EC Number   |
Localization |
GeneOntology No. |
Reference |
|---|
   3.4.24.24 | cell surface |
besides MT-MMPs, which efficiently bind proMMP-2 to induce its activation, a limited number of cell-surface molecules have been shown to contribute to enhance proteolytic activity at the migrating front of invasive cells by clustering active MMP-2 at the cell membrane. Among them the heat shock protein HSP90a expressed at the surface of tumor cells promotes MMP-2 activity and tumor invasion by binding to the Hpx-like domain of MMP-2. The alphanybeta3 integrin is first identified as a binding site for the C-terminal Hpx-like domain of MMP-2 in studies investigating in vivo and in vitro interactions between angiogenic blood vessels and melanoma cells |
GO:0009986 AmiGO QuickGO |
752865 |
| 3.4.24.24 | cell surface |
complex formed by MT1-MMP, TIMP-2 |
GO:0009986 AmiGO QuickGO |
683846 |
| 3.4.24.24 | cytoplasm |
- |
GO:0005737 AmiGO QuickGO |
717633 |
| 3.4.24.24 | cytosol |
- |
GO:0005829 AmiGO QuickGO |
752440, 752865 |
| 3.4.24.24 | cytosol |
main localization in invertebral disc, immunohistochemic analysis, overview |
GO:0005829 AmiGO QuickGO |
683804 |
| 3.4.24.24 | endoplasmic reticulum |
- |
GO:0005783 AmiGO QuickGO |
752865, 753613 |
| 3.4.24.24 | extracellular |
- |
- |
-, 31086, 31087, 31088, 31094, 31096, 31098, 31099, 31100, 31107, 683314, 683579, 683710, 733634, 752440, 753209, 754619 |
| 3.4.24.24 | extracellular |
extracellular matrix |
- |
683507 |
| 3.4.24.24 | extracellular |
MMP-2 is secreted |
- |
684054 |
| 3.4.24.24 | extracellular |
the enzyme is secreted |
- |
734254, 754641, 755324 |
