BAIT
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
PREY
LUC7L
1810045C04Rik, 2410018D03Rik
Luc7 homolog (S. cerevisiae)-like
GO Process (1)
GO Function (3)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Mus musculus
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
Identification of differential protein interactors of lamin A and progerin.
The nuclear lamina is an interconnected meshwork of intermediate filament proteins underlying the nuclear envelope. The lamina is an important regulator of nuclear structural integrity as well as nuclear processes, including transcription, DNA replication and chromatin remodeling. The major components of the lamina are A- and B-type lamins. Mutations in lamins impair lamina functions and cause a set of highly ... [more]
Unknown Dec. 01, 2009; 1(6);513-525 [Pubmed: 21327095]
Throughput
- Low Throughput
Curated By
- BioGRID