TIMP1
Gene Ontology Biological Process
- blood coagulation [TAS]
- extracellular matrix disassembly [TAS]
- extracellular matrix organization [TAS]
- negative regulation of endopeptidase activity [IDA]
- negative regulation of membrane protein ectodomain proteolysis [IDA]
- negative regulation of metalloenzyme activity [IDA]
- negative regulation of trophoblast cell migration [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of cell proliferation [IDA]
- regulation of integrin-mediated signaling pathway [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PCSK5
Gene Ontology Biological Process
- anterior/posterior pattern specification [IMP, ISO]
- cytokine biosynthetic process [IDA]
- embryo implantation [IMP]
- embryonic digestive tract development [IMP, ISO]
- embryonic skeletal system development [IMP, ISO]
- heart development [IMP]
- kidney development [IMP, ISO]
- limb morphogenesis [IMP]
- peptide biosynthetic process [IDA, ISO]
- peptide hormone processing [IDA, ISO]
- protein processing [IDA, ISO]
- proteolysis [ISO]
- respiratory tube development [IMP]
- signal peptide processing [ISO]
- viral life cycle [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-Western
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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases.
The proprotein convertases PC5, PACE4 and furin contain a C-terminal cysteine-rich domain (CRD) of unknown function. We demonstrate that the CRD confers to PC5A and PACE4 properties to bind tissue inhibitors of metalloproteinases (TIMPs) and the cell surface. Confocal microscopy and biochemical analyses revealed that the CRD is essential for cell surface tethering of PC5A and PACE4 and that it ... [more]
Throughput
- Low Throughput
Additional Notes
- Figure 11
Curated By
- BioGRID