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
PARK7
DJ-1, DJ1, HEL-S-67p, CTA-215D11.1
parkinson protein 7
GO Process (59)
GO Function (27)
GO Component (9)
Gene Ontology Biological Process
- Ras protein signal transduction [TAS]
- activation of protein kinase B activity [IC]
- cellular response to glyoxal [IDA]
- cellular response to hydrogen peroxide [IDA]
- cellular response to oxidative stress [IDA, IMP]
- glycolate biosynthetic process [IDA]
- glyoxal catabolic process [IDA]
- hydrogen peroxide metabolic process [IDA]
- lactate biosynthetic process [IDA]
- methylglyoxal catabolic process to D-lactate [IDA]
- mitochondrion organization [ISS]
- negative regulation of TRAIL-activated apoptotic signaling pathway [IMP]
- negative regulation of apoptotic process [IDA]
- negative regulation of cell death [IDA]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [IMP]
- negative regulation of death-inducing signaling complex assembly [IC]
- negative regulation of extrinsic apoptotic signaling pathway [IMP]
- negative regulation of gene expression [IDA]
- negative regulation of hydrogen peroxide-induced cell death [IMP]
- negative regulation of hydrogen peroxide-induced neuron death [IDA]
- negative regulation of neuron apoptotic process [IDA]
- negative regulation of neuron death [IDA]
- negative regulation of oxidative stress-induced cell death [IDA]
- negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [IDA]
- negative regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- negative regulation of protein K48-linked deubiquitination [IDA]
- negative regulation of protein acetylation [IDA]
- negative regulation of protein binding [IDA, IGI, IMP]
- negative regulation of protein export from nucleus [IGI]
- negative regulation of protein kinase activity [IGI]
- negative regulation of protein phosphorylation [IGI]
- negative regulation of protein sumoylation [IDA]
- negative regulation of protein ubiquitination [IDA]
- negative regulation of ubiquitin-protein transferase activity [IDA]
- negative regulation of ubiquitin-specific protease activity [IDA]
- positive regulation of L-dopa biosynthetic process [IMP]
- positive regulation of L-dopa decarboxylase activity [IDA]
- positive regulation of androgen receptor activity [IMP]
- positive regulation of dopamine biosynthetic process [IC, IDA]
- positive regulation of gene expression [TAS]
- positive regulation of interleukin-8 production [IDA]
- positive regulation of mitochondrial electron transport, NADH to ubiquinone [IMP]
- positive regulation of peptidyl-serine phosphorylation [IMP]
- positive regulation of protein homodimerization activity [IDA]
- positive regulation of protein kinase B signaling [IC]
- positive regulation of protein localization to nucleus [IDA, IMP]
- positive regulation of pyrroline-5-carboxylate reductase activity [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IMP, TAS]
- positive regulation of superoxide dismutase activity [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IGI, IMP]
- positive regulation of transcription regulatory region DNA binding [IMP]
- positive regulation of tyrosine 3-monooxygenase activity [IDA]
- protein stabilization [IDA, IMP]
- regulation of TRAIL receptor biosynthetic process [IMP]
- regulation of androgen receptor signaling pathway [IDA]
- regulation of fibril organization [TAS]
- regulation of inflammatory response [ISS]
- regulation of mitochondrial membrane potential [IMP]
- regulation of neuron apoptotic process [IDA]
Gene Ontology Molecular Function- L-dopa decarboxylase activator activity [IDA]
- androgen receptor binding [IPI]
- core promoter binding [IC]
- cupric ion binding [IDA]
- cuprous ion binding [IDA]
- cytokine binding [IPI]
- double-stranded DNA binding [IDA]
- enzyme binding [IPI]
- glyoxalase (glycolic acid-forming) activity [IDA]
- glyoxalase III activity [IDA]
- identical protein binding [IPI]
- mRNA binding [IDA]
- oxidoreductase activity, acting on peroxide as acceptor [IDA]
- peptidase activity [IDA]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- receptor binding [IPI]
- repressing transcription factor binding [IPI]
- scaffold protein binding [IPI]
- single-stranded DNA binding [IDA]
- small protein activating enzyme binding [IPI]
- small protein conjugating enzyme binding [IPI]
- superoxide dismutase copper chaperone activity [IDA]
- transcription coactivator activity [IGI, TAS]
- transcription factor binding [IPI]
- tyrosine 3-monooxygenase activator activity [IDA]
- ubiquitin-specific protease binding [IPI]
- L-dopa decarboxylase activator activity [IDA]
- androgen receptor binding [IPI]
- core promoter binding [IC]
- cupric ion binding [IDA]
- cuprous ion binding [IDA]
- cytokine binding [IPI]
- double-stranded DNA binding [IDA]
- enzyme binding [IPI]
- glyoxalase (glycolic acid-forming) activity [IDA]
- glyoxalase III activity [IDA]
- identical protein binding [IPI]
- mRNA binding [IDA]
- oxidoreductase activity, acting on peroxide as acceptor [IDA]
- peptidase activity [IDA]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- receptor binding [IPI]
- repressing transcription factor binding [IPI]
- scaffold protein binding [IPI]
- single-stranded DNA binding [IDA]
- small protein activating enzyme binding [IPI]
- small protein conjugating enzyme binding [IPI]
- superoxide dismutase copper chaperone activity [IDA]
- transcription coactivator activity [IGI, TAS]
- transcription factor binding [IPI]
- tyrosine 3-monooxygenase activator activity [IDA]
- ubiquitin-specific protease binding [IPI]
Homo sapiens
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
A novel role for the peptidyl-prolyl cis-trans isomerase Cyclophilin A in DNA-repair following replication fork stalling via the MRE11-RAD50-NBS1 complex.
Cyclosporin A (CsA) induces DNA double-strand breaks in LIG4 syndrome fibroblasts, specifically upon transit through S-phase. The basis underlying this has not been described. CsA-induced genomic instability may reflect a direct role of Cyclophilin A (CYPA) in DNA repair. CYPA is a peptidyl-prolyl cis-trans isomerase (PPI). CsA inhibits the PPI activity of CYPA. Using an integrated approach involving CRISPR/Cas9-engineering, siRNA, ... [more]
EMBO Rep Aug. 01, 2024; 25(8);3432-3455 [Pubmed: 38943005]
Throughput
- High Throughput
Additional Notes
- BioID
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PARK7 PPIA | Affinity Capture-MS 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. | High | 0.0023 | BioGRID | 2361809 | |
| PPIA PARK7 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 1.7299 | BioGRID | 2624811 |
Curated By
- BioGRID