PREY
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
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
Interaction of amyotrophic lateral sclerosis/frontotemporal lobar degeneration-associated fused-in-sarcoma with proteins involved in metabolic and protein degradation pathways.
Fused-in-sarcoma (FUS) is a nuclear protein linked to amyotrophic lateral sclerosis and frontotemporal dementia. Under pathologic conditions, FUS frequently is accumulated in cytosoplasm, but how this altered distribution affects the protein interaction pattern of FUS is unclear. Using dual-tag affinity purification and mass spectrometry, we compared the interactome of the wild-type FUS and the P525Â L mutant, which causes juvenile amyotrophic ... [more]
Neurobiol. Aging Aug. 04, 2014; 0(0); [Pubmed: 25192599]
Throughput
- High Throughput
Curated By
- BioGRID