BAIT
F2
PT, RPRGL2, THPH1
coagulation factor II (thrombin)
GO Process (24)
GO Function (5)
GO Component (7)
Gene Ontology Biological Process
- blood coagulation [TAS]
- blood coagulation, intrinsic pathway [TAS]
- cell surface receptor signaling pathway [IDA]
- cellular protein metabolic process [TAS]
- cytosolic calcium ion homeostasis [IDA]
- fibrinolysis [IDA]
- leukocyte migration [TAS]
- multicellular organismal development [TAS]
- negative regulation of astrocyte differentiation [IDA]
- negative regulation of fibrinolysis [TAS]
- negative regulation of platelet activation [TAS]
- negative regulation of proteolysis [IDA]
- peptidyl-glutamic acid carboxylation [TAS]
- platelet activation [IDA, TAS]
- positive regulation of blood coagulation [IDA]
- positive regulation of collagen biosynthetic process [IDA]
- positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway [IDA]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of reactive oxygen species metabolic process [IDA]
- positive regulation of release of sequestered calcium ion into cytosol [IDA]
- post-translational protein modification [TAS]
- proteolysis [TAS]
- regulation of blood coagulation [TAS]
- response to wounding [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
SERPIND1
D22S673, HC2, HCF2, HCII, HLS2, LS2, THPH10
serpin peptidase inhibitor, clade D (heparin cofactor), member 1
GO Process (2)
GO Function (2)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism.
The serine proteases sequentially activated to form a fibrin clot are inhibited primarily by members of the serpin family, which use a unique beta-sheet expansion mechanism to trap and destroy their targets. Since the discovery that serpins were a family of serine protease inhibitors there has been controversy as to the role of conformational change in their mechanism. It now ... [more]
Proc. Natl. Acad. Sci. U.S.A. Aug. 20, 2002; 99(17);11079-84 [Pubmed: 12169660]
Throughput
- Low Throughput
Curated By
- BioGRID