| UniProt ID | MMP2_HUMAN | |
|---|---|---|
| UniProt AC | P08253 | |
| Protein Name | 72 kDa type IV collagenase | |
| Gene Name | MMP2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 660 | |
| Subcellular Localization | Isoform 1: Secreted, extracellular space, extracellular matrix. Membrane. Nucleus. Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of c | |
| Protein Description | 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 GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.; PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.; Isoform 2: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.. | |
| Protein Sequence | MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 11 | Phosphorylation | LMARGALTGPLRALC HHHCCCCCHHHHHHH | 35.90 | - | |
| 32 | Phosphorylation | SHAAAAPSPIIKFPG HHHHHCCCCCEECCC | 24.81 | 24719451 | |
| 160 | Phosphorylation | DVTPLRFSRIHDGEA CCCCEECEEECCCCC | 24.72 | 22817900 | |
| 199 | Phosphorylation | AHAFAPGTGVGGDSH EEEECCCCCCCCCCC | 27.86 | 22199227 | |
| 205 | Phosphorylation | GTGVGGDSHFDDDEL CCCCCCCCCCCCCCC | 29.36 | 22199227 | |
| 246 | Phosphorylation | FNGKEYNSCTDTGRS ECCEECCCCCCCCCC | 19.93 | - | |
| 250 | Phosphorylation | EYNSCTDTGRSDGFL ECCCCCCCCCCCCEE | 19.15 | 22817900 | |
| 261 | Phosphorylation | DGFLWCSTTYNFEKD CCEEEEEEEEEECCC | 30.11 | - | |
| 360 | Phosphorylation | FTFLGNKYESCTSAG EEECCCCCCCCCCCC | 19.64 | - | |
| 362 | Phosphorylation | FLGNKYESCTSAGRS ECCCCCCCCCCCCCC | 21.43 | - | |
| 364 | Phosphorylation | GNKYESCTSAGRSDG CCCCCCCCCCCCCCC | 30.78 | 20166139 | |
| 365 | Phosphorylation | NKYESCTSAGRSDGK CCCCCCCCCCCCCCC | 32.81 | 22817900 | |
| 369 | Phosphorylation | SCTSAGRSDGKMWCA CCCCCCCCCCCEEEE | 50.20 | - | |
| 377 | Phosphorylation | DGKMWCATTANYDDD CCCEEEEEECCCCCC | 24.25 | 22817900 | |
| 378 | Phosphorylation | GKMWCATTANYDDDR CCEEEEEECCCCCCC | 8.38 | 22817900 | |
| 460 | O-linked_Glycosylation | LGTGPTPTLGPVTPE CCCCCCCCCCCCCHH | 46.99 | OGP | |
| 552 | Phosphorylation | ASTLERGYPKPLTSL CCCCCCCCCCCCHHC | 17.82 | 27174698 | |
| 557 | Phosphorylation | RGYPKPLTSLGLPPD CCCCCCCHHCCCCCC | 30.36 | 27174698 | |
| 558 | Phosphorylation | GYPKPLTSLGLPPDV CCCCCCHHCCCCCCH | 28.29 | 27174698 | |
| 573 | N-linked_Glycosylation | QRVDAAFNWSKNKKT HHEEEEECCCCCCCE | 37.07 | UniProtKB CARBOHYD | |
| 575 | Phosphorylation | VDAAFNWSKNKKTYI EEEEECCCCCCCEEE | 27.70 | 27732954 | |
| 636 | Phosphorylation | SYFFKGAYYLKLENQ EEEEEEEEEEEECCC | 20.28 | 25072903 | |
| 637 | Phosphorylation | YFFKGAYYLKLENQS EEEEEEEEEEECCCC | 9.23 | 25072903 | |
| 642 | N-linked_Glycosylation | AYYLKLENQSLKSVK EEEEEECCCCCCEEE | 47.37 | UniProtKB CARBOHYD | |
| 644 | Phosphorylation | YLKLENQSLKSVKFG EEEECCCCCCEEEEC | 49.71 | 25072903 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 160 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 250 | T | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 365 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 377 | T | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 378 | T | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MMP2_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 MMP2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00025 | Penile cancer | |||||
| H00028 | Choriocarcinoma | |||||
| H00472 | Torg-Winchester syndrome | |||||
| OMIM Disease | ||||||
| 259600 | Multicentric osteolysis, nodulosis, and arthropathy (MONA) | |||||
| Kegg Drug | ||||||
| D03061 | Batimastat (USAN/INN) | |||||
| D03793 | Ilomastat (USAN/INN) | |||||
| D03797 | Prinomastat (USAN/INN) | |||||
| D03802 | Tanomastat (USAN/INN) | |||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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