| + |
MMP14 | down-regulates quantity by destabilization 
cleavage
|
F12 |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263610 |
Gly376 |
SMTRVVGgLVALRGA |
in vitro |
|
| pmid |
sentence |
| 10930399 |
The data presented in this study show for the first time the degradation of Factor XII of the blood clotting system by matrix metalloproteinases. MMP-12, MMP-13, and MMP-14 cleave at Gly376Leu377|However, no activity of Factor XII can be observed after MMPinduced cleavage. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MMP14 | down-regulates quantity by destabilization
cleavage
|
FGG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263618 |
Ile105 |
ESSKPNMiDAATLKS |
in vitro |
|
| pmid |
sentence |
| 10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263617 |
Leu92 |
QLIKAIQlTYNPDES |
in vitro |
|
| pmid |
sentence |
| 10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263616 |
Tyr27 |
LSSTCVAyVATRDNC |
in vitro |
|
| pmid |
sentence |
| 10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
MMP14 | down-regulates quantity by destabilization
cleavage
|
FGA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263619 |
Leu105 |
NNKDSHSlTTNIMEI |
in vitro |
|
| pmid |
sentence |
| 10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263620 |
Leu433 |
REYHTEKlVTSKGDK |
in vitro |
|
| pmid |
sentence |
| 10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263621 |
Phe117 |
MEILRGDfSSANNRD |
in vitro |
|
| pmid |
sentence |
| 10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
SRC |
phosphorylation
|
MMP14 |
0.448 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154006 |
Tyr573 |
GTPRRLLyCQRSLLD |
Homo sapiens |
|
| pmid |
sentence |
| 17389600 |
We show that mt1-mmp is phosphorylated on the unique tyrosine residue located within this cytoplasmic sequence (tyr(573)) and that this phosphorylation requires the kinase src. accordingly, overexpression of a nonphosphorylable mt1-mmp mutant (y573f) blocked sphingosine-1-phosphate-induced migration of human umbilical vein endothelial cells and ht-1080 (human fibrosarcoma) cells and failed to stimulate migration of cells lacking the enzyme (bovine aortic endothelial cells). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP14 | down-regulates quantity by destabilization
cleavage
|
ADAM9 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260301 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22632802 |
Here we show that MT1-MMP forms a complex with FGFR2 and ADAM9 in osteoblasts and proteolytically inactivates ADAM9|Western blotting using antibodies against ectodomain of ADAM9 detected a fragment (around 26 kDa) of ADAM9 in the conditioned culture medium from cells cotransfected with wild-type MT1-MMP, but not in that with catalytic activity-dead MT1-MMP (Figure 6A, top). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP14 | up-regulates 
|
Adipogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255909 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28709001 |
MMP14 Promotes Adipogenesis Downstream of or in Parallel to TIMP3 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
TIMP3 | down-regulates activity
binding
|
MMP14 |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255908 |
|
|
Mus musculus |
Muscle Stem Cell |
| pmid |
sentence |
| 28709001 |
FAP cilia regulated the expression of TIMP3, a secreted metalloproteinase inhibitor, that inhibited MMP14 to block adipogenesis. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MMP14 | up-regulates
|
ECM_disassembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272359 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
FHIT | down-regulates quantity by repression 
transcriptional regulation
|
MMP14 |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159876 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18077326 |
In binding to the beta-catenin c-terminal domain, fhit represses transcription of target genes such as cyclin d1, axin2, mmp-14, and survivin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP14 | down-regulates
|
ECM |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272382 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
3.0
MMP14
- 
- 