| + |
ERK1/2 | down-regulates quantity by destabilization 
phosphorylation
|
XBP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276439 |
Ser181 |
QQVQAQLsPLQNISP |
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 23277279 |
Phosphorylation of XBP-1u by ERK is critical for the increased interaction of XBP-1u and FoxO1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276438 |
Ser68 |
RQRLTHLsPEEKALR |
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 23277279 |
Phosphorylation of XBP-1u by ERK is critical for the increased interaction of XBP-1u and FoxO1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
Exosome_Complex | up-regulates quantity 
relocalization
|
XBP1 (isoform 2) |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260946 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30319453 |
When the ER stress-induced unfolded protein response (UPR) is activated, the X-box binding protein 1 (XBP1) mRNA is spliced by inositol-requiring enzyme-1α (IRE1α) to produce the spliced form of XBP1 (sXBP1). In the present study, we found that sXBP1 mRNA in the cell may be incorporated into the exosomes and was released extracellularly. Spliced form of XBP1 mRNA was incorporated into the exosomes of HEK293T cells, which overexpress IRE1α. We found that one of the ER stress signal-induced transcripts, sXBP1, was incorporated into the exosomes. Our results suggest that exosomes may play a vital role in the extracellular release of ER stress signals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | SARS-CoV ER STRESS |
| + |
SIRT1 | down-regulates activity
deacetylation
|
XBP1 (isoform 2) |
0.389 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260430 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20955178 |
P300 increases the acetylation and protein stability of XBP1s, and enhances its transcriptional activity, whereas SIRT1 deacetylates XBP1s and inhibits its transcriptional activity.. The mRNA encoding the active spliced form of XBP1 (XBP1s) is generated from the unspliced form by IRE1 (inositol-requiring enzyme 1) during the UPR. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XBP1 | up-regulates quantity by expression 
transcriptional regulation
|
NPPB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255609 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20170659 |
The promoter assay with overexpression of sXBP1 or norepinephrine showed that the proximal AP1/CRE-like element in the promoter region of BNP was critical for transcriptional regulation of BNP by sXBP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMA5 | down-regulates quantity by destabilization
binding
|
XBP1 |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-239213 |
|
|
in vitro |
|
| pmid |
sentence |
| 19941857 |
We saw preferential binding of XBP-1u to subunits _5, _6 and _7.2. We demonstrate that XBP-1u undergoes efficient degradation in vitro by 20S proteasomes in the absence of ubiquitination. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
XBP1 (isoform 2) | down-regulates 
|
Unfolded_Proteins |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260186 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15598891 |
ATF6 and XBP1 are transcription factors activated specifically in response to endoplasmic reticulum (ER) stress. Three cis-acting elements capable of binding to ATF6, XBP1 or both have been identified to date, namely ER stress-response element (ERSE), unfolded protein response element (UPRE) and ERSE-II. ERSE controls the expression of ER-localized molecular chaperones such as BiP that can refold unfolded proteins in the ER; transcription from ERSE is fully activated by ATF6 even in the absence of XBP1. In contrast, transcription from UPRE depends solely on XBP1 and it has been suggested that UPRE may control the expression of components of the ER-associated degradation system that can degrade unfolded proteins in the ER. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
ATF6 | up-regulates quantity by expression
transcriptional regulation
|
XBP1 (isoform 2) |
0.677 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260184 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31226023 |
Apart from ER protein chaperones, ATF6 also induces the expression of CHOP and XBP1, thereby connecting the three UPR branches into an integrated signaling network |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
ERN1 | up-regulates quantity by expression
post transcriptional regulation
|
XBP1 (isoform 2) |
0.638 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260183 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31226023 |
Upon activation by oligomerization and autophosphorylation, the cytosolic RNase domain of IRE1 mediates an unconventional splicing of the mRNA of X-box-binding protein 1 (XBP1). The spliced and frameshifted transcript encodes XBP1S, a bZIP transcription factor inducing the expression of numerous UPR effector genes that enhance ER folding capacity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
EP300 | up-regulates quantity by stabilization
acetylation
|
XBP1 (isoform 2) |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260429 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20955178 |
P300 increases the acetylation and protein stability of XBP1s, and enhances its transcriptional activity, whereas SIRT1 deacetylates XBP1s and inhibits its transcriptional activity.. The mRNA encoding the active spliced form of XBP1 (XBP1s) is generated from the unspliced form by IRE1 (inositol-requiring enzyme 1) during the UPR. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network |
| + |
PSMA7 | down-regulates quantity by destabilization
binding
|
XBP1 |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-239042 |
|
|
in vitro |
|
| pmid |
sentence |
| 19941857 |
We saw preferential binding of XBP-1u to subunits _5, _6 and _7.2. We demonstrate that XBP-1u undergoes efficient degradation in vitro by 20S proteasomes in the absence of ubiquitination. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
XBP1 | up-regulates activity
binding
|
XBP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-224199 |
|
|
in vitro |
|
| pmid |
sentence |
| 12805554 |
E4BP4, ATF-6, OASIS, and XBP-1 all formed strong homodimeric associations on the array Transcription factor dimerization can increase the selectivity of protein-DNA interactions and generate a large amount of DNA binding diversity from a relatively small number of proteins |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
XBP1 | up-regulates activity
|
B-Lymphocyte_diff |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259957 |
|
|
Homo sapiens |
Plasma Cell |
| pmid |
sentence |
| 11460154 |
XBP-1 is the only transcription factor known to be selectively and specifically required for the terminal differentiation of B lymphocytes to plasma cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XBP1 (isoform 2) | up-regulates
|
Chaperone-mediated protein folding |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260185 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15598891 |
ATF6 and XBP1 are transcription factors activated specifically in response to endoplasmic reticulum (ER) stress. Three cis-acting elements capable of binding to ATF6, XBP1 or both have been identified to date, namely ER stress-response element (ERSE), unfolded protein response element (UPRE) and ERSE-II. ERSE controls the expression of ER-localized molecular chaperones such as BiP that can refold unfolded proteins in the ER; transcription from ERSE is fully activated by ATF6 even in the absence of XBP1. In contrast, transcription from UPRE depends solely on XBP1 and it has been suggested that UPRE may control the expression of components of the ER-associated degradation system that can degrade unfolded proteins in the ER. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PSMA6 | down-regulates quantity by destabilization
binding
|
XBP1 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-239039 |
|
|
in vitro |
|
| pmid |
sentence |
| 19941857 |
We saw preferential binding of XBP-1u to subunits _5, _6 and _7.2. We demonstrate that XBP-1u undergoes efficient degradation in vitro by 20S proteasomes in the absence of ubiquitination. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BACH2 | down-regulates quantity by repression
transcriptional regulation
|
XBP1 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253756 |
|
|
Homo sapiens |
B-cell Leukemia Cell |
| pmid |
sentence |
| 24821775 |
Expression and activity of the UPR downstream effector XBP1 is regulated positively by STAT5 and negatively by the B-cell-specific transcriptional repressors BACH2 and BCL6. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
XBP1
- 
- 