| + |
Unfolded_Proteins | up-regulates 
|
ERP44 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261047 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11847130 |
Like many ER folding factors, ERp44 transcripts are induced by agents that cause the accumulation of unfolded proteins in the ER. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERP44 | down-regulates activity 
binding
|
ITPR1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261046 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15652484 |
In this study, we found that ERp44, an ER lumenal protein of the thioredoxin family, directly interacts with the third lumenal loop of IP(3)R type 1 (IP(3)R1) and that the interaction is dependent on pH, Ca(2+) concentration, and redox state. In this study we demonstrated that ERp44 directly interacts with the L3V domain of IP3R1, thereby inhibiting its channel activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERO1A | up-regulates quantity by stabilization 
binding
|
ERP44 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261049 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11847130 |
Here, we report the functional characterization of a novel UPR-induced ER resident protein (ERp44) that forms mixed disulfides with both hEROs, as well as with partially unfolded Ig subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERO1B | up-regulates quantity by stabilization
binding
|
ERP44 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261048 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11847130 |
Here, we report the functional characterization of a novel UPR-induced ER resident protein (ERp44) that forms mixed disulfides with both hEROs, as well as with partially unfolded Ig subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ERP44
- 
- 