The Function of DNAJC10
Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress.
Protein names
Recommended name:
DnaJ homolog subfamily C member 10Alternative name(s):
Endoplasmic reticulum DNA J domain-containing protein 5ER-resident protein ERdj5
ERdj5
Macrothioredoxin
MTHr
Top Gene-Substance Interactions
DNAJC10 Interacts with These Diseases
| Disease | Score |
Substances That Increase DNAJC10
| Substances | Interaction | Organism | Category |
Substances That Decrease DNAJC10
| Substances | Interaction | Organism | Category |
Conditions with Increased Gene Activity
| Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
|---|
Conditions with Decreased Gene Activity
| Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
|---|
Technical
The following transcription factors affect gene expression:
Gene Pathways:
Induction:
By endoplasmic reticulum stress.
Molecular Function:
- Atpase Activator Activity
- Atpase Binding
- Chaperone Binding
- Disulfide Oxidoreductase Activity
- Hsp70 Protein Binding
- Misfolded Protein Binding
- Oxidoreductase Activity, Acting On A Sulfur Group Of Donors, Disulfide As Acceptor
- Protein Disulfide Oxidoreductase Activity
Biological Processes:
- Cell Redox Homeostasis
- Er-Associated Ubiquitin-Dependent Protein Catabolic Process
- Intrinsic Apoptotic Signaling Pathway In Response To Endoplasmic Reticulum Stress
- Negative Regulation Of Protein Phosphorylation
- Positive Regulation Of Atpase Activity
- Protein Folding In Endoplasmic Reticulum
- Response To Endoplasmic Reticulum Stress