3.4.21.69: Protein C (activated)
This is an abbreviated version!
For detailed information about Protein C (activated), go to the full flat file.
Word Map on EC 3.4.21.69
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3.4.21.69
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thrombosis
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venous
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leiden
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sepsis
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endothelial
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antithrombin
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thromboembolism
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thrombophilia
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clot
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thrombomodulin
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platelet
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procoagulant
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heparin
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arterial
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vein
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bleeding
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plasminogen
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hypercoagulable
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thromboplastin
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lupus
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fibrinogen
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fibrinolysis
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hemostatic
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viiia
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epcr
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intravascular
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contraceptive
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antiphospholipid
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antithrombotic
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prothrombotic
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fibrin
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k-dependent
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anticardiolipin
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d-dimers
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coagulopathy
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embolism
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prothrombinase
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amidolytic
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thrombin-antithrombin
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haemostasis
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par1
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profibrinolytic
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pharmacology
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goal-directed
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diagnostics
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drug development
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gamma-carboxyglutamic
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deep-vein
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time-based
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tafi
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hypofibrinolysis
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thromboprophylaxis
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medicine
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protac
- 3.4.21.69
- thrombosis
- venous
- leiden
- sepsis
- endothelial
- antithrombin
- thromboembolism
- thrombophilia
- clot
- thrombomodulin
- platelet
-
procoagulant
- heparin
- arterial
- vein
-
bleeding
- plasminogen
-
hypercoagulable
- thromboplastin
-
lupus
- fibrinogen
-
fibrinolysis
-
hemostatic
- viiia
- epcr
-
intravascular
-
contraceptive
-
antiphospholipid
-
antithrombotic
-
prothrombotic
- fibrin
-
k-dependent
-
anticardiolipin
-
d-dimers
- coagulopathy
- embolism
- prothrombinase
-
amidolytic
-
thrombin-antithrombin
-
haemostasis
- par1
-
profibrinolytic
- pharmacology
-
goal-directed
- diagnostics
- drug development
-
gamma-carboxyglutamic
-
deep-vein
-
time-based
- tafi
-
hypofibrinolysis
-
thromboprophylaxis
- medicine
- protac
Reaction
degradation of blood coagulation factors Va and VIIIa =
Synonyms
Activated blood coagulation factor XIV, Activated protein C, anticoagulant activated protein C, anticoagulant protein C/protein S system, anticoagulant serine protease-activated protein C, anticoagulant-activated protein C, APC, Autoprothrombin II-A, Autoprothrombin IIA, Blood coagulation factor XIV, Blood-coagulation factor XIV, activated, Blood-coagulation factor XIVa, ghrelin endopeptidase, GSAPC, hAPC, PROC, Protein Ca, rhAPC
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.69 - Protein C (activated)
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glycoprotein
proteolytic modification
side-chain modification
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beta-hydroxylation of Asp71, and carboxylation of nine glutamic acid residues in the N-terminus
glycoprotein
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bovine protein C contains 14% carbohydrate, approximately 15 residues of hexose, 12 residues of hexosamine and 9 residues of sialic acid distributed in 3 carbohydrate chains, human protein C contains 23% carbohydrate, approximately 14 residues of galactose, 21 residues of mannose, 23 residues of glucosamine and 12 residues of sialic acid
glycoprotein
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bovine protein C contains 14% carbohydrate, approximately 15 residues of hexose, 12 residues of hexosamine and 9 residues of sialic acid distributed in 3 carbohydrate chains, human protein C contains 23% carbohydrate, approximately 14 residues of galactose, 21 residues of mannose, 23 residues of glucosamine and 12 residues of sialic acid
glycoprotein
N-linked glycan attachment site that is occupied by a complex sialyated glycan chain in about 70% of plasma protein C (termed protein C-alpha), but not in the remaining protein C pool, which is termed protein C-beta
glycoprotein
the enzyme is in naturally occurring APC-beta plasma glycoform, N-glycosidase PNGase F treatment of APC excises all N-linked glycans leading to a fourfold increased PAR1 proteolysis compared to untreated APC
proteolytic modification
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protein C zymogen activation by thrombin on the endothelial cell surface, the double mutant thrombin W215A/E217A is also active in protein C activation and produces APC with high barrier protective activity
proteolytic modification
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proteolytic cleavage and activation by thrombin at Arg169 removing the activation peptide, thrombomodulin and endothelial cell protein C receptor PAR-1 are required for efficient enzyme activation
proteolytic modification
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the protein C zymogen is activate through cleavage by thrombin in a Ca2+-dependent manner, thrombin acts in complex with the required thrombomodulin, the reaction is is markedly stimulated by endothelial protein C receptor
proteolytic modification
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protein C circulates in plasma as an inactive zymogen and is activated by thrombin bound to the endothelium associated transmembrane receptor thrombomodulin, that removes the 158-169 activation peptide of protein C via cleavage at R169, thus generating activated protein C, APC
proteolytic modification
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thrombin bound to the endothelial cell surface by thrombomodulin cleaves protein C into its active form
proteolytic modification
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inactive plasma zymogen protein C is activated by proteolysis through the thrombin-thrmbomdulin complex on the vascular endothelial cell surface
proteolytic modification
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modulation of protein C activation by histones, platelet factor 4, and heparinoids, overview. The 2-O, 3-O desulfated heparin affects activated protein C generation in the presence of histones and platelet factor 4, histones alone enhance protein C activation, while the enhancement is inhibited by platelet factor 4 addition
proteolytic modification
the physiologic mechanism for protein C activation involves proteolysis at Arg169in EPCR-bound protein C by thrombomodulin-bound thrombin. The half-life of endogenous circulating APC in humans is 15 to 0 minutes and is dominantly determined by its irreversible reaction with the plasma serine protease inhibitors, alpha1-antitrypsin, protein C inhibitor, and alpha2-macroglobulin
proteolytic modification
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proteolytic cleavage and activation by thrombin removing the activation peptide, thrombomodulin and endothelial cell protein C receptor PAR-1 are required for efficient enzyme activation
proteolytic modification
the physiologic mechanism for protein C activation involves proteolysis at Arg169 in EPCR-bound protein C by thrombomodulin-bound thrombin
proteolytic modification
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in thrombotic stress, the protein C zymogen is converted to its active form by thrombin in complex with endothelial surface thrombomodulin