BAIT
PLG
RP1-81D8.1
plasminogen
GO Process (12)
GO Function (6)
GO Component (8)
Gene Ontology Biological Process
- blood coagulation [IMP, TAS]
- cellular protein metabolic process [TAS]
- extracellular matrix disassembly [IDA, TAS]
- extracellular matrix organization [TAS]
- fibrinolysis [TAS]
- negative regulation of cell proliferation [TAS]
- negative regulation of cell-cell adhesion mediated by cadherin [TAS]
- negative regulation of cell-substrate adhesion [IDA]
- negative regulation of fibrinolysis [IDA]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of fibrinolysis [IDA]
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
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Plasminogen and angiostatin interact with heat shock proteins.
Previous studies from this laboratory have demonstrated that plasminogen and angiostatin bind to endothelial cell (EC) surface-associated actin via their kringles in a specific manner. Heat shock proteins (hsps) like hsp 27 are constitutively expressed by vascular ECs and regulate actin polymerization, cell growth, and migration. Since many hsps have also been found to be highly abundant on cell surfaces ... [more]
Mol. Cell. Biochem. Jun. 01, 2007; 300(1);197-205 [Pubmed: 17206383]
Throughput
- Low Throughput
Additional Notes
- identical bait gene/protein (PLG) represents binding of both angiostatin and plasminogen to HSPs
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PLG HSPA1A | Far Western Far Western An interaction is detected between a protein immobilized on a membrane and a purified protein probe. | Low | - | BioGRID | 859995 |
Curated By
- BioGRID