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PF4V1 PF4V1 THBD THBD SERPINA1 SERPINA1 SERPINE1 SERPINE1 VEGFB VEGFB PF4 PF4 ACTN4 ACTN4 F2 F2 SERPING1 SERPING1 F5 F5 CLU CLU VEGFA VEGFA TGFB2 TGFB2 FN1 FN1 FGA FGA LEFTY2 LEFTY2 HRG HRG PPBP PPBP ACTN1 ACTN1 SERPINF2 SERPINF2 FGG FGG TMSB4X TMSB4X ALB ALB CFD CFD SERPINC1 SERPINC1
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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small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
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colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
Edges:
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
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gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
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Your Input:
SERPINE1serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 1; Serine protease inhibitor. This inhibitor acts as ’bait’ for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis (402 aa)
PF4V1platelet factor 4 variant 1; Inhibitor of angiogenesis. Inhibitor of endothelial cell chemotaxis (in vitro) (104 aa)
HRGhistidine-rich glycoprotein; Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell [...] (525 aa)
ACTN4actinin, alpha 4; F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (911 aa)
SERPING1serpin peptidase inhibitor, clade G (C1 inhibitor), member 1 (500 aa)
ALBalbumin (609 aa)
PPBPpro-platelet basic protein (chemokine (C-X-C motif) ligand 7); LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet al [...] (128 aa)
PF4platelet factor 4; Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form (101 aa)
FGAfibrinogen alpha chain; Fibrinogen has a double function- yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation (866 aa)
F2coagulation factor II (thrombin); Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (622 aa)
VEGFBvascular endothelial growth factor B; Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis (207 aa)
CLUclusterin; Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress- induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosom [...] (449 aa)
SERPINF2serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2; Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin (491 aa)
CFDcomplement factor D (adipsin); Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway (253 aa)
FGGfibrinogen gamma chain (453 aa)
FN1fibronectin 1 (2477 aa)
SERPINA1serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 (418 aa)
LEFTY2left-right determination factor 2; Required for left-right (L-R) asymmetry determination of organ systems in mammals. May play a role in endometrial bleeding (366 aa)
TGFB2transforming growth factor, beta 2; TGF-beta 2 has suppressive effects on interleukin-2 dependent T-cell growth (442 aa)
SERPINC1serpin peptidase inhibitor, clade C (antithrombin), member 1 (464 aa)
F5coagulation factor V (proaccelerin, labile factor); 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)
VEGFAvascular endothelial growth factor A (412 aa)
THBDthrombomodulin; Thrombomodulin is a specific endothelial cell receptor that forms a 1-1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated (575 aa)
TMSB4Xthymosin beta 4, X-linked; Plays an important role in the organization of the cytoskeleton (By similarity). Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (44 aa)
ACTN1actinin, alpha 1; F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (914 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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