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APOH APOH ASPH ASPH SERPINA10 SERPINA10 F3 F3 GAD2 GAD2 F7 F7 SERPINC1 SERPINC1 TRMT112 TRMT112 F10 F10 SERPINA5 SERPINA5 F5 F5 SERPINB8 SERPINB8 TFPI TFPI F8 F8 SERPINB6 SERPINB6 GGCX GGCX ENSG00000259680 ENSG00000259680 PROS1 PROS1 PLAT PLAT PLG PLG PSMD4 PSMD4 SHFM1 SHFM1 F2R F2R PCOLCE PCOLCE F2RL2 F2RL2 F2RL3 F2RL3
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
APOHBeta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells; Apolipoproteins (345 aa)
PLATTissue-type plasminogen activator; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration (562 aa)
PCOLCEProcollagen C-endopeptidase enhancer 1; Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity (449 aa)
TFPITissue factor pathway inhibitor; Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma (304 aa)
GGCXVitamin K-dependent gamma-carboxylase; Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide (758 aa)
F2RL3Proteinase-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 (385 aa)
SERPINA10Protein Z-dependent protease inhibitor; Inhibits activity of the coagulation protease factor Xa in the presence of PROZ, calcium and phospholipids. Also inhibits factor XIa in the absence of cofactors; Belongs to the serpin family (444 aa)
F2RL2Proteinase-activated receptor 3; Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis; F2R receptors (374 aa)
PLGPlasminogen; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated b [...] (810 aa)
F2RProteinase-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 (425 aa)
SERPINA5Plasma serine protease inhibitor; Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coa [...] (406 aa)
F3Tissue factor; Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF-VIIa] complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade (295 aa)
F8Coagulation factor VIII; Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa; Belongs to the multicopper oxidase family (2351 aa)
SERPINC1Antithrombin-III; Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin; Serpin peptidase inhibitors (464 aa)
F5Coagulation 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 (2224 aa)
PSMD426S 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- [...] (377 aa)
F10Coagulation factor X; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Gla domain containing (488 aa)
F7Coagulation factor VII; Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium; Gla domain containing (466 aa)
GAD2Glutamate decarboxylase 2; Catalyzes the production of GABA (585 aa)
ASPHAspartyl/asparaginyl beta-hydroxylase; Isoform 1- specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins; Belongs to the aspartyl/asparaginyl beta-hydroxylase family (758 aa)
PROS1Vitamin K-dependent protein S; Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis; Gla domain containing (676 aa)
SERPINB8Serpin B8; Has an important role in epithelial desmosome-mediated cell-cell adhesion; Belongs to the serpin family. Ov-serpin subfamily (374 aa)
TRMT112Multifunctional methyltransferase subunit TRM112-like protein; Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA. The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on ’Gln-185’, using S-adenosyl L- methionine as methyl donor. The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5- methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. Involved in the pre-rRNA processing steps leading t [...] (125 aa)
ENSG00000259680Uncharacterized protein (116 aa)
SHFM1Putative protein SEM1, isoform 2; Split hand/foot malformation (ectrodactyly) type 1 (118 aa)
SERPINB6Serpin B6; May be involved in the regulation of serine proteinases present in the brain or extravasated from the blood (By similarity). Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an important role in the inner ear in the protection against leakage of lysosomal content during stress and loss of this protection results in cell death and sensorineural hearing loss; Deafness associated genes (395 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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