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
GSN
ADF, AGEL, RP11-477J21.1
gelsolin
GO Process (6)
GO Function (2)
GO Component (5)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Extracellular Hsp90? and clusterin synergistically promote breast cancer epithelial-to-mesenchymal transition and metastasis via LRP1.
Extracellular heat shock protein 90 alpha (eHsp90?, also known as HSP90AA1) has been widely reported to promote tumor cell motility and tumor metastasis in various types of cancer. Several extracellular proteins and membrane receptors have been identified as interacting proteins of eHsp90? and mediate its pro-metastasis function. However, the regulatory mechanism of eHsp90? activity remains largely unknown. Here, we report ... [more]
J Cell Sci Dec. 31, 2018; 132(15); [Pubmed: 31273033]
Throughput
- High Throughput
Curated By
- BioGRID