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MMP10 MMP10 MMP3 MMP3 FOS FOS MMP1 MMP1 MMP15 MMP15 JUN JUN MMP14 MMP14 TIMP1 TIMP1 IGF2 IGF2 VEGFA VEGFA TGFB1 TGFB1 A2M A2M ACTN2 ACTN2 TGFB2 TGFB2 VEGFC VEGFC SERPINA1 SERPINA1 APP APP VWF VWF LEFTY2 LEFTY2 PROS1 PROS1 EGF EGF F5 F5 TMSB4X TMSB4X HRG HRG FN1 FN1 ACTN1 ACTN1
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.
Node Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
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
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
TIMP1TIMP metallopeptidase inhibitor 1; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16. Does not act on MMP-14 (207 aa)
MMP15matrix metallopeptidase 15 (membrane-inserted); Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A (669 aa)
TGFB1transforming growth factor, beta 1; Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (390 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)
VWFvon Willebrand factor; Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma (2813 aa)
EGFepidermal growth factor; EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (1207 aa)
MMP10matrix metallopeptidase 10 (stromelysin 2); Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase (476 aa)
VEGFCvascular endothelial growth factor C; Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors (420 aa)
APPamyloid beta (A4) precursor protein (770 aa)
MMP3matrix metallopeptidase 3 (stromelysin 1, progelatinase); Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase (477 aa)
FOSFBJ murine osteosarcoma viral oncogene homolog; Nuclear phosphoprotein which forms a tight but non- covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD- binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell p [...] (380 aa)
MMP14matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 (582 aa)
MMP1matrix metallopeptidase 1 (interstitial collagenase); Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat’s mediated neurotoxicity (469 aa)
A2Malpha-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 co [...] (1474 aa)
FN1fibronectin 1 (2477 aa)
SERPINA1serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 (418 aa)
ACTN2actinin, alpha 2; F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (894 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)
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)
JUNjun proto-oncogene; Transcription factor that recognizes and binds to the enhancer heptamer motif 5’-TGA[CG]TCA-3’. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (331 aa)
VEGFAvascular endothelial growth factor A (412 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)
PROS1protein S (alpha); 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 (676 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)
IGF2insulin-like growth factor 2 (somatomedin A) (236 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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