BAIT
SERPINF2
A2AP, AAP, ALPHA-2-PI, API, PLI
serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2
GO Process (20)
GO Function (5)
GO Component (7)
Gene Ontology Biological Process
- blood coagulation [TAS]
- blood vessel morphogenesis [ISS]
- collagen fibril organization [ISS]
- fibrinolysis [TAS]
- negative regulation of endopeptidase activity [IBA]
- negative regulation of fibrinolysis [IDA]
- negative regulation of plasminogen activation [IDA]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of ERK1 and ERK2 cascade [IDA]
- positive regulation of JNK cascade [IDA]
- positive regulation of cell differentiation [IDA]
- positive regulation of cell-cell adhesion mediated by cadherin [TAS]
- positive regulation of collagen biosynthetic process [IDA]
- positive regulation of smooth muscle cell proliferation [ISS]
- positive regulation of stress fiber assembly [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transforming growth factor beta production [IDA]
- regulation of blood vessel size by renin-angiotensin [ISS]
- regulation of proteolysis [IBA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
SSR1
TRAPA, PSEC0262
signal sequence receptor, alpha
GO Process (8)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- cellular protein metabolic process [TAS]
- cotranslational protein targeting to membrane [TAS]
- endoplasmic reticulum unfolded protein response [TAS]
- gene expression [TAS]
- positive regulation of cell proliferation [TAS]
- translation [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Toward an understanding of the protein interaction network of the human liver.
Proteome-scale protein interaction maps are available for many organisms, ranging from bacteria, yeast, worms and flies to humans. These maps provide substantial new insights into systems biology, disease research and drug discovery. However, only a small fraction of the total number of human protein-protein interactions has been identified. In this study, we map the interactions of an unbiased selection of ... [more]
Mol. Syst. Biol. Oct. 13, 2011; 7(0);536 [Pubmed: 21988832]
Throughput
- High Throughput
Curated By
- BioGRID