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MMP11 MMP11 MMP14 MMP14 LAMC2 LAMC2 TIMP3 TIMP3 TIMP2 TIMP2 NID1 NID1 LAMB3 LAMB3 TIMP1 TIMP1 MMP15 MMP15 LAMA3 LAMA3 MMP2 MMP2 MMP1 MMP1 MMP19 MMP19 MMP7 MMP7 ACAN ACAN MMP10 MMP10 MMP9 MMP9 ELANE ELANE MMP8 MMP8 BCAN BCAN COL14A1 COL14A1 COL16A1 COL16A1 COL9A2 COL9A2 COL9A1 COL9A1 COL9A3 COL9A3 COL12A1 COL12A1
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:
MMP11matrix metallopeptidase 11 (stromelysin 3); May play an important role in the progression of epithelial malignancies (488 aa)
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)
MMP2matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa 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 s [...] (660 aa)
MMP15matrix metallopeptidase 15 (membrane-inserted); Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A (669 aa)
MMP8matrix metallopeptidase 8 (neutrophil collagenase); Can degrade fibrillar type I, II, and III collagens (467 aa)
MMP7matrix metallopeptidase 7 (matrilysin, uterine); Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase (267 aa)
TIMP2TIMP metallopeptidase inhibitor 2; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19 (220 aa)
ELANEelastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (267 aa)
LAMC2laminin, gamma 2; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells (1193 aa)
NID1nidogen 1; Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell- extracellular matrix interactions (1247 aa)
TIMP3TIMP metallopeptidase inhibitor 3; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15 (211 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)
COL14A1collagen, type XIV, alpha 1 (1796 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)
MMP19matrix metallopeptidase 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 (508 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)
LAMA3laminin, alpha 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (3333 aa)
COL12A1collagen, type XII, alpha 1; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix (By similarity) (3063 aa)
BCANbrevican; May play a role in the terminally differentiating and the adult nervous system during postnatal development. Could stabilize interactions between hyaluronan (HA) and brain proteoglycans (911 aa)
COL9A3collagen, type IX, alpha 3; Structural component of hyaline cartilage and vitreous of the eye (684 aa)
LAMB3laminin, beta 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (1172 aa)
COL9A1collagen, type IX, alpha 1 (921 aa)
MMP9matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (707 aa)
COL9A2collagen, type IX, alpha 2; Structural component of hyaline cartilage and vitreous of the eye (689 aa)
COL16A1collagen, type XVI, alpha 1; Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology (1604 aa)
ACANaggrecan; 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 (2530 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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