+ |
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 |
+ |
CBLL1 | down-regulates quantity by destabilization
ubiquitination
|
ANXA2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271473 |
|
|
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. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
CBLL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271179 |
|
|
Homo sapiens |
|
pmid |
sentence |
34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
Publications: |
1 |
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 |