Search Results
Overview
| Uniprot ID | Q9UBS3 |
|---|---|
| Protein Name | DnaJ homolog subfamily B member 9 |
| Gene Name | DNAJB9 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 134 | QNQNTGSKKRFENHF |
| 66 | KSPDAEAKFREIAEA |
Function
Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (PubMed:18400946). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similarity). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005788 | endoplasmic reticulum lumen |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005730 | nucleolus |
| Molecular Function | GO:0030544 | Hsp70 protein binding |
| Molecular Function | GO:0051787 | misfolded protein binding |
| Molecular Function | GO:0051087 | protein-folding chaperone binding |
| Biological Process | GO:0030183 | B cell differentiation |
| Biological Process | GO:0036503 | ERAD pathway |
| Biological Process | GO:1903895 | negative regulation of IRE1-mediated unfolded protein response |
| Biological Process | GO:0002639 | positive regulation of immunoglobulin production |
| Biological Process | GO:0034976 | response to endoplasmic reticulum stress |
| Biological Process | GO:0006986 | response to unfolded protein |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.