TP53
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator [IDA, IMP]
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [TAS]
- DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [IMP]
- DNA strand renaturation [IDA]
- ER overload response [IDA]
- Notch signaling pathway [TAS]
- Ras protein signal transduction [IEP]
- apoptotic process [TAS]
- base-excision repair [TAS]
- blood coagulation [TAS]
- cell aging [IMP]
- cell cycle arrest [IDA, IMP]
- cell differentiation [TAS]
- cell proliferation [TAS]
- cellular protein localization [IDA]
- cellular response to DNA damage stimulus [IDA]
- cellular response to UV [IBA]
- cellular response to drug [IEP]
- cellular response to glucose starvation [IDA]
- cellular response to hypoxia [IEP]
- cellular response to ionizing radiation [IMP]
- chromatin assembly [IDA]
- determination of adult lifespan [ISS]
- intrinsic apoptotic signaling pathway [TAS]
- intrinsic apoptotic signaling pathway by p53 class mediator [IMP]
- intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [IDA]
- mitotic G1 DNA damage checkpoint [IMP]
- multicellular organismal development [IMP]
- negative regulation of apoptotic process [IDA]
- negative regulation of cell growth [IMP]
- negative regulation of cell proliferation [ISS]
- negative regulation of fibroblast proliferation [IMP]
- negative regulation of helicase activity [TAS]
- negative regulation of transcription from RNA polymerase II promoter [IBA, IDA, ISS]
- negative regulation of transcription, DNA-templated [ISS]
- nucleotide-excision repair [IMP]
- oligodendrocyte apoptotic process [IDA]
- oxidative stress-induced premature senescence [IMP]
- positive regulation of apoptotic process [IDA]
- positive regulation of cell cycle arrest [IMP]
- positive regulation of histone deacetylation [IBA]
- positive regulation of intrinsic apoptotic signaling pathway [IMP]
- positive regulation of neuron apoptotic process [IBA]
- positive regulation of peptidyl-tyrosine phosphorylation [ISS]
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [TAS]
- positive regulation of protein oligomerization [IDA]
- positive regulation of reactive oxygen species metabolic process [IMP]
- positive regulation of release of cytochrome c from mitochondria [IDA]
- positive regulation of thymocyte apoptotic process [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IGI, IMP]
- positive regulation of transcription, DNA-templated [IDA, IMP]
- protein complex assembly [IDA]
- protein localization [IDA]
- protein tetramerization [TAS]
- regulation of apoptotic process [IDA]
- regulation of mitochondrial membrane permeability [TAS]
- regulation of transcription, DNA-templated [IDA]
- replicative senescence [IMP]
- response to X-ray [IBA]
- response to antibiotic [IEP]
- response to gamma radiation [IMP]
Gene Ontology Molecular Function- ATP binding [IDA]
- DNA binding [IMP]
- RNA polymerase II transcription factor binding [IPI]
- RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- chaperone binding [IPI]
- chromatin binding [IDA]
- copper ion binding [IDA]
- damaged DNA binding [IBA]
- enzyme binding [IPI]
- histone acetyltransferase binding [IPI]
- identical protein binding [IPI]
- p53 binding [IBA]
- protease binding [IPI]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- protein kinase binding [IPI]
- protein phosphatase 2A binding [IPI]
- protein phosphatase binding [IPI]
- receptor tyrosine kinase binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription factor binding [IPI]
- transcription regulatory region DNA binding [IDA]
- ubiquitin protein ligase binding [IPI]
- zinc ion binding [TAS]
- ATP binding [IDA]
- DNA binding [IMP]
- RNA polymerase II transcription factor binding [IPI]
- RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- chaperone binding [IPI]
- chromatin binding [IDA]
- copper ion binding [IDA]
- damaged DNA binding [IBA]
- enzyme binding [IPI]
- histone acetyltransferase binding [IPI]
- identical protein binding [IPI]
- p53 binding [IBA]
- protease binding [IPI]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- protein kinase binding [IPI]
- protein phosphatase 2A binding [IPI]
- protein phosphatase binding [IPI]
- receptor tyrosine kinase binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription factor binding [IPI]
- transcription regulatory region DNA binding [IDA]
- ubiquitin protein ligase binding [IPI]
- zinc ion binding [TAS]
Gene Ontology Cellular Component
DNAJB1
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.
Using highly purified proteins, we have identified intermediate reactions that lead to the assembly of molecular chaperone complexes with wild-type or mutant p53R175H protein. Hsp90 possesses higher affinity for wild-type p53 than for the conformational mutant p53R175H. The presence of Hsp90 in a complex with wild-type p53 inhibits the binding of Hsp40 and Hsc70 to p53, consequently preventing the formation ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TP53 DNAJB1 | 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. | Low | - | BioGRID | - | |
| DNAJB1 TP53 | Affinity Capture-Western 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. | Low | - | BioGRID | - | |
| TP53 DNAJB1 | Affinity Capture-Western 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. | Low | - | BioGRID | - |
Curated By
- BioGRID