DNAJA3
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- mitochondrion organization [IBA]
- negative regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- negative regulation of NF-kappaB transcription factor activity [IDA]
- negative regulation of apoptotic process [IDA]
- negative regulation of cell proliferation [IDA]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- negative regulation of interferon-gamma-mediated signaling pathway [IDA]
- negative regulation of protein kinase activity [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- neuromuscular junction development [IDA]
- positive regulation of apoptotic process [IDA]
- positive regulation of protein ubiquitination [IDA]
- protein folding [IDA]
- protein refolding [IBA]
- protein stabilization [IDA]
- response to interferon-gamma [IDA]
- skeletal muscle acetylcholine-gated channel clustering [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- I-kappaB/NF-kappaB complex [IDA]
- IkappaB kinase complex [IDA]
- actin filament [IDA]
- cytoplasm [IDA]
- cytosol [IMP]
- extrinsic component of plasma membrane [ISS]
- intracellular membrane-bounded organelle [IDA]
- mitochondrial matrix [IDA]
- mitochondrial nucleoid [IDA]
- mitochondrion [IDA]
- neuromuscular junction [ISS]
- nucleus [IDA]
- postsynaptic membrane [ISS]
HSPA9
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease.
Parkinson's disease (PD) is the second most prevalent progressive neurological disorder commonly associated with impaired mitochondrial function in dopaminergic neurons. Although familial PD is multifactorial in nature, a recent genetic screen involving PD patients identified two mitochondrial Hsp70 variants (P509S and R126W) that are suggested in PD pathogenesis. However, molecular mechanisms underlying how mtHsp70 PD variants are centrally involved in ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| DNAJA3 HSPA9 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 13.01 | BioGRID | 2937025 | |
| HSPA9 DNAJA3 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 715552 | |
| DNAJA3 HSPA9 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 1 | BioGRID | 1263384 |
Curated By
- BioGRID