| + |
BRCA1 | down-regulates quantity by repression 
transcriptional regulation
|
HSPA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253761 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 18776923 |
We report here that glucose-regulated protein (GRP)-78, a critical regulator of the unfolded protein response (UPR), is a novel downstream target of BRCA1. We showed that overexpression of wild-type BRCA1 suppressed the expression of GRP78, whereas expression of mutant BRCA1 gene or targeted inhibition of endogenous BRCA1 using small-interfering RNA (siRNA) enhanced GRP78 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Unfolded_Proteins | down-regulates
|
HSPA5 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260163 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31226023 |
In the stressed ER, protein chaperone GRP78 binds to unfolded proteins and dissociates from the luminal domain of PERK, leading to oligomerization and activation of PERK by autophosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
HDAC1 | down-regulates quantity by repression
transcriptional regulation
|
HSPA5 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254227 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19417144 |
We show the involvement of HDAC1 in the negative regulation of the Grp78 promoter not only by its induction in the presence of the HDAC inhibitors trichostatin A and MS-275 but also by exogenous overexpression and small interfering RNA knockdown of specific HDACs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DNAJB9 | up-regulates activity 
binding
|
HSPA5 |
0.558 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261044 |
|
|
in vitro |
|
| pmid |
sentence |
| 12356756 |
When BAP was added to BiP (2:1 molar ratio of BAP:BiP), it increased the ATPase activity of BiP by about 2-fold, which was similar to the increase observed when the J domain of ERdj4 was added to BiP (Fig.5). When both BAP and the J domain were added to BiP, the rate of ATP hydrolysis by BiP was stimulated by about 4-fold over basal levels, indicating that both BAP and ERdj4 positively regulate the ATPase activity of BiP |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HSPA5 | up-regulates 
|
UPR |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265282 |
|
|
|
|
| pmid |
sentence |
| 28286085 |
The HSPA5 gene encodes the binding immunoglobulin protein (BiP), an Hsp70 family chaperone localized in the ER lumen.|When unfolded/misfolded proteins in the ER overwhelm the capacity of protein folding machinery, BiP can initiate the unfolded protein response (UPR), decrease unfolded/misfolded protein load, induce autophagy, and crosstalk with apoptosis machinery to assist in the cell survival decision. |
|
| Publications: |
1 |
| + |
SIL1 | up-regulates activity
binding
|
HSPA5 |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261045 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12356756 |
BAP, a Mammalian BiP-associated Protein, Is a Nucleotide Exchange Factor That Regulates the ATPase Activity of BiP. In addition,BAP was associated with BiP in mammalian cells and inter-acted with BiP functionallyin vitro. BAP stimulated the ATPase activity of BiP when added alone or together with the ER DnaJ protein, ERdj4, by promoting the release of ADP from BiP. Together, these data demonstrate that BAP serves as a nucleotide exchange factor for BiP and provide insights into the mechanisms that control protein folding in the mammalian ER. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
GTF2I | up-regulates quantity by expression
transcriptional regulation
|
HSPA5 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254221 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19097122 |
Transcription factor TFII-I causes transcriptional upregulation of GRP78 synthesis in prostate cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YY1 | up-regulates quantity by expression
transcriptional regulation
|
HSPA5 |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255620 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15899857 |
YY1, a constitutively expressed multifunctional transcription factor, activates the Grp78 promoter only under ER stress conditions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATF4 | down-regulates quantity by repression
transcriptional regulation
|
HSPA5 |
0.655 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253749 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16205636 |
Suppression of ATF4 expression by small interfering RNA (siRNA) partially inhibited the celecoxib-dependent upregulation of GRP78. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
HERPUD1 | up-regulates quantity by stabilization
relocalization
|
HSPA5 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261346 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29295953 |
A key inhibitor of the turnover and Nt-arginylation of BiP was HERP (homocysteine-responsive ER protein), a 43-kDa ER membrane-integrated protein that is an essential component of ER-associated protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
S | up-regulates quantity by expression
transcriptional regulation
|
HSPA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260351 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16940539 |
Perturbation of the function of endoplasmic reticulum (ER) causes stress leading to the activation of cell signaling pathways known as the unfolded protein response (UPR). Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) uses ER as a site for synthesis and processing of viral proteins. In this report, we demonstrate that infection with SARS-CoV induces the UPR in cultured cells. A comparison with M, E, and NSP6 proteins indicates that SARS-CoV spike (S) protein sufficiently induces transcriptional activation of several UPR effectors, including glucose-regulated protein 78 (GRP78), GRP94, and C/EBP homologous protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
ATF6B | up-regulates quantity by expression
transcriptional regulation
|
HSPA5 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261566 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 14973138 |
Accordingly, N-terminal fragments of each ATF6 isoform (N-ATF6α and N-ATF6β) were overexpressed in HeLa cells and the effects on GRP78 induction were assessed. When expressed at similar levels, N-ATF6α conferred ∼200-fold greater GRP78 promoter activation than N-ATF6β. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATF6 | up-regulates quantity by expression
transcriptional regulation
|
HSPA5 |
0.816 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261565 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 14973138 |
Accordingly, N-terminal fragments of each ATF6 isoform (N-ATF6α and N-ATF6β) were overexpressed in HeLa cells and the effects on GRP78 induction were assessed. When expressed at similar levels, N-ATF6α conferred ∼200-fold greater GRP78 promoter activation than N-ATF6β. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
HSPA5 | down-regulates activity 
binding
|
ERN1 |
0.815 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260176 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31226023 |
Besides being activated like PERK via dissociation of GRP78, IRE1 is also activated by direct binding of the unfolded protein to its N-terminal luminal domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
ATE1 | down-regulates quantity by destabilization
post transcriptional regulation
|
HSPA5 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261345 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 29295953 |
We showed that the molecular chaperone BiP (also known as GRP78) was short-lived under basal conditions and ER stress. The turnover of BiP was in part driven by its amino-terminal arginylation (Nt-arginylation) by the arginyltransferase ATE1, which generated an autophagic N-degron of the N-end rule pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSPA5 | up-regulates
|
Chaperone-mediated protein folding |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265283 |
|
|
|
|
| pmid |
sentence |
| 28286085 |
The HSPA5 gene encodes the binding immunoglobulin protein (BiP), an Hsp70 family chaperone localized in the ER lumen.|When unfolded/misfolded proteins in the ER overwhelm the capacity of protein folding machinery, BiP can initiate the unfolded protein response (UPR), decrease unfolded/misfolded protein load, induce autophagy, and crosstalk with apoptosis machinery to assist in the cell survival decision. |
|
| Publications: |
1 |
| + |
HSPA5 | down-regulates activity
binding
|
EIF2AK3 |
0.715 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260164 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31226023 |
In the stressed ER, protein chaperone GRP78 binds to unfolded proteins and dissociates from the luminal domain of PERK, leading to oligomerization and activation of PERK by autophosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
E2F1 | down-regulates quantity by repression
transcriptional regulation
|
HSPA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253845 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18840615 |
we show that E2F1 represses GRP78/BIP at the transcriptional level, and this requires its DNA binding domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SEC61 complex | up-regulates activity
binding
|
HSPA5 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265276 |
|
|
|
|
| pmid |
sentence |
| 33925740 |
This is where allosteric effectors of the Sec61 complex (BiP together with Sec62/Sec63 complex or TRAP complex) (Figure 2 and Figure 5) and auxiliary membrane protein insertases (EMC and TMCO1 complex) join the game |
|
| Publications: |
1 |
| + |
HSPA5 | down-regulates activity
binding
|
ATF6 |
0.816 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260179 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31226023 |
Similar to PERK and IRE1, ATF6 is activated by ER stress-induced dissociation from GRP78 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
3.0
HSPA5
- 
- 