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
HSPA1A
HEL-S-103, HSP70-1, HSP70-1A, HSP70I, HSP72, HSPA1, DAQB-147D11.1
heat shock 70kDa protein 1A
GO Process (20)
GO Function (13)
GO Component (17)
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- RNA metabolic process [TAS]
- cellular heat acclimation [IMP]
- cellular response to heat [IDA]
- cellular response to oxidative stress [TAS]
- gene expression [TAS]
- mRNA catabolic process [IDA]
- mRNA metabolic process [TAS]
- negative regulation of apoptotic process [IMP, TAS]
- negative regulation of cell death [IDA, IMP]
- negative regulation of cell growth [IMP]
- negative regulation of cell proliferation [IMP]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [IMP]
- negative regulation of inclusion body assembly [IDA]
- negative regulation of protein ubiquitination [IDA]
- positive regulation of erythrocyte differentiation [IMP]
- protein refolding [IDA]
- protein stabilization [TAS]
- regulation of cell death [IMP]
- response to unfolded protein [IDA]
Gene Ontology Molecular Function- ATP binding [IDA]
- ATPase activity [IDA]
- ATPase activity, coupled [IDA]
- G-protein coupled receptor binding [IPI]
- double-stranded RNA binding [IDA]
- enzyme binding [IPI]
- heat shock protein binding [IPI]
- poly(A) RNA binding [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein binding involved in protein folding [IDA]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IDA, NAS, TAS]
- ATP binding [IDA]
- ATPase activity [IDA]
- ATPase activity, coupled [IDA]
- G-protein coupled receptor binding [IPI]
- double-stranded RNA binding [IDA]
- enzyme binding [IPI]
- heat shock protein binding [IPI]
- poly(A) RNA binding [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein binding involved in protein folding [IDA]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IDA, NAS, TAS]
Gene Ontology Cellular Component
- COP9 signalosome [IDA]
- aggresome [IDA]
- blood microparticle [IDA]
- centriole [IDA]
- cytoplasm [IDA, TAS]
- cytosol [IDA, TAS]
- endoplasmic reticulum [TAS]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- inclusion body [IDA]
- mitochondrion [TAS]
- nuclear speck [IDA]
- nucleus [IDA]
- perinuclear region of cytoplasm [IDA]
- ribonucleoprotein complex [IDA]
- ubiquitin ligase complex [IDA]
- vesicle [IDA]
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