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EFEMP1 EFEMP1 ENSG00000258852 ENSG00000258852 MMP27 MMP27 MMP26 MMP26 MMP3 MMP3 KDR KDR MMP25 MMP25 VTN VTN TP53 TP53 ADAM17 ADAM17 TIMP3 TIMP3 MMP24 MMP24 MMP28 MMP28 MMP9 MMP9 ADAMTS5 ADAMTS5 MMP2 MMP2 MMP13 MMP13 MMP17 MMP17 MMP14 MMP14 MMP7 MMP7 MMP16 MMP16 MMP15 MMP15 MMP8 MMP8 MMP21 MMP21 MMP11 MMP11 MMP19 MMP19
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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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small protein node
small nodes:
protein of unknown 3D structure
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large nodes:
some 3D structure is known or predicted
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colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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from curated databases
experiment edge
experimentally determined
Predicted Interactions
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fusion edge
gene fusions
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gene co-occurrence
Others
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textmining
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co-expression
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Your Input:
MMP11matrix metallopeptidase 11 (stromelysin 3); May play an important role in the progression of epithelial malignancies (488 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)
VTNvitronectin; Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway (478 aa)
MMP8matrix metallopeptidase 8 (neutrophil collagenase); Can degrade fibrillar type I, II, and III collagens (467 aa)
MMP24matrix metallopeptidase 24 (membrane-inserted); Activates progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity) (645 aa)
MMP28matrix metallopeptidase 28; Can degrade casein. Could play a role in tissues homeostasis and repair (130 aa)
MMP7matrix metallopeptidase 7 (matrilysin, uterine); Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase (267 aa)
MMP27matrix metallopeptidase 27; Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens (By similarity) (513 aa)
MMP13matrix metallopeptidase 13 (collagenase 3); Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process (471 aa)
KDRkinase insert domain receptor (a type III receptor tyrosine kinase); Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an importan [...] (1356 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)
TP53tumor protein p53; Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (By similarity) (393 aa)
ADAMTS5ADAM metallopeptidase with thrombospondin type 1 motif, 5; 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. May play a role in proteolytic processing mostly during the peri-implantation period (930 aa)
MMP16matrix metallopeptidase 16 (membrane-inserted); Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells (607 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)
MMP26matrix metallopeptidase 26; May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B (261 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)
ADAM17ADAM metallopeptidase domain 17; Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Also involved in the activation of Notch pathway (By similarity) (824 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)
MMP25matrix metallopeptidase 25; May activate progelatinase A (562 aa)
EFEMP1EGF containing fibulin-like extracellular matrix protein 1; Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth (493 aa)
MMP17matrix metallopeptidase 17 (membrane-inserted); Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin (603 aa)
MMP21matrix metallopeptidase 21; May have an important and specific function in tumor progression and embryogenesis. Cleaves alpha-1-antitrypsin (569 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)
ENSG00000258852Uncharacterized protein (148 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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