| + |
CSNK2A1 |
phosphorylation
|
HSP90AA1 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250899 |
Ser231 |
KERDKEVsDDEAEEK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 2492519 |
Both hsp 90 proteins are phosphorylated at two homologous sites. For the alpha protein, these sites correspond to serine 231 and serine 263. | Dephosphorylated hsp 90 is phosphorylated at both sites by casein kinase II from HeLa cells, calf thymus, or rabbit reticulocytes; no other hsp 90 residues were phosphorylated by casein kinase II in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250900 |
Ser263 |
PEIEDVGsDEEEEKK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 2492519 |
Both hsp 90 proteins are phosphorylated at two homologous sites. For the alpha protein, these sites correspond to serine 231 and serine 263. | Dephosphorylated hsp 90 is phosphorylated at both sites by casein kinase II from HeLa cells, calf thymus, or rabbit reticulocytes; no other hsp 90 residues were phosphorylated by casein kinase II in vitro. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates 
phosphorylation
|
HSP90AA1 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202812 |
Thr115 |
GTIAKSGtKAFMEAL |
Homo sapiens |
|
| pmid |
sentence |
| 24117238 |
Threonine residue set, thr(115)/thr(425)/thr(603), of hsp90_ is specifically phosphorylated by pkc_phosphorylation of hsp90_ by pkc_ decreases the binding affinity of hsp90_ towards atp and co-chaperones such as cdc37 (cell-division cycle 37), thereby decreasing its chaperone activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202816 |
Thr425 |
KKCLELFtELAEDKE |
Homo sapiens |
|
| pmid |
sentence |
| 24117238 |
Threonine residue set, thr(115)/thr(425)/thr(603), of hsp90_ is specifically phosphorylated by pkc_, and, more interestingly, this threonine residue set serves as a 'phosphorylation switch' for hsp90_ binding or release of pkc_. Moreover, phosphorylation of hsp90_ by pkc_ decreases the binding affinity of hsp90_ towards atp and co-chaperones such as cdc37 (cell-division cycle 37), thereby decreasing its chaperone activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202820 |
Thr603 |
PCCIVTStYGWTANM |
Homo sapiens |
|
| pmid |
sentence |
| 24117238 |
Threonine residue set, thr(115)/thr(425)/thr(603), of hsp90_ is specifically phosphorylated by pkc_, and, more interestingly, this threonine residue set serves as a 'phosphorylation switch' for hsp90_ binding or release of pkc_. Moreover, phosphorylation of hsp90_ by pkc_ decreases the binding affinity of hsp90_ towards atp and co-chaperones such as cdc37 (cell-division cycle 37), thereby decreasing its chaperone activity. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKDC |
phosphorylation
|
HSP90AA1 |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248887 |
Thr5 |
tQTQDQPM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 2507541 |
Here we show that the dsDNA-activated protein kinase from human HeLa cells phosphorylates 2 threonine residues in the sequence PEETQTQDQPME at the amino terminus of human hsp90 alpha. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248888 |
Thr7 |
tQDQPMEE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 2507541 |
Here we show that the dsDNA-activated protein kinase from human HeLa cells phosphorylates 2 threonine residues in the sequence PEETQTQDQPME at the amino terminus of human hsp90 alpha. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKACA |
phosphorylation
|
HSP90AA1 |
0.454 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176614 |
Thr90 |
NKQDRTLtIVDTGIG |
Homo sapiens |
|
| pmid |
sentence |
| 21919888 |
Thr90 phosphorylation of hsp90_ by protein kinase a regulates its chaperone machinery |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSP90AA1 | up-regulates quantity by stabilization 
binding
|
PAFAH1B1 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252168 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20133715 |
The type I lissencephaly gene product LIS1, a key regulator of cytoplasmic dynein, is critical for cell proliferation, survival, and neuronal migration. However, little is known about the regulation of LIS1. Here, we identify a previously uncharacterized mammalian homolog of Aspergillus NudC, NudCL2 (NudC-like protein 2), as a regulator of LIS1. NudCL2 is localized to the centrosome in interphase, and spindle poles and kinetochores during mitosis, a pattern similar to the localization of LIS1 and cytoplasmic dynein. Depletion of NudCL2 destabilized LIS1 and led to phenotypes resembling those of either dynein or LIS1 deficiency. NudCL2 complexed with and enhanced the interaction between LIS1 and Hsp90. Either disruption of the LIS1-Hsp90 interaction with the C terminus of NudCL2 or inhibition of Hsp90 chaperone function by geldanamycin decreased LIS1 stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSP90AA1 | up-regulates quantity
binding
|
CBLL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271474 |
|
|
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 |
| + |
HSP90AA1 | up-regulates quantity by stabilization
binding
|
LGMN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272855 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 24610907 |
We demonstrate that TRAF6 ubiquitinates the proform of AEP through K63-linked polyubiquitin, reversible by USP17, and forms a complex with HSP90α to subsequently promote pro-AEP intracellular stability as well as secretion. We now present evidence that AEP is a substrate for TRAF6 ubiquitination, resulting in AEP/TRAF6/HSP90α complex formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FNIP2 | down-regulates activity
binding
|
HSP90AA1 |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261414 |
|
|
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 |
| + |
HECTD1 | down-regulates quantity
ubiquitination
|
HSP90AA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261199 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22431752 |
We demonstrate that Hectd1 is a functional ubiquitin ligase and that one of its substrates is Hsp90, a chaperone protein with both intra- and extracellular clients. Identification of Hsp90 in both proteomic screens suggested that members of the Hsp90 superfamily may be substrates of Hectd1. Myc-Hectd1ANK and HA-Hsp90bd (the fragment identified in the yeast two-hybrid screen) bind in an in vitro binding assay (Fig. 3 D) and when coexpressed in HEK293T cells. Hectd1 is required for K63-linked Ubn of Hsp90. Together, these results demonstrate that Hectd1-dependent Ubn of Hsp90 targets it away from the membrane and the secretory pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSP90AA1 | up-regulates
binding
|
NOS3 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-57211 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9580552 |
The binding of hsp90 to enos enhances the activation of enos. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTGES3 | up-regulates activity
binding
|
HSP90AA1 |
0.913 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262831 |
|
|
in vitro |
|
| pmid |
sentence |
| 9817749 |
The mutant Hsp90 proteins tested are defective in the binding and ATP hydrolysis-dependent cycling of the co-chaperone p23, which is thought to regulate the binding and release of substrate polypeptide from Hsp90. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STIP1 | down-regulates activity
binding
|
HSP90AA1 |
0.932 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261411 |
|
|
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 cycle. 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 |
| + |
AHSA1 | up-regulates activity
binding
|
HSP90AA1 |
0.772 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252211 |
|
|
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 |
| + |
HSP90AA1 | up-regulates quantity by stabilization
binding
|
NOD2 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252414 |
|
|
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 |
| + |
luminespib | down-regulates
chemical inhibition
|
HSP90AA1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190038 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSP90AA1 | up-regulates
binding
|
PPP5C |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131564 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15577939 |
Hsp90 causes substantial activation of ppp5 by competing for tpr_phosphatase domain contacts and allowing access to the catalytic site. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSP90AA1 | up-regulates
binding
|
TGFBR1 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179268 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18591668 |
The data in fig. 5 suggest that hsp90 specifically interacts with t?RI And t?RII In vitro and in vivo. Coupled with our data showing that loss of hsp90 function decreases t?R Levels and blocks tgf?-Induced smad2/3 activation and transcription, this result suggests that hsp90 controls tgf? Signaling as an essential component for stabilizing t?Rs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FNIP1 | down-regulates activity
binding
|
HSP90AA1 |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261413 |
|
|
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 |
| + |
HSP90AA1 | up-regulates quantity by stabilization
binding
|
FLCN |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256505 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27353360 |
Here we show that the stability of the tumour suppressor folliculin (FLCN) depends on the chaperone function of Hsp90. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSP90AA1 | down-regulates
binding
|
NR3C1 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251667 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21511880 |
We report the crucial underlying role of the intranuclear heat shock protein 90 molecular chaperone complex in pulsatile GR regulation. Pharmacological interference of heat shock protein 90 (HSP90) with geldanamycin during the intranuclear chaperone cycle completely ablated GR's cyclical activity, cyclical cAMP response element-binding protein (CREB) binding protein (CBP)/p300 recruitment, and the associated cyclical acetylation at the promoter region. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glucocorticoid receptor Signaling |
| + |
HSP90AA1 | up-regulates
binding
|
TGFBR2 |
0.391 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179271 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18591668 |
The data in fig. 5 suggest that hsp90 specifically interacts with t?RI And t?RII In vitro and in vivo. Coupled with our data showing that loss of hsp90 function decreases t?R Levels and blocks tgf?-Induced smad2/3 activation and transcription, this result suggests that hsp90 controls tgf? Signaling as an essential component for stabilizing t?Rs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TOMM70 | up-regulates activity
binding
|
HSP90AA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261379 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12526792 |
The Tom70 receptor is a membrane-localized cochaperone that integrates the Hsp70/Hsp90 chaperones with mitochondrial preprotein targeting and translocation. In mammals, preprotein in the cytosol is associated with both Hsp90 and Hsp70 in a multichaperone complex, and docking of Hsp90 and/or Hsp70 onto Tom70 is essential for preprotein targeting. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
HSP90AA1 | up-regulates activity
binding
|
AR |
0.754 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251536 |
|
|
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 |
3.0
HSP90AA1
- 
- 