BAG1
Gene Ontology Biological Process
Gene Ontology Molecular Function
BCL2
Gene Ontology Biological Process
- B cell proliferation [IDA]
- B cell receptor signaling pathway [IMP]
- apoptotic process [IDA, TAS]
- cellular response to DNA damage stimulus [IMP]
- defense response to virus [IDA]
- endoplasmic reticulum calcium ion homeostasis [TAS]
- extrinsic apoptotic signaling pathway via death domain receptors [IDA]
- female pregnancy [NAS]
- humoral immune response [TAS]
- innate immune response [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- intrinsic apoptotic signaling pathway in response to DNA damage [IBA]
- intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [IDA]
- negative regulation of anoikis [IMP]
- negative regulation of apoptotic process [IDA, IMP]
- negative regulation of apoptotic signaling pathway [IMP]
- negative regulation of autophagy [TAS]
- negative regulation of cellular pH reduction [IDA]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [IGI]
- negative regulation of intrinsic apoptotic signaling pathway [IDA]
- negative regulation of mitochondrial depolarization [TAS]
- negative regulation of neuron apoptotic process [IDA]
- neuron apoptotic process [TAS]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- positive regulation of B cell proliferation [IMP]
- positive regulation of cell growth [IDA]
- positive regulation of intrinsic apoptotic signaling pathway [TAS]
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [TAS]
- protein polyubiquitination [IDA]
- regulation of calcium ion transport [IDA]
- regulation of mitochondrial membrane permeability [ISS]
- regulation of mitochondrial membrane potential [ISS]
- regulation of protein heterodimerization activity [IDA]
- regulation of protein homodimerization activity [IDA]
- regulation of transmembrane transporter activity [IDA]
- release of cytochrome c from mitochondria [ISS, NAS]
- response to cytokine [IDA]
- response to drug [IDA, IMP]
- response to iron ion [IDA]
- response to nicotine [IDA]
- response to radiation [NAS]
- response to toxic substance [IDA]
- transmembrane transport [IDA]
Gene Ontology Molecular Function- BH3 domain binding [IPI]
- channel activity [IDA]
- channel inhibitor activity [IDA]
- identical protein binding [IPI]
- protease binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- protein homodimerization activity [IPI]
- sequence-specific DNA binding [IDA]
- ubiquitin protein ligase binding [IPI]
- BH3 domain binding [IPI]
- channel activity [IDA]
- channel inhibitor activity [IDA]
- identical protein binding [IPI]
- protease binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- protein homodimerization activity [IPI]
- sequence-specific DNA binding [IDA]
- ubiquitin protein ligase binding [IPI]
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
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
The 70 kDa heat shock family of molecular chaperones is essential to a variety of cellular processes, yet it is unclear how these proteins are regulated in vivo. We present evidence that the protein BAG-1 is a potential modulator of the molecular chaperones, Hsp70 and Hsc70. BAG-1 binds to the ATPase domain of Hsp70 and Hsc70, without requirement for their ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID