Co-chaperone for HSPA8/Hsc70. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV.
|Gene References into Functions
- that DNAJA1 controls the fate of misfolded stabilization of mutant p53 PMID: 27775703
- Therefore, we propose that DnaJA1 is co-opted by the influenza A virus to enter the nucleus and to enhance its RNA polymerase activity in an Hsp70 cochaperone-independent manner. PMID: 25253355
- structure and function of human DNAJA1 and its relationship to pancreatic cancer PMID: 24512202
- we combined the Hsp70-NEF pairs with cochaperones of the J protein family (DnaJA1, DnaJA2, DnaJB1, and DnaJB4) to generate 16 permutations. PMID: 24318877
- Moreover, the levels of DnaJA1 and Hsp70 seem to play against each other with regard to tau: as DnaJA1 levels increase, tau levels are reduced, but this can be prevented if Hsp70 levels are simultaneously induced. PMID: 22343013
- Hdj2 directly associates with Japanese encephalitis virus nonstructural protein NS5 and facilitates viral replication. PMID: 21999493
- Hsc70 and a dimer of DjA1 independently bind to an unfolded protein PMID: 20363747
- Hsp40 type 1 chaperones DJA1 (DNAJA1/Hdj2) and DJA2 (DNAJA2) as key modulators of hERG degradation PMID: 19940115
- Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy PMID: 11796717
- HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor PMID: 11809754
- sequence analysis of two isoforms PMID: 12974469
- Multiple tissue polymerase chain reaction (PCR) results showed that nDnaJA1 expressed highly in testis and lung but low in thymus, prostate, colon and liver PMID: 15595953
- Results indicate that DjA1 and DjB4 of subfamilies A and B of human Hsp40 have different quaternary structures and chaperone functions. PMID: 15661747
- DJA1 was inhibitory of refolding with DJA2 and Hsc70. PMID: 18684711
||Membrane; Lipid-anchor. Cytoplasm. Microsome. Nucleus. Cytoplasm, perinuclear region. Mitochondrion.
||Ubiquitous. Isoform 2 is highly expressed in testis and lung, but detected at low levels in thymus, prostate, colon and liver.