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Protein Page:
MMP10 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
MMP10 Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase. Belongs to the peptidase M10A family. Note: This description may include information from UniProtKB.
Protein type: Secreted; Secreted, signal peptide; EC 3.4.24.22; Protease; Extracellular matrix
Cellular Component: extracellular space; proteinaceous extracellular matrix; extracellular region
Molecular Function: zinc ion binding; metalloendopeptidase activity; calcium ion binding
Biological Process: collagen catabolic process; extracellular matrix disassembly; extracellular matrix organization and biogenesis; proteolysis; regulation of cell migration
Reference #:  P09238 (UniProtKB)
Alt. Names/Synonyms: matrix metallopeptidase 10 (stromelysin 2); matrix metalloprotease 10; matrix metalloproteinase 10 (stromelysin 2); Matrix metalloproteinase-10; MMP-10; MMP10; SL-2; STMY2; stromelysin 2; Stromelysin-2; transin 2; Transin-2
Gene Symbols: MMP10
Molecular weight: 54,151 Da
Basal Isoelectric point: 5.49  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis  |  GPCRs Signaling to MAPK/Erk
Select Structure to View Below

MMP10
Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 1 K54-a DVKQFRRkDSNLIVK
0 1 - under review  
0 1 K62-a DSNLIVKkIQGMQKF
0 2 S281-p VPTKSVPsGsEMPAK
0 1 S283-p TKSVPsGsEMPAKCD
  mouse

 
K55 EKQIFKRKDSSPVVK
S30-p AVTQGHPsMDLAQQY
K63 DSSPVVKKIQEMQKF
- under review  
- under review  
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