+ |
NEK6 | up-regulates activity
phosphorylation
|
HSPA1A |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273885 |
Thr66 |
VALNPQNtVFDAKRL |
in vitro |
|
pmid |
sentence |
30108182 |
Mitotic phosphorylation of Hsp72 by the kinase NEK6 at Thr66 located in the NBD promotes the localization of Hsp72 to the mitotic spindle and is required for efficient spindle assembly and chromosome congression and segregation. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
HSPA1A | down-regulates
binding
|
NR3C1 |
0.618 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251668 |
|
|
Homo sapiens |
|
pmid |
sentence |
21730050 |
Interestingly, FKBP51 forms complexes in mitochondria with the glucocorticoid receptor and the Hsp90/Hsp70-based chaperone heterocomplex |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSPA1A | up-regulates quantity by stabilization
binding
|
PACRG |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272890 |
|
|
in vitro |
|
pmid |
sentence |
12150907 |
Our in vitro data suggest that CHIP competes with Hsp70 in binding to Parkin, probably via suppression of the ATPase activity of Hsc/Hsp70 (Figure 4E).In fact, it acts as an inhibitory factor that suppresses the ubiquitination of Pael-R mediated by Parkin in vitro, and Hsp70 enhances the efficiency of folding of overexpressed Pael-R in vivo. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
HSPA1A | down-regulates
|
MAPK8 |
0.495 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-140553 |
|
|
Homo sapiens |
|
pmid |
sentence |
16172114 |
Hsp70 inhibited stress-induced jnk activation and jnk with sp600125 or by expression of a dominant negative mutant of jnk-blocked bax translocation as effectively as hsp70 overexpression |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FOXA1 | up-regulates quantity by expression
transcriptional regulation
|
HSPA1A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254164 |
|
|
Homo sapiens |
|
pmid |
sentence |
19486887 |
The results showed overexpression of Foxa1 promoted the expression of HSP72, while Foxa1 depletion, induced by antisense oligonucleotides, decreased the expression of HSP72 in MCF-7 cells under normal and heat stress condition. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STAT3 | up-regulates quantity by expression
transcriptional regulation
|
HSPA1A |
0.323 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255240 |
|
|
Homo sapiens |
|
pmid |
sentence |
19754877 |
Hsp105beta upregulates hsp70 gene expression through signal transducer and activator of transcription-3. Hsp105beta induces Hsp70 expression markedly through the STAT3 pathway in heat-shocked cells. This may represent the mechanism that connects the heat shock protein and STAT families for cell defense against deleterious stress. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSPH1 | up-regulates quantity by expression
transcriptional regulation
|
HSPA1A |
0.479 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255242 |
|
|
Homo sapiens |
|
pmid |
sentence |
19754877 |
Hsp105beta upregulates hsp70 gene expression through signal transducer and activator of transcription-3. Hsp105beta induces Hsp70 expression markedly through the STAT3 pathway in heat-shocked cells. This may represent the mechanism that connects the heat shock protein and STAT families for cell defense against deleterious stress. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSPA1A | up-regulates quantity by stabilization
binding
|
FLCN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256506 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27353360 |
These data suggest that inhibition of Hsp70 does not lead to an increase in misfolded FLCN but instead to its degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSPA1A | down-regulates
binding
|
APAF1 |
0.443 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80451 |
|
|
Homo sapiens |
|
pmid |
sentence |
10934467 |
Here we show that the documented anti-apoptotic effect of the principal heat-shock protein, hsp70, is mediated through its direct association with the caspase-recruitment domain (card) of apaf-1 and through apoptosome formation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSPA1A | up-regulates quantity
post transcriptional regulation
|
ENPP1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252197 |
|
|
Homo sapiens |
|
pmid |
sentence |
19083193 |
We demonstrated the binding of heat shock protein 70 (HSP70) to ENPP1-3'UTR. Through this binding, HSP70 stabilizes ENPP1 mRNA and increases ENPP1 transcript and protein levels. This positive modulation of ENPP1 expression is paralleled by a reduced insulin-induced IR and IRS-1 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TOMM70 | up-regulates activity
binding
|
HSPA1A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261380 |
|
|
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 |
+ |
HSPA1A | up-regulates quantity by stabilization
binding
|
NOD2 |
0.259 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252416 |
|
|
Homo sapiens |
|
pmid |
sentence |
24790089 |
The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSPA1A | down-regulates quantity by destabilization
binding
|
ACOT4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271819 |
|
|
|
|
pmid |
sentence |
33148467 |
HSPA1A binds unphosphorylated ACOT4 and promotes its degradation |
|
Publications: |
1 |
+ |
BAG5 | down-regulates activity
binding
|
HSPA1A |
0.742 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261196 |
|
|
Homo sapiens |
Brain |
pmid |
sentence |
15603737 |
Here, we show that BAG5, a BAG domain-containing family member, interacts with both Hsp70 and parkin with deleterious functional consequences. Through these interactions, BAG5 inhibits Hsp70 chaperone activity and parkin E3 ubiquitin ligase activity; Thus, BAG5 interacts with Hsp70 in vitro and in vivo, and substitution of select residues within the BAG domains is sufficient to abolish this interaction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSPA1A | up-regulates activity
relocalization
|
GSTA4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264799 |
|
|
|
|
pmid |
sentence |
21929724 |
Model showing Ser189/Thr193 protein kinase dependent phosphorylation of GST A4‐4 has increased affinity for chaperone Hsp70 which activates mitochondrial competent import signals for GSTA4‐4. |Protein kinase A mediated phosphorylation of serine residues of CYPs increases the affinity of proteins for binding to cytoplasmic chaperones such as heat shock proteins (Hsp), Hsp70/Hsp90, resulting in increased mitochondrial translocation |
|
Publications: |
1 |