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Tbio
MMP20
Matrix metalloproteinase-20

Protein Summary
Description
Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site. 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 protein encoded by this gene degrades amelogenin, the major protein component of dental enamel matrix, and thus thought to play a role in tooth enamel formation. A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has bee ...more
Uniprot Accession IDs
Gene Name
Ensembl ID
  • ENST00000260228
  • ENSP00000260228
  • ENSG00000137674

Symbol
  • AI2A2
  • MMP-20
Illumination Graph
Knowledge Table
Most Knowledge About
Knowledge Value (0 to 1 scale)
protein domain
1
cell line
0.61
gene perturbation
0.6
molecular function
0.56
kinase perturbation
0.54


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: 102.24   (req: < 5)
Gene RIFs: 28   (req: <= 3)
Antibodies: 263   (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: 102.24   (req: >= 5)
Gene RIFs: 28   (req: > 3)
Antibodies: 263   (req: > 50)

- OR - satisfy the following criterion:

Gene Ontology Terms: 9
Tchem

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

Active Ligand: 0
Tclin

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

Active Drug: 0
GWAS Traits (4)
GWAS Trait
EFO ID
Study Count
SNP Count
Beta Count
Odds Ratio
Evidence (Mean Rank Score)
Provenance
matrix metalloproteinase 1 measurement
1
1
1
65.6
1
1
0
2.8
61.8
urinary metabolite measurement
1
1
1
15.9
1
1
1
15.9
GWAS Trait
EFO ID
Beta Count
Odds Ratio
Evidence (Mean Rank Score)
Provenance
matrix metalloproteinase 1 measurement
1
65.6
0
2.8
61.8
urinary metabolite measurement
1
15.9
1
15.9
Orthologs (12)
1 – 5 of 12
Species
Name
Source ID
Gene ID
OMA
EggNOG
Inparanoid
Chimp
matrix metallopeptidase 20
VGNC:1096
740407
Macaque
matrix metallopeptidase 20
703188
Mouse
MGI:1353466
30800
Rat
RGD:1308730
300341
Dog
matrix metallopeptidase 20
VGNC:43281
611829
Species
Name
OMA
EggNOG
Inparanoid
Chimp
matrix metallopeptidase 20
Macaque
matrix metallopeptidase 20
Mouse
Rat
Dog
matrix metallopeptidase 20
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-O60882-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 (8)
Assembly of collagen fibrils and other multimeric structures (R-HSA-2022090)

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

Items per page:
1 – 5 of 5
Data Source
Name
Explore in Pharos
Explore in Source
Reactome
Assembly of collagen fibrils and other multimeric structures
Reactome
Collagen degradation
Reactome
Collagen formation
Reactome
Degradation of the extracellular matrix
Reactome
Extracellular matrix organization
Name
Explore in Pharos
Explore in Source
Assembly of collagen fibrils and other multimeric structures
Collagen degradation
Collagen formation
Degradation of the extracellular matrix
Extracellular matrix organization
Protein-Protein Interactions (66)
1 – 10 of 66
LAMB3
Tbio
Novelty: 0.00717673
Score: 0.945
Data Source: STRINGDB
LAMA3
Tbio
Novelty: 0.00733792
Score: 0.932
Data Source: STRINGDB
AMELX
Tbio
Novelty: 0.00063284
Score: 0.921
Data Source: STRINGDB
ENAM
Tbio
Novelty: 0.00593293
Score: 0.921
Data Source: STRINGDB
LAMC2
Tbio
Novelty: 0.00695692
Score: 0.914
Data Source: STRINGDB
COL18A1
Tbio
Novelty: 0.00074602
Score: 0.903
Data Source: STRINGDB
COL15A1
Tbio
Novelty: 0.04078006
Score: 0.902
Data Source: STRINGDB
WDR72
Tbio
Novelty: 0.07576018
Score: 0.902
Data Source: STRINGDB
A2M
Tbio
Novelty: 0.00070446
Score: 0.901
Data Source: STRINGDB
AMBN
Tbio
Novelty: 0.00354946
Score: 0.897
Data Source: STRINGDB
Publication Statistics
PubMed Score  102.24

PubMed score by year
PubTator Score  92.15

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