BAIT
HSP90AA1
EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP-2, LAP2
heat shock protein 90kDa alpha (cytosolic), class A member 1
GO Process (16)
GO Function (10)
GO Component (10)
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- G2/M transition of mitotic cell cycle [TAS]
- axon guidance [TAS]
- chaperone-mediated protein complex assembly [IDA]
- innate immune response [TAS]
- mitochondrial transport [TAS]
- mitotic cell cycle [TAS]
- nitric oxide metabolic process [TAS]
- positive regulation of nitric oxide biosynthetic process [ISS]
- protein import into mitochondrial outer membrane [IDA]
- protein refolding [TAS]
- regulation of nitric-oxide synthase activity [TAS]
- response to unfolded protein [NAS]
- signal transduction [NAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
LIMK1
LIMK, LIMK-1
LIM domain kinase 1
GO Process (11)
GO Function (4)
GO Component (4)
Gene Ontology Biological Process
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- Rho protein signal transduction [TAS]
- actin cytoskeleton organization [TAS]
- axon guidance [TAS]
- innate immune response [TAS]
- negative regulation of ubiquitin-protein transferase activity [IDA]
- nervous system development [TAS]
- positive regulation of actin filament bundle assembly [IDA]
- positive regulation of axon extension [ISS]
- protein phosphorylation [IDA, IMP]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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 analysis of HSP90-client interactions reveals principles of substrate recognition.
HSP90 is a molecular chaperone that associates with numerous substrate proteins called clients. It plays many important roles in human biology and medicine, but determinants of client recognition by HSP90 have remained frustratingly elusive. We systematically and quantitatively surveyed most human kinases, transcription factors, and E3 ligases for interaction with HSP90 and its cochaperone CDC37. Unexpectedly, many more kinases than ... [more]
Cell Aug. 31, 2012; 150(5);987-1001 [Pubmed: 22939624]
Throughput
- High Throughput
Curated By
- BioGRID