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Tbio
COL9A2
Collagen alpha-2(IX) chain

Protein Summary
Description
Structural component of hyaline cartilage and vitreous of the eye. This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. This chain is unusual in that, unlike the other two type IX alpha chains, it contains a covalently attached glycosaminoglycan side chain. Mutations in this gene are associated with multiple epiphyseal dysplasia. [provided by RefSeq, Jul 2008]
Uniprot Accession IDs
Gene Name
Ensembl ID
  • ENST00000372748
  • ENSP00000361834
  • ENSG00000049089

Symbol
  • MED
  • EDM2
  • STL5
  • DJ39G22.4
Illumination Graph
Knowledge Table
Most Knowledge About
Knowledge Value (0 to 1 scale)
disease perturbation
0.87
PubMedID
0.74
tissue sample
0.67
cell line
0.65
disease
0.61


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: 41.02   (req: < 5)
Gene RIFs: 24   (req: <= 3)
Antibodies: 15   (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: 41.02   (req: >= 5)
Gene RIFs: 24   (req: > 3)
Antibodies: 15   (req: > 50)

- OR - satisfy the following criterion:

Gene Ontology Terms: 4
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
Protein Data Bank (4)
1 – 4 of 4
PDB Structure Id
Ligand
Method
Resolution (Å)
M.W. (kDa)
Pub Year
Title
PDB Structure Id
M.W.
Resolution
Pub Year
Pathways (41)
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 16
Data Source
Name
Explore in Pharos
Explore in Source
Reactome
Assembly of collagen fibrils and other multimeric structures
Reactome
Axon guidance
Reactome
Collagen biosynthesis and modifying enzymes
Reactome
Collagen chain trimerization
Reactome
Collagen degradation
Name
Explore in Pharos
Explore in Source
Assembly of collagen fibrils and other multimeric structures
Axon guidance
Collagen biosynthesis and modifying enzymes
Collagen chain trimerization
Collagen degradation
Protein-Protein Interactions (132)
1 – 10 of 132
COL9A1
Tbio
Novelty: 0.02281721
Score: 0.999
Data Source: Reactome,STRINGDB
COL9A3
Tbio
Novelty: 0.03642087
Score: 0.997
Data Source: Reactome,STRINGDB
COL2A1
Tbio
Novelty: 0.00119609
Score: 0.966
Data Source: STRINGDB
COL11A1
Tbio
Novelty: 0.00813892
Score: 0.936
Data Source: STRINGDB
COL11A2
Tbio
Novelty: 0.01141248
Score: 0.935
Data Source: STRINGDB
P3H1
Tbio
Family: Enzyme
Novelty: 0.02610289
Score: 0.928
Data Source: STRINGDB
MMP3
Tchem
Novelty: 0.00050371
Score: 0.928
Data Source: STRINGDB
MMP13
Tchem
Family: Enzyme
Novelty: 0.00068218
Score: 0.928
Data Source: STRINGDB
BGN
Tbio
Novelty: 0.00181025
Score: 0.925
Data Source: STRINGDB
COL10A1
Tbio
Novelty: 0.00697565
Score: 0.924
Data Source: STRINGDB
Publication Statistics
PubMed Score  41.02

PubMed score by year
PubTator Score  49.82

PubTator score by year
Amino Acid Sequence
Residue Counts
Sequence
MAAATASPRSLLVLLQVVVLALAQIRGPPGERGPPGPPGPPGVPGSDGIDGDNGPPGKAGPPGPKGEPGK
1-70
AGPDGPDGKPGIDGLTGAKGEPGPMGIPGVKGQPGLPGPPGLPGPGFAGPPGPPGPVGLPGEIGIRGPKG
70-140
DPGPDGPSGPPGPPGKPGRPGTIQGLEGSADFLCPTNCPPGMKGPPGLQGVKGHAGKRGILGDPGHQGKP
140-210
GPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGETGPHGYKGMVGAIGATGPPGEEGPRGPPGRAGEKG
210-280
DEGSPGIRGPQGITGPKGATGPPGINGKDGTPGTPGMKGSAGQAGQPGSPGHQGLAGVPGQPGTKGGPGD
280-350
QGEPGPQGLPGFSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQGPPGIPGPQ
350-420
GLPGVKGDKGSPGKTGPRGKVGDPGVAGLPGEKGEKGESGEPGPKGQQGVRGEPGYPGPSGDAGAPGVQG
420-490
YPGPPGPRGLAGNRGVPGQPGRQGVEGRDATDQHIVDVALKMLQEQLAEVAVSAKREALGAVGMMGPPGP
490-560
PGPPGYPGKQGPHGHPGPRGVPGIVGAVGQIGNTGPKGKRGEKGDPGEVGRGHPGMPGPPGIPGLPGRPG
560-630
QAINGKDGDRGSPGAPGEAGRPGLPGPVGLPGFCEPAACLGASAYASARLTEPGSIKGP
630-689
MAAATASPRSLLVLLQVVVLALAQIRGPPGERGPPGPPGPPGVPGSDGIDGDNGPPGKAGPPGPKGEPGKAGPDGPDGKPGIDGLTGAKGEPGPMGIPGVKGQPGLPGPPGLPGPGFAGPPGPPGPVGLPGEIGIRGPKGDPGPDGPSGPPGPPGKPGRPGTIQGLEGSADFLCPTNCPPGMKGPPGLQGVKGHAGKRGILGDPGHQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGETGPHGYKGMVGAIGATGPPGEEGPRGPPGRAGEKGDEGSPGIRGPQGITGPKGATGPPGINGKDGTPGTPGMKGSAGQAGQPGSPGHQGLAGVPGQPGTKGGPGDQGEPGPQGLPGFSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQGPPGIPGPQGLPGVKGDKGSPGKTGPRGKVGDPGVAGLPGEKGEKGESGEPGPKGQQGVRGEPGYPGPSGDAGAPGVQGYPGPPGPRGLAGNRGVPGQPGRQGVEGRDATDQHIVDVALKMLQEQLAEVAVSAKREALGAVGMMGPPGPPGPPGYPGKQGPHGHPGPRGVPGIVGAVGQIGNTGPKGKRGEKGDPGEVGRGHPGMPGPPGIPGLPGRPGQAINGKDGDRGSPGAPGEAGRPGLPGPVGLPGFCEPAACLGASAYASARLTEPGSIKGP