+ |
CSNK2A1 | down-regulates
phosphorylation
|
HSP90AB1 |
0.339 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179260 |
Ser226 |
KEREKEIsDDEAEEE |
Homo sapiens |
|
pmid |
sentence |
18591256 |
Although the kinase responsible for hsp90? Phosphorylation in vivo is not known, it has been reported that ck2 can phosphorylate these sites in vitro (24). Thus, we prephosphorylated recombinant hsp90? With ck2 before addition to the reaction. Remarkably, hsp90? Phosphorylation greatly reduced its ability to inhibit apaf-1 oligomerization and caspase-9 recruitment (fig. 5b). These results indicate that the phosphorylation status of hsp90? Significantly impacts its ability to inhibit apoptosome formation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179264 |
Ser255 |
PKIEDVGsDEEDDSG |
Homo sapiens |
|
pmid |
sentence |
18591256 |
Although the kinase responsible for hsp90? Phosphorylation in vivo is not known, it has been reported that ck2 can phosphorylate these sites in vitro (24). Thus, we prephosphorylated recombinant hsp90? With ck2 before addition to the reaction. Remarkably, hsp90? Phosphorylation greatly reduced its ability to inhibit apaf-1 oligomerization and caspase-9 recruitment (fig. 5b). These results indicate that the phosphorylation status of hsp90? Significantly impacts its ability to inhibit apoptosome formation. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
SRC | up-regulates
phosphorylation
|
HSP90AB1 |
0.57 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157781 |
Tyr301 |
DDITQEEyGEFYKSL |
Homo sapiens |
|
pmid |
sentence |
17855507 |
C-src directly phosphorylates hsp90 on tyrosine 300 residue and that this event is essential for vegf-stimulated enos association to hsp90 and thus no release from endothelial cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FNIP1 | down-regulates activity
binding
|
HSP90AB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261415 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27353360 |
FNIP1 and FNIP2 facilitate FLCN binding to Hsp90 chaperone. Our results suggest that FNIP1 is a potent inhibitor of Hsp90 ATPase activity, as 200 nM of FNIP1 inhibits Hsp90 ATPase activity by 50-fold. FNIP2 also has shown inhibitory activity towards Hsp90; however, it required 1.6 μM of FNIP2 to inhibit the ATPase activity by eightfold. Although we use the term ‘inhibition' here, FNIPs seem only to be slowing the chaperone cycle. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSP90AB1 | up-regulates quantity by stabilization
binding
|
FLCN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261417 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27353360 |
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and it is regulated by co-chaperones. Here we show that the tumour suppressor FLCN is an Hsp90 client protein and its binding partners FNIP1/FNIP2 function as co-chaperones. FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261418 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27353360 |
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and it is regulated by co-chaperones. Here we show that the tumour suppressor FLCN is an Hsp90 client protein and its binding partners FNIP1/FNIP2 function as co-chaperones. FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
HSP90AB1 | up-regulates quantity
binding
|
CBLL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271475 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
31952268 |
By immunoprecipitation, we present evidence that Hakai interacts with Hsp90 chaperone complex in several epithelial cells and demonstrate that is a novel Hsp90 client protein. Interestingly, by overexpressing and knocking-down experiments with Hakai, we identified Annexin A2 as a Hakai-regulated protein. Interestingly, geldanamycin-induced Hakai degradation is accompanied by an increased expression of E-cadherin and Annexin A2. Hsp90 participates in the correct folding of its client proteins, allowing them to maintain their stability and activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FNIP2 | down-regulates activity
binding
|
HSP90AB1 |
0.266 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261416 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27353360 |
FNIP1 and FNIP2 facilitate FLCN binding to Hsp90 chaperone. Our results suggest that FNIP1 is a potent inhibitor of Hsp90 ATPase activity, as 200 nM of FNIP1 inhibits Hsp90 ATPase activity by 50-fold. FNIP2 also has shown inhibitory activity towards Hsp90; however, it required 1.6 μM of FNIP2 to inhibit the ATPase activity by eightfold. Although we use the term ‘inhibition' here, FNIPs seem only to be slowing the chaperone cycle. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NVP-BEP800 | down-regulates
chemical inhibition
|
HSP90AB1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-194904 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSP90AB1 | down-regulates
binding
|
APAF1 |
0.397 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-81043 |
|
|
Homo sapiens |
|
pmid |
sentence |
10944114 |
The present studies demonstrate that heat shock protein 90 (hsp90) forms a cytosolic complex with apaf-1 and thereby inhibits the formation of the active complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AHSA1 | up-regulates activity
binding
|
HSP90AB1 |
0.681 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252212 |
|
|
Homo sapiens |
|
pmid |
sentence |
16696853 |
The N-terminal region of Aha1 interacts with the central domain of Hsp90 and stimulates Hsp90 ATPase activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSP90AB1 | up-regulates quantity by stabilization
binding
|
NOD2 |
0.327 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252415 |
|
|
Homo sapiens |
|
pmid |
sentence |
23019338 |
Nod2 is constitutively associated with a chaperone protein, Hsp90, which is required for Nod2 stability and protects Nod2 from degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSP90AB1 | up-regulates activity
binding
|
AR |
0.692 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251535 |
|
|
Homo sapiens |
|
pmid |
sentence |
15861399 |
The unliganded AR resides predominately in the cytoplasm as a heteromeric complex with hsp90 and other chaperone proteins. These chaperone proteins maintain AR in a form that is receptive to ligand binding. Regulation of gene expression by androgen-activated AR occurs through receptor nuclear translocation, dimerization, and binding to androgen response elements (AREs) in the DNA of target genes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSP90AB1 | up-regulates activity
binding
|
NOS3 |
0.527 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252214 |
|
|
Homo sapiens |
|
pmid |
sentence |
9580552 |
Here we show that Hsp90 associates with endothelial nitric oxide synthase (eNOS) and is rapidly recruited to the eNOS complex by agonists that stimulate production of nitric oxide, namely vascular endothelial growth factor, histamine and fluid shear stress. Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STIP1 | down-regulates activity
binding
|
HSP90AB1 |
0.848 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261412 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27353360 |
Hsp90 chaperone cycle is tightly regulated by another group of proteins referred to as ‘co-chaperones'. Their stability does not depend on Hsp90 function but they interact with distinct Hsp90 conformational states, providing directionality to the Hsp90 cycle4. Furthermore, certain co-chaperones, such as HOP and Cdc37p50 inhibit the Hsp90 chaperone cycle, assisting in delivery of distinct sets of client proteins (steroid hormone receptors and kinases, respectively) to the Hsp90 chaperone machine. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
luminespib | down-regulates
chemical inhibition
|
HSP90AB1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-190041 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |