BAIT
TRP53BP1
53BP1, Tp53bp1, m53BP1, p53BP1, RP23-437L13.2
transformation related protein 53 binding protein 1
GO Process (5)
GO Function (9)
GO Component (6)
Gene Ontology Biological Process
Gene Ontology Molecular Function- RNA polymerase II activating transcription factor binding [ISO]
- RNA polymerase II transcription cofactor activity [ISO]
- damaged DNA binding [IDA]
- methylated histone binding [ISO]
- p53 binding [ISO]
- protein binding [IPI]
- sequence-specific DNA binding [IDA]
- telomeric DNA binding [IDA]
- transcription factor binding [TAS]
- RNA polymerase II activating transcription factor binding [ISO]
- RNA polymerase II transcription cofactor activity [ISO]
- damaged DNA binding [IDA]
- methylated histone binding [ISO]
- p53 binding [ISO]
- protein binding [IPI]
- sequence-specific DNA binding [IDA]
- telomeric DNA binding [IDA]
- transcription factor binding [TAS]
Gene Ontology Cellular Component
Mus musculus
PREY
LMNA
Dhe
lamin A
GO Process (13)
GO Function (1)
GO Component (9)
Gene Ontology Biological Process
- establishment of cell polarity [NAS]
- establishment or maintenance of microtubule cytoskeleton polarity [IMP]
- muscle organ development [ISO]
- negative regulation of extrinsic apoptotic signaling pathway [IMP]
- negative regulation of release of cytochrome c from mitochondria [IMP]
- nuclear envelope organization [IGI]
- nucleus organization [IMP]
- positive regulation of cell aging [ISO]
- protein localization to nucleus [IMP]
- regulation of cell migration [IMP]
- regulation of protein localization to nucleus [IMP]
- sterol regulatory element binding protein import into nucleus [IMP]
- ventricular cardiac muscle cell development [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
Dosage Rescue
A genetic interaction is inferred when over expression or increased dosage of one gene rescues the lethality or growth defect of a strain that is mutated or deleted for another gene.
Publication
A dual role for A-type lamins in DNA double-strand break repair.
A-type lamins are emerging as regulators of nuclear organization and function. Changes in their expression are associated with cancer and mutations are linked to degenerative diseases -laminopathies-. Although a correlation exists between alterations in lamins and genomic instability, the molecular mechanisms remain largely unknown. We previously found that loss of A-type lamins leads to degradation of 53BP1 protein and defective ... [more]
Cell Cycle Aug. 01, 2011; 10(15);2549-60 [Pubmed: 21701264]
Throughput
- Low Throughput
Additional Notes
- figure 2.
Curated By
- BioGRID