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TNFAIP6 TNFAIP6 MMP20 MMP20 MMP8 MMP8 TNC TNC ADAMTS4 ADAMTS4 TENM2 TENM2 ADAMTS1 ADAMTS1 MMP19 MMP19 MMP14 MMP14 ADAMTS5 ADAMTS5 MMP3 MMP3 MMP1 MMP1 ACAN ACAN TNN TNN HAPLN1 HAPLN1 CTSB CTSB FBLN2 FBLN2 MMP2 MMP2 LUM LUM FBLN1 FBLN1 TNR TNR FCN2 FCN2 TNXB TNXB FCN1 FCN1 PCOLCE PCOLCE WIF1 WIF1
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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
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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
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textmining
co-expression
protein homology
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MMP272 kDa type IV collagenase; Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3b [...] (660 aa)
PCOLCEProcollagen C-endopeptidase enhancer 1; Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity (449 aa)
MMP8Neutrophil collagenase; Can degrade fibrillar type I, II, and III collagens; Belongs to the peptidase M10A family (467 aa)
TNNTenascin-N; Extracellular matrix protein that seems to be a ligand for ITGA8-ITGB1, ITGAV-ITGB1 and ITGA4-ITGB1 (By similarity). Involved in neurite outgrowth and cell migration in hippocampal explants (By similarity). During endochondral bone formation, inhibits proliferation and differentiation of proteoblasts mediated by canonical WNT signaling (By similarity). In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells. Expressed in most mammary tumors, may facilitate tumorigenesis by supporting the migratory behavior of breast cancer cells; Belon [...] (1299 aa)
TNFAIP6Tumor necrosis factor-inducible gene 6 protein; Possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis (277 aa)
MMP20Matrix metalloproteinase-20; Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix- aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the ’360-Asn-|-Phe-361’ site; M10 matrix metallopeptidases (483 aa)
TNCTenascin; Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells; Belongs to the tenascin family (2201 aa)
LUMLumican; Small leucine rich repeat proteoglycans; Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily (338 aa)
HAPLN1Hyaluronan and proteoglycan link protein 1; Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix; V-set domain containing (354 aa)
ADAMTS1A disintegrin and metalloproteinase with thrombospondin motifs 1; Cleaves aggrecan, a cartilage proteoglycan, at the ’1938-Glu-|-Leu-1939’ site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture; ADAM metallopeptidases with thrombospondin type 1 motif (967 aa)
ADAMTS5A disintegrin and metalloproteinase with thrombospondin motifs 5; Metalloproteinase that plays an important role in connective tissue organization, development, inflammation, arthritis, and cell migration. ADAMTS5 is an extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including aggrecan, versican, brevican and neurocan. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle de [...] (930 aa)
WIF1Wnt inhibitory factor 1; Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation (379 aa)
FCN2Ficolin-2; May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc- binding lectin. Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an opsonic effect via the collagen region; Fibrinogen C domain containing (313 aa)
MMP3Stromelysin-1; Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase; Belongs to the peptidase M10A family (477 aa)
MMP14Matrix metalloproteinase-14; Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiog [...] (582 aa)
MMP19Matrix metalloproteinase-19; Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin; Belongs to the peptidase M10A family (508 aa)
MMP1Interstitial 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; Endogenous ligands (469 aa)
FBLN1Fibulin-1; Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a signi [...] (703 aa)
CTSBCathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (339 aa)
TNRTenascin-R; Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repuls [...] (1358 aa)
ADAMTS4A disintegrin and metalloproteinase with thrombospondin motifs 4; Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the ’392-Glu-|-Ala-393’ site; ADAM metallopeptidases with thrombospondin type 1 motif (837 aa)
FCN1Ficolin-1; Extracellular lectin functioning as a pattern- recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8. Binds preferentially to 9-O-acetylated 2-6- linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage (326 aa)
FBLN2Fibulin-2; Its binding to fibronectin and some other ligands is calcium dependent. May act as an adapter that mediates the interaction between FBN1 and ELN; Fibulins (1231 aa)
ACANAggrecan core protein; This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region; C-type lectin domain containing (2530 aa)
TNXBTenascin-X; Appears to mediate interactions between cells and the extracellular matrix. Substrate-adhesion molecule that appears to inhibit cell migration. Accelerates collagen fibril formation. May play a role in supporting the growth of epithelial tumors; Fibrinogen C domain containing (673 aa)
TENM2Teneurin-2; Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion (By similarity). May function as a cellular signal transducer (2774 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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