Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Thrombin inhibits tumor cell growth in association with up-regulation of p21(waf/cip1) and caspases via a p53-independent, STAT-1-dependent pathway.
Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex.
Nuclear diacylglycerol kinase-theta is activated in response to alpha-thrombin.
Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha.
Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles.
Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes.
Novel fluorescent prothrombin analogs as probes of staphylocoagulase-prothrombin interactions.
Human colostrum: identification of minor proteins in the aqueous phase by proteomics.
Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation.
Reciprocal modulation of astrocyte stellation by thrombin and protease nexin-1.
Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.
NOX5 variants are functionally active in endothelial cells.
Protease nexin-1 interacts with thrombomodulin and modulates its anticoagulant effect.
Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells.
A novel protease-activated receptor-1 interactor, Bicaudal D1, regulates G protein signaling and internalization.
Proteolysis of human thrombin generates novel host defense peptides.
Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Isolation of the thrombospondin membrane receptor.
Comprehensive proteomic characterization of stem cell-derived extracellular matrices.
Localization of protease nexin-1 on the fibroblast extracellular matrix.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Mechanism of inhibition of activated protein C by protein C inhibitor.
Changes in the structure and function of the human thrombin receptor during receptor activation, internalization, and recycling.
Protein kinase C regulates pleckstrin by phosphorylation of sites adjacent to the N-terminal pleckstrin homology domain.
Inhibition of ADP-induced platelet responses by covalent modification of aggregin, a putative ADP receptor, by 8-(4-bromo-2,3-dioxobutylthio)ADP.
Molecular cloning, expression, and partial characterization of two novel members of the ovalbumin family of serine proteinase inhibitors.
Plasminogen activator inhibitor-1 and vitronectin promote the cellular clearance of thrombin by low density lipoprotein receptor-related proteins 1 and 2.
Thrombin receptors on human platelets. Initial localization and subsequent redistribution during platelet activation.
Prothrombin, albumin and immunoglobulin A form covalent complexes with alpha1-microglobulin in human plasma.
Thrombin stimulates fibroblast procollagen production via proteolytic activation of protease-activated receptor 1.
Activated thrombin (factor IIa) cleaves PAR3,4, activating them
factor XIII -> factor XIII cleaved tetramer + 2 factor XIII A activation peptides
prothrombin -> activated thrombin (factor IIa) + thrombin activation peptide (prothrombinase catalyst)
factor V -> factor Va + factor V activation peptide (thrombin catalyst)
prothrombin -> activated thrombin (factor IIa) + thrombin activation peptide (Xa catalyst)
activated thrombin (factor IIa) + antithrombin III:heparan sulfate -> thrombin:antithrombin III:heparan sulfate
fibrinogen -> fibrin monomer + 2 fibrinopeptide A + 2 fibrinopeptide B
thrombin:antithrombin III:heparan sulfate -> thrombin:cleaved antithrombin III:heparan sulfate
thrombin:cleaved SERPINC1:HSPGs-> thrombin:cleaved SERPINC1 + HSPGs
Activated thrombin:thrombomodulin cleaves PROCR:Protein C to PROCR:Activated protein C
activated thrombin (factor IIa) + thrombomodulin -> activated thrombin:thrombomodulin
factor VIII:von Willibrand factor multimer -> factor VIIIa + factor VIIIa B A3 acidic polypeptide + von Willibrand factor multimer
factor XI:platelet glycoprotein (GP) Ib:IX:V complex -> factor XIa:platelet glycoprotein (GP) Ib:IX:V complex (thrombin catalyst)
Furin cleaves pro-prothrombin to prothrombin
GGCX gamma-carboxylates F2(25-622) (pro-prothrombin)
Gamma-carboxy pro-prothrombin transport from the endoplasmic reticulum to the Golgi apparatus
Liganded Gq/11-activating GPCRs act as GEFs for Gq/11
Thrombin proteolyzes IGF:IGFBP3:ALS
Proteinase-activated receptors can bind thrombin
Thrombin binding to GP1b:IX:V
Heparin cofactor 2 (SERPIND1) binds activated thrombin (factor IIa)
Protease nexin-1 (SERPINE2) is a specific and extremely efficient inhibitor of thrombin
Liganded Gq-activating GPCRs bind inactive heterotrimeric Gq
The Ligand:GPCR:Gq complex dissociates
Thrombin, ELANE cleave C5
Factor IIa inhibitors (compounds) binds IIa
Factor IIa inhibitors (peptide) bind IIa
Cleavage of factor XII variant by activated thrombin
F8 variant is not cleaved by thrombin
Activated thrombin (factor IIa) cleaves F2R (PAR1), activating it
Secreted NS1 binds 10xCbxE-F2(44-622)
factor V -> factor Va intermediate + factor V activation peptide (thrombin catalyst)
factor Va intermediate -> factor Va