| + |
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 |
| + |
ATF6 | up-regulates
|
Chaperone-mediated protein folding |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260182 |
|
|
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 |
| + |
PAQosome co-chaperone complex | up-regulates
|
Chaperone-mediated protein folding |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270920 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29203338 |
The PAQosome, an R2TP-Based Chaperone for Quaternary Structure Formation. The Rvb1-Rvb2-Tah1-Pih1/prefoldin-like (R2TP/PFDL) complex is a unique chaperone that provides a platform for the assembly and maturation of many key multiprotein complexes in mammalian cells. Here, we propose to rename R2TP/PFDL as PAQosome (particle for arrangement of quaternary structure) to more accurately represent its unique function. |
|
| 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 |
| + |
Prefoldin co-chaperone | up-regulates 
|
Chaperone-mediated protein folding |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270936 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32699605 |
The correct folding is a key process for a protein to acquire its functional structure and conformation. Prefoldin is a well-known chaperone protein that regulates the correct folding of proteins. Canonical prefoldin complex is a heterohexameric complex composed of two α subunits (PFDN3 and PFDN5) and four β subunits (PFDN1, PFDN2, PFDN4 and PFDN6) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
R2SP co-chaperone | up-regulates
|
Chaperone-mediated protein folding |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270941 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29844425 |
Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Chaperone-mediated protein folding