BAIT
LMNA
CDCD1, CDDC, CMD1A, CMT2B1, EMD2, FPL, FPLD, FPLD2, HGPS, IDC, LDP1, LFP, LGMD1B, LMN1, LMNC, LMNL1, PRO1, RP11-54H19.1
lamin A/C
GO Process (14)
GO Function (2)
GO Component (9)
Gene Ontology Biological Process
- activation of signaling protein activity involved in unfolded protein response [TAS]
- apoptotic process [TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- cellular protein metabolic process [TAS]
- cellular response to hypoxia [IEP]
- endoplasmic reticulum unfolded protein response [TAS]
- establishment or maintenance of microtubule cytoskeleton polarity [ISS]
- mitotic cell cycle [TAS]
- mitotic nuclear envelope disassembly [TAS]
- mitotic nuclear envelope reassembly [TAS]
- muscle organ development [IMP]
- positive regulation of cell aging [IDA]
- protein localization to nucleus [ISS]
- regulation of cell migration [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
CD2BP2
FWP010, LIN1, PPP1R59, Snu40, U5-52K
CD2 (cytoplasmic tail) binding protein 2
GO Process (5)
GO Function (2)
GO Component (6)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
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.
Publication
Disruption of the lamin A and matrin-3 interaction by myopathic LMNA mutations.
The nuclear face of the nuclear membrane is enriched with the intermediate filament protein lamin A. Mutations in LMNA, the gene encoding lamin A, lead to a diverse set of inherited conditions including myopathies that affect both the heart and skeletal muscle. To gain insight about lamin A protein interactions, binding proteins associated with the tail of lamin A were ... [more]
Hum. Mol. Genet. Aug. 01, 2015; 24(15);4284-95 [Pubmed: 25948554]
Throughput
- High Throughput
Curated By
- BioGRID