BAIT
PPIA
CYPA, CYPH, HEL-S-69p
peptidylprolyl isomerase A (cyclophilin A)
GO Process (18)
GO Function (5)
GO Component (7)
Gene Ontology Biological Process
- RNA-dependent DNA replication [TAS]
- blood coagulation [TAS]
- entry into host cell [TAS]
- establishment of integrated proviral latency [TAS]
- leukocyte migration [TAS]
- lipid particle organization [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of protein secretion [IMP]
- positive regulation of viral genome replication [IMP]
- protein folding [TAS]
- protein peptidyl-prolyl isomerization [IDA]
- regulation of viral genome replication [IMP, TAS]
- uncoating of virus [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral release from host cell [TAS]
- virion assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
HNRNPM
CEAR, HNRNPM4, HNRPM, HNRPM4, HTGR1, NAGR1, hnRNP M
heterogeneous nuclear ribonucleoprotein M
GO Process (4)
GO Function (4)
GO Component (9)
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
Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.
Peptidylprolyl isomerase A (PPIA), also known as cyclophilin A, is a multifunctional protein with peptidyl-prolyl cis-trans isomerase activity. PPIA is also a translational biomarker for amyotrophic lateral sclerosis, and is enriched in aggregates isolated from amyotrophic lateral sclerosis and frontotemporal lobar degeneration patients. Its normal function in the central nervous system is unknown. Here we show that PPIA is a ... [more]
Brain Apr. 01, 2015; 138(Pt 4);974-91 [Pubmed: 25678563]
Throughput
- Low Throughput
Curated By
- BioGRID