LONP1
Gene Ontology Biological Process
- cellular response to oxidative stress [IC, IDA]
- mitochondrial DNA metabolic process [NAS]
- mitochondrial genome maintenance [NAS]
- mitochondrion organization [IMP]
- oxidation-dependent protein catabolic process [IMP]
- protein homooligomerization [IDA]
- proteolysis involved in cellular protein catabolic process [IDA]
- response to hypoxia [IEP]
Gene Ontology Molecular Function- ADP binding [IDA]
- ATP binding [IDA]
- ATP-dependent peptidase activity [IDA]
- DNA polymerase binding [IPI]
- G-quadruplex DNA binding [IDA]
- mitochondrial heavy strand promoter anti-sense binding [IDA]
- mitochondrial heavy strand promoter sense binding [IDA]
- mitochondrial light strand promoter anti-sense binding [IDA]
- mitochondrial light strand promoter sense binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding [IDA]
- single-stranded RNA binding [IDA]
- ADP binding [IDA]
- ATP binding [IDA]
- ATP-dependent peptidase activity [IDA]
- DNA polymerase binding [IPI]
- G-quadruplex DNA binding [IDA]
- mitochondrial heavy strand promoter anti-sense binding [IDA]
- mitochondrial heavy strand promoter sense binding [IDA]
- mitochondrial light strand promoter anti-sense binding [IDA]
- mitochondrial light strand promoter sense binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding [IDA]
- single-stranded RNA binding [IDA]
Gene Ontology Cellular Component
HSPA8
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- RNA metabolic process [TAS]
- axon guidance [TAS]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- membrane organization [TAS]
- negative regulation of fibril organization [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- neurotransmitter secretion [TAS]
- post-Golgi vesicle-mediated transport [TAS]
- protein folding [NAS]
- protein refolding [IDA]
- response to unfolded protein [NAS]
- synaptic transmission [TAS]
Gene Ontology Molecular Function- ATP binding [IDA]
- ATPase activity [IDA]
- ATPase activity, coupled [NAS]
- G-protein coupled receptor binding [IPI]
- MHC class II protein complex binding [IDA]
- enzyme binding [IPI]
- heat shock protein binding [IPI]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IDA]
- ATP binding [IDA]
- ATPase activity [IDA]
- ATPase activity, coupled [NAS]
- G-protein coupled receptor binding [IPI]
- MHC class II protein complex binding [IDA]
- enzyme binding [IPI]
- heat shock protein binding [IPI]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IDA]
Gene Ontology Cellular Component
- Prp19 complex [IDA]
- blood microparticle [IDA]
- clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane [TAS]
- cytosol [IDA, TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- intracellular [NAS]
- membrane [IDA]
- nucleus [IDA]
- plasma membrane [TAS]
- ribonucleoprotein complex [IDA]
- ubiquitin ligase complex [IDA]
Affinity Capture-Western
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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.
Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID