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
TNFAIP3
A20, OTUD7C, TNFA1P2, RP11-356I2.3
tumor necrosis factor, alpha-induced protein 3
GO Process (37)
GO Function (7)
GO Component (5)
Gene Ontology Biological Process
- B-1 B cell homeostasis [ISS]
- cellular response to hydrogen peroxide [ISS]
- cellular response to lipopolysaccharide [IDA]
- innate immune response [TAS]
- negative regulation of B cell activation [ISS]
- negative regulation of CD40 signaling pathway [IMP]
- negative regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- negative regulation of NF-kappaB transcription factor activity [IDA]
- negative regulation of bone resorption [NAS]
- negative regulation of endothelial cell apoptotic process [IDA]
- negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [IDA]
- negative regulation of inflammatory response [ISS]
- negative regulation of innate immune response [ISS]
- negative regulation of interleukin-2 production [IMP]
- negative regulation of interleukin-6 production [ISS]
- negative regulation of osteoclast proliferation [NAS]
- negative regulation of protein ubiquitination [IDA]
- negative regulation of smooth muscle cell proliferation [IDA]
- negative regulation of toll-like receptor 2 signaling pathway [NAS]
- negative regulation of toll-like receptor 3 signaling pathway [IDA]
- negative regulation of toll-like receptor 4 signaling pathway [NAS]
- negative regulation of tumor necrosis factor production [ISS]
- negative regulation of type I interferon production [TAS]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- nucleotide-binding oligomerization domain containing signaling pathway [TAS]
- positive regulation of protein catabolic process [IDA]
- protein K11-linked deubiquitination [IDA]
- protein K48-linked deubiquitination [IDA]
- protein K48-linked ubiquitination [IDA]
- protein K63-linked deubiquitination [IDA]
- protein deubiquitination [TAS]
- protein oligomerization [NAS]
- regulation of defense response to virus by host [NAS]
- regulation of germinal center formation [ISS]
- regulation of vascular wound healing [NAS]
- response to molecule of bacterial origin [IDA]
- tolerance induction to lipopolysaccharide [IMP]
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
- Low Throughput
Curated By
- BioGRID