology Biological Process
- ATP catabolic process [ISS]
- ER-associated ubiquitin-dependent protein catabolic process [TAS]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- blood coagulation [TAS]
- cellular protein metabolic process [TAS]
- cellular response to glucose starvation [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- maintenance of protein localization in endoplasmic reticulum [IMP]
- negative regulation of apoptotic process [IMP, TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of cell migration [IMP]
- regulation of protein folding in endoplasmic reticulum [TAS]
- substantia nigra development [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- COP9 signalosome [IDA]
- endoplasmic reticulum [IDA, IMP, TAS]
- endoplasmic reticulum chaperone complex [IDA]
- endoplasmic reticulum lumen [TAS]
- endoplasmic reticulum membrane [TAS]
- endoplasmic reticulum-Golgi intermediate compartment [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- integral component of endoplasmic reticulum membrane [IDA]
- membrane [IDA]
- midbody [IDA]
- nucleus [IDA, IMP]
Homo sapiens
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.
Publication
The dynamic interactome of human Aha1 upon Y223 phosphorylation.
Heat Shock Protein 90 (Hsp90) is an essential chaperone that supports the function of a wide range of signaling molecules. Hsp90 binds to a suite of co-chaperone proteins that regulate Hsp90 function through alteration of intrinsic ATPase activity. Several studies have determined Aha1 to be an important co-chaperone whose binding to Hsp90 is modulated by phosphorylation, acetylation and SUMOylation of ... [more]
Data Brief Dec. 01, 2015; 5(0);752-5 [Pubmed: 26693507]
Throughput
- High Throughput
Curated By
- BioGRID