Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the c [...]

Chymotrypsin-like elastase family member 1; Acts upon elastin

Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the c [...]

Coagulation factor V; Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin

Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the c [...]

Beta-nerve growth factor; Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades through those receptor tyrosine kinase to regulate neuronal proliferation, differentiation and survival. Inhibits metalloproteinase dependent proteolysis of platelet glycoprotein VI; Neurotrophins

Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the c [...]

Alpha-1-antitrypsin; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin; Belongs to the serpin family

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily

Sarcoplasmic/endoplasmic reticulum calcium ATPase 3; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction; ATPases Ca2+ transporting

Sarcoplasmic/endoplasmic reticulum calcium ATPase 3; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction; ATPases Ca2+ transporting

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily

Chymotrypsin-like elastase family member 1; Acts upon elastin

Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the c [...]

Chymotrypsin-like elastase family member 1; Acts upon elastin

Elafin; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis; WAP four-disulfide core domain containing

Chymotrypsin-like elastase family member 1; Acts upon elastin

Alpha-1-antitrypsin; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin; Belongs to the serpin family

Uncharacterized protein

Beta-nerve growth factor; Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades through those receptor tyrosine kinase to regulate neuronal proliferation, differentiation and survival. Inhibits metalloproteinase dependent proteolysis of platelet glycoprotein VI; Neurotrophins

Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development; F2R receptors

Proteinase-activated receptor 3; Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis; F2R receptors

Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development; F2R receptors

Proteinase-activated receptor 4; Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation; Belongs to the G-protein coupled receptor 1 family

Proteinase-activated receptor 3; Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis; F2R receptors

Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development; F2R receptors

Proteinase-activated receptor 3; Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis; F2R receptors

Proteinase-activated receptor 4; Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation; Belongs to the G-protein coupled receptor 1 family

Proteinase-activated receptor 4; Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation; Belongs to the G-protein coupled receptor 1 family

Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development; F2R receptors

Proteinase-activated receptor 4; Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation; Belongs to the G-protein coupled receptor 1 family

Proteinase-activated receptor 3; Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis; F2R receptors

Coagulation factor V; Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin

Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the c [...]

Coagulation factor V; Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin

Apolipoprotein(a); Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330; Belongs to the peptidase S1 family. Plasminogen subfamily

Coagulation factor V; Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin

Alpha-1-antitrypsin; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin; Belongs to the serpin family

Transcriptional activator GLI3; Has a dual function as a transcriptional activator and a repressor of the sonic hedgehog (Shh) pathway, and plays a role in limb development. The full-length GLI3 form (GLI3FL) after phosphorylation and nuclear translocation, acts as an activator (GLI3A) while GLI3R, its C-terminally truncated form, acts as a repressor. A proper balance between the GLI3 activator and the repressor GLI3R, rather than the repressor gradient itself or the activator/repressor ratio gradient, specifies limb digit number and identity. In concert with TRPS1, plays a role in reg [...]

26S proteasome non-ATPase regulatory subunit 4; Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin- [...]