| UniProt ID | MMP3_HUMAN | |
|---|---|---|
| UniProt AC | P08254 | |
| Protein Name | Stromelysin-1 | |
| Gene Name | MMP3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 477 | |
| Subcellular Localization | Secreted, extracellular space, extracellular matrix . | |
| Protein Description | Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.. | |
| Protein Sequence | MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 18 | Phosphorylation | CVAVCSAYPLDGAAR HHHHHHHCCCCCHHC | 6.50 | - | |
| 37 | Phosphorylation | SMNLVQKYLENYYDL HHHHHHHHHHHHHHH | 11.36 | 22817900 | |
| 41 | Phosphorylation | VQKYLENYYDLKKDV HHHHHHHHHHHHHHH | 6.75 | 22817900 | |
| 42 | Phosphorylation | QKYLENYYDLKKDVK HHHHHHHHHHHHHHH | 26.78 | 22817900 | |
| 57 | Phosphorylation | QFVRRKDSGPVVKKI HHHHHCCCCHHHHHH | 48.29 | 28348404 | |
| 81 | Phosphorylation | EVTGKLDSDTLEVMR EEECCCCCCHHHHHC | 42.82 | 22777824 | |
| 116 | Phosphorylation | WRKTHLTYRIVNYTP CCCCEEEEEEEECCC | 12.52 | - | |
| 120 | N-linked_Glycosylation | HLTYRIVNYTPDLPK EEEEEEEECCCCCCH | 32.37 | UniProtKB CARBOHYD | |
| 121 | Phosphorylation | LTYRIVNYTPDLPKD EEEEEEECCCCCCHH | 14.57 | - | |
| 127 | Ubiquitination | NYTPDLPKDAVDSAV ECCCCCCHHHHHHHH | 66.66 | 29967540 | |
| 277 | O-linked_Glycosylation | PETPLVPTEPVPPEP CCCCCCCCCCCCCCC | 45.50 | OGP | |
| 286 | O-linked_Glycosylation | PVPPEPGTPANCDPA CCCCCCCCCCCCCCC | 29.91 | OGP |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of MMP3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MMP3_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of MMP3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PGCB_HUMAN | BCAN | physical | 10986281 | |
| K319L_HUMAN | KIAA0319L | physical | 26186194 | |
| MMP10_HUMAN | MMP10 | physical | 26186194 | |
| CLUS_HUMAN | CLU | physical | 26186194 | |
| PTPRS_HUMAN | PTPRS | physical | 26186194 | |
| CLN5_HUMAN | CLN5 | physical | 26186194 | |
| HBD_HUMAN | HBD | physical | 26186194 | |
| NUCB1_HUMAN | NUCB1 | physical | 26186194 | |
| APOE_HUMAN | APOE | physical | 26186194 | |
| TIMP3_HUMAN | TIMP3 | physical | 26186194 | |
| MMP10_HUMAN | MMP10 | physical | 28514442 | |
| APOE_HUMAN | APOE | physical | 28514442 | |
| PTPRS_HUMAN | PTPRS | physical | 28514442 | |
| NUCB1_HUMAN | NUCB1 | physical | 28514442 | |
| TIMP3_HUMAN | TIMP3 | physical | 28514442 | |
| LTBP1_HUMAN | LTBP1 | physical | 28514442 | |
| K319L_HUMAN | KIAA0319L | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 614466 | Coronary heart disease 6 (CHDS6) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...