| + |
MMP3 | down-regulates quantity by destabilization 
cleavage
|
ACAN |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266986 |
Asn360 |
DFVDIPEnFFGVGGE |
Homo sapiens |
|
| pmid |
sentence |
| 9202061 |
Aggrecan Degradation in Human Cartilage Evidence for both Matrix Metalloproteinase and Aggrecanase Activity in Normal, Osteoarthritic, and Rheumatoid Joints|Stromelysin-1 (MMP-3), as well as other MMPs, cleave aggrecan in the interglobular domain between Asn341 and Phe342 to generate a G1 fragment with the COOH terminus VDIPEN341 (11–13). This fragment has been isolated and identified by NH2-terminal sequence analysis from human OA cartilage (11). A second proteolytic activity identified as “aggrecanase” also cleaves aggrecan in the interglobular domain, but between Glu373 and Ala374 (19–24), generating a G1 fragment with a COOH terminus of NITEGE374 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Cartilage |
| + |
MMP3 | down-regulates quantity by destabilization
cleavage
|
HAPLN1 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256330 |
His31 |
LDHDRAIhIQAENGP |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MMP3 | down-regulates quantity by destabilization
cleavage
|
DCN |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256353 |
Ser240 |
ISRVDAAsLKGLNNL |
in vitro |
|
| pmid |
sentence |
| 9148753 |
Degradation of decorin by matrix metalloproteinases. These data indicate proteolytic degradation of DCN by MMP-2, MMP-3 and MMP-7, and suggest the possibility that, under pathophysiological conditions, the digestion by the MMPs may induce tissue reactions mediated by TGF-beta1 released from DCN in the connective tissues. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MMP3 | down-regulates 
|
ECM |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272396 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
TCF20 | up-regulates quantity by expression 
transcriptional regulation
|
MMP3 |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266223 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 7760812 |
This result indicates that expression of SPBP is sufficient to transactivate a minimal promoter containing a single copy of the SPRE, as well as the full-length stromelysin promoter. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MMP3 | up-regulates
cleavage
|
HBEGF |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-83339 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 11043579 |
It was concluded that mmp-3 cleaves hb-egf at a specific site in the jm domain and that this enzyme might regulate the conversion of hb-egf from being a juxtacrine to a paracrine/autocrine growth factor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity 
|
MMP3 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251109 |
|
|
|
|
| pmid |
sentence |
| 23967200 |
C-Src-induced STAT3 activation regulates MMP3 levels |
|
| Publications: |
1 |
| + |
MMP3 | up-regulates activity
cleavage
|
SPP1 |
0.656 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253320 |
|
|
|
|
| pmid |
sentence |
| 25545242 |
In this study, we found a novel motif, LRSKSRSFQVSDEQY, in the C-terminal fragment of MMP-3/7-cleaved mouse OPN binds to α9β1 integrin. Importantly, this novel motif is involved in the development of anti-type II collagen antibody-induced arthritis (CAIA). This study provides the first in vitro and in vivo evidence that OPN cleavage by MMP-3/7 is an important regulatory mechanism for CAIA. |
|
| Publications: |
1 |
| + |
MMP3 | up-regulates
|
ECM_disassembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272373 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
ZMYND8 | down-regulates quantity by repression
transcriptional regulation
|
MMP3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262043 |
|
|
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 27477906 |
Our quantitative ChIP experiments confirmed that ZMYND8 and JARID1D were co-localized at Slug, CD44, VEGFA, and EGFR genes (Figures 4F–4I). Our ChIP results also showed that ZMYND8 repressed and occupied other JARID1D target genes, such as the matrix metalloproteinase 1 (MMP1) and MMP3, that we previously reported |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MMP3
- 
- 