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
TP53BP1
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular response to DNA damage stimulus [IDA]
- double-strand break repair [TAS]
- double-strand break repair via homologous recombination [TAS]
- positive regulation of sequence-specific DNA binding transcription factor activity [IC]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of transcription, DNA-templated [NAS]
- transcription from RNA polymerase II promoter [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor.
The BRCT (BRCA1 C-terminus) is an evolutionary conserved protein-protein interacting module found as single, tandem or multiple repeats in a diverse range of proteins known to play roles in the DNA-damage response. The BRCT domains of 53BP1 bind to the tumour suppressor p53. To investigate the nature of this interaction, we have determined the crystal structure of the 53BP1 BRCT ... [more]
Throughput
- Low Throughput
Additional Notes
- 53BP1 BRCT tandem repeat in complex with the DNA-binding domain of p53;binds to p53 through contacts with the N-terminal BRCT repeat and the inter-BRCT linker;p53 residues involved in this binding are mutated in cancer and are also important for DNA bindi
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TP53 TP53BP1 | 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 | - | BioGRID | - | |
| TP53BP1 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 TP53BP1 | 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 | - | |
| TP53BP1 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 | - | |
| TP53BP1 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 | 245022 | |
| TP53BP1 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 | 243895 | |
| TP53 TP53BP1 | 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 TP53BP1 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| TP53 TP53BP1 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 245094 | |
| TP53 TP53BP1 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| TP53BP1 TP53 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 2380463 | |
| TP53 TP53BP1 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | 2546262 | |
| TP53BP1 TP53 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | 243894 | |
| TP53BP1 TP53 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | 2380464 | |
| TP53 TP53BP1 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 244558 | |
| TP53 TP53BP1 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| TP53BP1 TP53 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| TP53 TP53BP1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |
Curated By
- BioGRID