BARD1
Gene Ontology Biological Process
- cell cycle arrest [NAS]
- cellular response to DNA damage stimulus [NAS]
- negative regulation of apoptotic process [IMP]
- negative regulation of mRNA 3'-end processing [NAS]
- negative regulation of protein export from nucleus [IDA]
- positive regulation of apoptotic process [IMP]
- positive regulation of protein catabolic process [NAS]
- protein K6-linked ubiquitination [IDA]
- protein ubiquitination [NAS]
- regulation of phosphorylation [IMP]
- tissue homeostasis [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
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.
Publication
The BARD1 BRCT domain contributes to p53 binding, cytoplasmic and mitochondrial localization, and apoptotic function.
BARD1 is a breast cancer tumor suppressor with multiple domains and functions. BARD1 comprises a tandem BRCT domain at the C-terminus, and this sequence has been reported to target BARD1 to distinct subcellular locations such as nuclear DNA breakage sites and the centrosome through binding to regulatory proteins such as HP1 and OLA1, respectively. We now identify the BRCT domain ... [more]
Throughput
- Low Throughput
Additional Notes
- PLA
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| BARD1 TP53 | 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 | - | |
| BARD1 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 | 244460 | |
| BARD1 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 BARD1 | 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 | - | |
| BARD1 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 BARD1 | 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