Search results for HSP90B1

Showing 8 results out of 8

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Species

Types

Compartments

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Protein (4 results from a total of 4)

Identifier: R-HSA-981545
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: HSP90B1: P14625
Identifier: R-HSA-3221653
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: HSP90B1: P14625
Identifier: R-HSA-3221623
Species: Homo sapiens
Compartment: endocytic vesicle lumen
Primary external reference: UniProt: HSP90B1: P14625
Identifier: R-HSA-8957016
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: HSP90B1: P14625

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-5642304
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSEMBL:ENSG00000166598

Reaction (3 results from a total of 3)

Identifier: R-HSA-6790038
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen, nucleoplasm
Signal transducer and activator of transcription 3 (STAT3) is a key regulator of gene expression in response to signaling of many cytokines including interleukin-6 (IL6), Oncostatin M, and leukemia inhibitory factor. Using microarray techniques, hundreds of genes have been reported as potential STAT3 target genes (Dauer et al. 2005, Hsieh et al. 2005). Some of these genes have been proven to be direct STAT3 targets using genome-wide chromatin immunoprecipitation screening (Snyder et al. 2008, Carpenter & Lo 2014), including the gene which encodes the endoplasmic reticulum lumen protein Endoplasmin (HSP90B1) (Madamanchi et al. 2001).
Identifier: R-HSA-1791163
Species: Homo sapiens
Compartment: nucleoplasm, endoplasmic reticulum lumen
The Endoplasmin (HSP90B1) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Identifier: R-HSA-1678923
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen, endoplasmic reticulum membrane
GP96 (also known as GRP94, HSP90b1), a paralogue of HSP90 in the endoplasmic reticulum, acts as a chaperone for some integrines and Toll-like receptors. Macrophages or B-cells from gp96 knockout mice have abrogated function of TLR2, 4, 5, 7 and 9, but not TLR3 (Yang Y et al 2007, Liu B and Li Z 2008, Staron M et al 2010). GP96 interacts with TLRs and integrines via its C-terminal hydrophobic domain, formed by residues 652-678 (Wu S et al 2012). GP96 functions as a V-shaped dimer in ATP-dependent manner, however it remains unclear how ATP hydrolysis-dependent conformational changes of GP96 are regulated (Li Z and Srivastava PK 1993).

GP96 forms a complex with co-chaperone CNPY3, also known as PRAT4A. GP96-CNPY3 promotes the proper post-translational ectodomain folding of TLRs, but not TLR3 (Liu B et al 2010).

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