+ |
Unfolded_Proteins | up-regulates
|
CREB3L1 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-143823 |
|
|
Homo sapiens |
|
pmid |
sentence |
16417584 |
Oasis (old astrocyte specifically induced substance) is an er stress transducer in astrocytes, a membrane-bound transcription factor that activates genes in the er stress response / when unfolded proteins accumulate in the er, oasis is cleaved at the membrane to release its cytoplasmic domain, which then enters the nucleus and activates target genes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
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 |
+ |
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 |
+ |
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 |
+ |
Unfolded_Proteins | up-regulates quantity by expression
|
HERPUD1 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80156 |
|
|
Homo sapiens |
|
pmid |
sentence |
10922362 |
We demonstrate a new target gene for upr-induced transcription, herp. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Unfolded_Proteins | up-regulates
|
Protein_aggregates |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262268 |
|
|
|
|
pmid |
sentence |
9502314 |
Inclusion body formation and other aggregates formed during protein folding have been assumed to arise from hydrophobic aggregation of the unfolded or denatured states |
|
Publications: |
1 |
+ |
Unfolded_Proteins | up-regulates
|
CREB3L2 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151312 |
|
|
Homo sapiens |
|
pmid |
sentence |
17178827 |
Although bbf2h7 protein is not expressed under normal conditions, it is markedly induced at the translational level during er stress, suggesting that bbf2h7 might contribute to only the late phase of unfolded protein response signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Unfolded_Proteins | up-regulates
|
ERN1 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260175 |
|
|
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 |
+ |
UBQLN2 | down-regulates
|
Unfolded_Proteins |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262267 |
|
|
Mus musculus |
|
pmid |
sentence |
27477512 |
UBQLN2 recognizes client-bound HSP70 and links it to the proteasome to allow for the degradation of aggregated and misfolded proteins. |
|
Publications: |
1 |
Organism: |
Mus Musculus |