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  • 11.0 [archived version]
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MMP17 MMP17 MMP25 MMP25 MMP16 MMP16 MMP2 MMP2 MMP15 MMP15 MMP14 MMP14 RECK RECK TIMP2 TIMP2 MMP9 MMP9 MMP24 MMP24 MMP8 MMP8
"TIMP2" - Metalloproteinase inhibitor 2 in Homo sapiens
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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TIMP2Metalloproteinase 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; Belongs to the protease inhibitor I35 (TIMP) family (220 aa)    
Predicted Functional Partners:
MMP2
72 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)
     
  0.999
MMP14
Matrix 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)
     
  0.997
MMP9
Matrix metalloproteinase-9; 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; M10 matrix metallopeptidases (707 aa)
     
  0.992
MMP8
Neutrophil collagenase; Can degrade fibrillar type I, II, and III collagens; Belongs to the peptidase M10A family (467 aa)
     
  0.985
MMP16
Matrix metalloproteinase-16; 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; Belongs to the peptidase M10A family (607 aa)
       
  0.979
MMP15
Matrix metalloproteinase-15; Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A; Belongs to the peptidase M10A family (669 aa)
       
  0.978
RECK
Reversion-inducing cysteine-rich protein with Kazal motifs; Negatively regulates matrix metalloproteinase-9 (MMP-9) by suppressing MMP-9 secretion and by direct inhibition of its enzymatic activity. RECK down-regulation by oncogenic signals may facilitate tumor invasion and metastasis. Appears to also regulate MMP-2 and MT1-MMP, which are involved in cancer progression (971 aa)
     
 
  0.975
MMP17
Matrix metalloproteinase-17; 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. Cleaves pro-TNF-alpha at the ’74-Ala-|-Gln-75’ site. 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)
     
  0.973
MMP25
Matrix metalloproteinase-25; May activate progelatinase A; M10 matrix metallopeptidases (562 aa)
       
  0.971
MMP24
Matrix metalloproteinase-24; Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate th [...] (645 aa)
       
  0.957
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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