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Tchem
MMP16
Matrix metalloproteinase-16

Protein Summary
Description
Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The encoded protein activates MMP2 by cleavage. This gene was once referred to as MT-MMP2, but was renamed as MT-MMP3 or MMP16. [provided by RefSeq, Oct 2010]
Uniprot Accession IDs
Gene Name
Ensembl ID
  • ENST00000286614
  • ENSP00000286614
  • ENSG00000156103

Symbol
  • C8orf57
  • MMPX2
  • MMP-X2
  • C8orf57
  • MT-MMP2
  • MT-MMP3
  • MT3-MMP
Illumination Graph
Knowledge Table
Most Knowledge About
Knowledge Value (0 to 1 scale)
protein domain
1
PubMedID
0.89
disease
0.78
cell type or tissue
0.76
kinase perturbation
0.76


Related Tools
Target Illumination GWAS Analytics (TIGA)
TIGA scores and ranks GWAS discovered associations according to the quantity and quality of the evidence supporting the association.
GENEVA
GENEVA (GENe Expression Variance Analysis) allows you to identify RNA-sequencing datasets from the Gene Expression Omnibus (GEO) that contain conditions modulating a gene or a gene signature.
GlyGen
GlyGen is a data integration and dissemination project for carbohydrate and glycoconjugate related data.
ARCHS4
ARCHS4 provides access to gene-function predictions based on RNA-seq co-expression, and gene expression levels across cell and tissues.
IDG Development Level Summary
Tdark

These are targets about which virtually nothing is known. They do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:

Pubmed score: 95.52   (req: < 5)
Gene RIFs: 26   (req: <= 3)
Antibodies: 399   (req: <= 50)
Tbio

These targets do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:

Pubmed score: 95.52   (req: >= 5)
Gene RIFs: 26   (req: > 3)
Antibodies: 399   (req: > 50)

- OR - satisfy the following criterion:

Gene Ontology Terms: 13
Tchem

Target has at least one ChEMBL compound with an activity cutoff of < 30 nM - AND - satisfies the preceding conditions

Active Ligands: 31
Tclin

Target has at least one approved drug - AND - satisfies the preceding conditions

Active Drug: 0
GWAS Traits (3)
GWAS Trait
EFO ID
Study Count
SNP Count
Beta Count
Odds Ratio
Evidence (Mean Rank Score)
Provenance
5
3
0
1.1
83.3
heel bone mineral density
1
1
1
72
1
1
0
1.1
7.4
GWAS Trait
EFO ID
Beta Count
Odds Ratio
Evidence (Mean Rank Score)
Provenance
0
1.1
83.3
heel bone mineral density
1
72
0
1.1
7.4
Orthologs (13)
1 – 5 of 13
Species
Name
Source ID
Gene ID
OMA
EggNOG
Inparanoid
Chimp
matrix metallopeptidase 16
VGNC:6570
736322
Macaque
matrix metallopeptidase 16
695120
Mouse
MGI:1276107
17389
Rat
RGD:620199
65205
Dog
matrix metallopeptidase 16
VGNC:43278
487036
Species
Name
OMA
EggNOG
Inparanoid
Chimp
matrix metallopeptidase 16
Macaque
matrix metallopeptidase 16
Mouse
Rat
Dog
matrix metallopeptidase 16
Protein Structure (1 Structure, 1 AlphaFold Model)
RepresentationColor Scheme

Click on a row in the table to change the structure displayed.
More information can be found at RCSB PDB

AF-P51512-F1-model_v1

AlphaFold Structures Developed by DeepMind and EMBL-EBI

1 – 1 of 1
PDB Structure Id
Ligand
Method
Resolution (Å)
Residues
Fraction of Total Protein
Pub Year
Title
PDB Structure Id
Fraction of Total Protein
Resolution
Pub Year
Pathways (7)
Activation of Matrix Metalloproteinases (R-HSA-1592389)

Click on a row in the table to change the structure displayed.

Items per page:
1 – 3 of 3
Data Source
Name
Explore in Pharos
Explore in Source
Reactome
Activation of Matrix Metalloproteinases
Reactome
Degradation of the extracellular matrix
Reactome
Extracellular matrix organization
Name
Explore in Pharos
Explore in Source
Activation of Matrix Metalloproteinases
Degradation of the extracellular matrix
Extracellular matrix organization
Protein-Protein Interactions (53)
1 – 10 of 53
TIMP2
Tbio
Family: Enzyme
Novelty: 0.00064016
Score: 0.979
Data Source: STRINGDB
FURIN
Tchem
Family: Enzyme
Novelty: 0.00055079
Score: 0.942
Data Source: Reactome,STRINGDB
MMP2
Tchem
Family: Enzyme
Novelty: 0.00012762
Score: 0.925
Data Source: STRINGDB
MMP13
Tchem
Family: Enzyme
Novelty: 0.00057893
Score: 0.91
Data Source: STRINGDB
MMP14
Tchem
Family: Enzyme
Novelty: 0.00083836
Score: 0.903
Data Source: STRINGDB
SPOCK3
Tbio
Novelty: 0.11871451
Score: 0.759
Data Source: STRINGDB
SPOCK2
Tbio
Novelty: 0.05125638
Score: 0.716
Data Source: STRINGDB
TIMP3
Tbio
Family: Enzyme
Novelty: 0.00134742
Score: 0.692
Data Source: STRINGDB
TIMP1
Tbio
Family: Enzyme
Novelty: 0.00020986
Score: 0.676
Data Source: STRINGDB
SPOCK1
Tbio
Novelty: 0.01256778
Score: 0.671
Data Source: STRINGDB
Publication Statistics
PubMed Score  95.52

PubMed score by year
PubTator Score  71.23

PubTator score by year
Amino Acid Sequence
Residue Counts
Protein Sequence
ProtVista Viewer
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