Any feedback?
Literature summary extracted from
- The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology (2015), Matrix Biol., 44-46C, 46-53.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.14 | additional information | proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity | Bos taurus | |
| 3.4.24.14 | additional information | proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity | Homo sapiens | |
| 3.4.24.14 | additional information | proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity | Mus musculus | |
| 3.4.24.14 | additional information | proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity | Rattus norvegicus | |
| 3.4.24.14 | additional information | proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity | Sus scrofa | |
| 3.4.24.14 | additional information | proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity | Ovis aries |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.24.14 | gene ADAMTS14, alternative splicing is possible | Bos taurus |
| 3.4.24.14 | gene ADAMTS14, alternative splicing is possible | Homo sapiens |
| 3.4.24.14 | gene ADAMTS2, alternative splicing is possible | Bos taurus |
| 3.4.24.14 | gene ADAMTS2, sequence comparisons | Canis lupus familiaris |
| 3.4.24.14 | gene ADAMTS2, sequence comparisons, alternative splicing is possible | Gallus gallus |
| 3.4.24.14 | gene ADAMTS2, sequence comparisons, alternative splicing is possible | Homo sapiens |
| 3.4.24.14 | gene ADAMTS2, sequence comparisons, alternative splicing is possible | Mus musculus |
| 3.4.24.14 | gene ADAMTS2, sequence comparisons, alternative splicing is possible | Rattus norvegicus |
| 3.4.24.14 | gene ADAMTS2, sequence comparisons, alternative splicing is possible | Sus scrofa |
| 3.4.24.14 | gene ADAMTS2, sequence comparisons, alternative splicing is possible | Ovis aries |
| 3.4.24.14 | gene ADAMTS3 | Bos taurus |
| 3.4.24.14 | gene ADAMTS3 | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.24.14 | additional information | in vivo, the formation of tumors in nude mice by HEK cells is strongly reduced when they overexpress ADAMTS2, an observation that is correlated to a reduced intratumoral vascularization but that can also involve direct anti-tumor effects | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.14 | papilin | - |
Bos taurus | |
| 3.4.24.14 | papilin | - |
Canis lupus familiaris | |
| 3.4.24.14 | papilin | - |
Gallus gallus | |
| 3.4.24.14 | papilin | - |
Homo sapiens | |
| 3.4.24.14 | papilin | - |
Mus musculus | |
| 3.4.24.14 | papilin | - |
Ovis aries | |
| 3.4.24.14 | papilin | - |
Rattus norvegicus | |
| 3.4.24.14 | papilin | - |
Sus scrofa | |
| 3.4.24.14 | TIMP3 | - |
Bos taurus | |
| 3.4.24.14 | TIMP3 | - |
Canis lupus familiaris | |
| 3.4.24.14 | TIMP3 | - |
Gallus gallus | |
| 3.4.24.14 | TIMP3 | - |
Homo sapiens | |
| 3.4.24.14 | TIMP3 | - |
Mus musculus | |
| 3.4.24.14 | TIMP3 | - |
Ovis aries | |
| 3.4.24.14 | TIMP3 | - |
Rattus norvegicus | |
| 3.4.24.14 | TIMP3 | - |
Sus scrofa |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.24.14 | extracellular | collagen and extracellular matrix | Gallus gallus | - |
- |
| 3.4.24.14 | extracellular | collagen and extracellular matrix | Bos taurus | - |
- |
| 3.4.24.14 | extracellular | collagen and extracellular matrix | Canis lupus familiaris | - |
- |
| 3.4.24.14 | extracellular | collagen and extracellular matrix | Homo sapiens | - |
- |
| 3.4.24.14 | extracellular | collagen and extracellular matrix | Mus musculus | - |
- |
| 3.4.24.14 | extracellular | collagen and extracellular matrix | Rattus norvegicus | - |
- |
| 3.4.24.14 | extracellular | collagen and extracellular matrix | Sus scrofa | - |
- |
| 3.4.24.14 | extracellular | collagen and extracellular matrix | Ovis aries | - |
- |
| 3.4.24.14 | additional information | identification of nucleolin as a potential endothelial cell surface receptor for ADAMTS2 | Homo sapiens | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.14 | Ca2+ | required | Gallus gallus |  |
| 3.4.24.14 | Ca2+ | required | Bos taurus | |
| 3.4.24.14 | Ca2+ | required | Canis lupus familiaris | |
| 3.4.24.14 | Ca2+ | required | Homo sapiens | |
| 3.4.24.14 | Ca2+ | required | Mus musculus | |
| 3.4.24.14 | Ca2+ | required | Rattus norvegicus | |
| 3.4.24.14 | Ca2+ | required | Sus scrofa | |
| 3.4.24.14 | Ca2+ | required | Ovis aries | |
| 3.4.24.14 | Zn2+ | required | Gallus gallus | |
| 3.4.24.14 | Zn2+ | required | Bos taurus | |
| 3.4.24.14 | Zn2+ | required | Canis lupus familiaris | |
| 3.4.24.14 | Zn2+ | required | Homo sapiens | |
| 3.4.24.14 | Zn2+ | required | Mus musculus | |
| 3.4.24.14 | Zn2+ | required | Rattus norvegicus | |
| 3.4.24.14 | Zn2+ | required | Sus scrofa | |
| 3.4.24.14 | Zn2+ | required | Ovis aries | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.14 | additional information | Bos taurus | ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site | ? | - |
? | |
| 3.4.24.14 | additional information | Homo sapiens | ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site | ? | - |
? | |
| 3.4.24.14 | additional information | Homo sapiens | ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3 | ? | - |
? | |
| 3.4.24.14 | additional information | Bos taurus | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively | ? | - |
? | |
| 3.4.24.14 | additional information | Gallus gallus | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The chicken enzyme ADAMTS2 cleaves at sites 148NFAP-/-QMSY155 in chain alpha1(I), as well as at 74NFAA-/-QYDP81 in chains alpha2(I) | ? | - |
? | |
| 3.4.24.14 | additional information | Canis lupus familiaris | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The dog enzyme ADAMTS2 cleaves at sites 154NFAP-/-QMSY161 in chain alpha1(I), and at 147FSP-/-QYDS154 in chain alpha1(III), as well as at 76NFAA-/-QYDG83 in chains alpha2(I) | ? | - |
? | |
| 3.4.24.14 | additional information | Homo sapiens | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The human enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), at 178NFAA-/-QMAG185 in chain alpha1(II), and at 150NYSP-/-QYDS157 in chain alpha1(III), as well as at 76NFAA-/-QYDG83 in chains alpha2(I), respectively | ? | - |
? | |
| 3.4.24.14 | additional information | Mus musculus | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The murine enzyme ADAMTS2 cleaves at sites 148NFAS-/-QMSY155 in chain alpha1(I), at 178NFAA-/-QMAG185 in chain alpha1(II), and at 151NYSP-/-QFDS158 in chain alpha1(III), as well as at 81NFAA-/-QYSD89 in chains alpha2(I), respectively | ? | - |
? | |
| 3.4.24.14 | additional information | Rattus norvegicus | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The rat enzyme ADAMTS2 cleaves at sites 148NFAS-/-QMSY155 in chain alpha1(I), at 110NFAA-/-QMAG117 in chain alpha1(II), and at 15NYSP-/-QFDS158 in chain alpha1(III), as well as at 81NFAA-/-QYSD89 in chains alpha2(I), respectively | ? | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | Gallus gallus | - |
collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | Bos taurus | - |
collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | Canis lupus familiaris | - |
collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | Homo sapiens | - |
collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | Mus musculus | - |
collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | Rattus norvegicus | - |
collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | Sus scrofa | - |
collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | Ovis aries | - |
collagen + collagen N-propeptide | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.14 | Bos taurus | E1BC50 | gene ADAMTS3; gene ADAMTS3 | - |
| 3.4.24.14 | Bos taurus | E1BFV4 | gene ADAMTS14; gene ADAMTS14 | - |
| 3.4.24.14 | Bos taurus | P79331 | gene ADAMTS2; gene ADAMTS2 | - |
| 3.4.24.14 | Canis lupus familiaris | E2R8G2 | gene ADAMTS2; gene ADAMTS2 | - |
| 3.4.24.14 | Gallus gallus | - |
gene ADAMTS2; gene ADAMTS2 | - |
| 3.4.24.14 | Homo sapiens | O15072 | gene ADAMTS3; gene ADAMTS3 | - |
| 3.4.24.14 | Homo sapiens | O95450 | gene ADAMTS2; gene ADAMTS2 | - |
| 3.4.24.14 | Homo sapiens | Q8WXS8 | gene ADAMTS14; gene ADAMTS14 | - |
| 3.4.24.14 | Mus musculus | Q8C9W3 | gene ADAMTS2; gene ADAMTS2 | - |
| 3.4.24.14 | Ovis aries | W5P0Z2 | gene ADAMTS2; gene ADAMTS2 | - |
| 3.4.24.14 | Rattus norvegicus | D3ZTE7 | gene ADAMTS2; gene ADAMTS2 | - |
| 3.4.24.14 | Sus scrofa | I3LAK9 | gene ADAMTS2; gene ADAMTS2 | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.24.14 | proteolytic modification | ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain | Bos taurus |
| 3.4.24.14 | proteolytic modification | ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain | Homo sapiens |
| 3.4.24.14 | proteolytic modification | ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain | Mus musculus |
| 3.4.24.14 | proteolytic modification | ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain | Rattus norvegicus |
| 3.4.24.14 | proteolytic modification | ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain | Sus scrofa |
| 3.4.24.14 | proteolytic modification | ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain | Ovis aries |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.24.14 | blood vessel | - |
Homo sapiens | - |
| 3.4.24.14 | cartilage | - |
Bos taurus | - |
| 3.4.24.14 | endothelial cell | enzyme expression | Homo sapiens | - |
| 3.4.24.14 | macrophage | enzyme expression | Homo sapiens | - |
| 3.4.24.14 | macrophage | enzyme expression, overexpression by macrophages and peripheral blood monocytes stimulated by glucocorticoids | Homo sapiens | - |
| 3.4.24.14 | monocyte | overexpression by macrophages and peripheral blood monocytes stimulated by glucocorticoids | Homo sapiens | - |
| 3.4.24.14 | additional information | ADAMTS14 is usually co-expressed with ADAMTS2, although at a lower level, suggesting potential functional redundancy | Bos taurus | - |
| 3.4.24.14 | additional information | ADAMTS2 and ADAMTS3, but not ADAMTS14, are more abundant in the culprit plaques from patients presenting with acute myocardial infarction versus stable angina | Homo sapiens | - |
| 3.4.24.14 | additional information | ADAMTS3 is mainly expressed in cartilage, where it colocalizes with type II procollagen, and in the nervous system | Bos taurus | - |
| 3.4.24.14 | nervous system | - |
Bos taurus | - |
| 3.4.24.14 | skin | - |
Gallus gallus | - |
| 3.4.24.14 | skin | - |
Bos taurus | - |
| 3.4.24.14 | skin | - |
Canis lupus familiaris | - |
| 3.4.24.14 | skin | - |
Homo sapiens | - |
| 3.4.24.14 | skin | - |
Mus musculus | - |
| 3.4.24.14 | skin | - |
Rattus norvegicus | - |
| 3.4.24.14 | skin | - |
Sus scrofa | - |
| 3.4.24.14 | skin | - |
Ovis aries | - |
| 3.4.24.14 | skin | high expression of ADAMTS2 is detected in all type I collagen-rich tissues from fetal calf such as skin, bones, tendons and aorta, which supports its importance for type I collagen maturation | Bos taurus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.14 | additional information | ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site | Bos taurus | ? | - |
? | |
| 3.4.24.14 | additional information | ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site | Homo sapiens | ? | - |
? | |
| 3.4.24.14 | additional information | ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3 | Homo sapiens | ? | - |
? | |
| 3.4.24.14 | additional information | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively | Bos taurus | ? | - |
? | |
| 3.4.24.14 | additional information | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The chicken enzyme ADAMTS2 cleaves at sites 148NFAP-/-QMSY155 in chain alpha1(I), as well as at 74NFAA-/-QYDP81 in chains alpha2(I) | Gallus gallus | ? | - |
? | |
| 3.4.24.14 | additional information | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The dog enzyme ADAMTS2 cleaves at sites 154NFAP-/-QMSY161 in chain alpha1(I), and at 147FSP-/-QYDS154 in chain alpha1(III), as well as at 76NFAA-/-QYDG83 in chains alpha2(I) | Canis lupus familiaris | ? | - |
? | |
| 3.4.24.14 | additional information | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The human enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), at 178NFAA-/-QMAG185 in chain alpha1(II), and at 150NYSP-/-QYDS157 in chain alpha1(III), as well as at 76NFAA-/-QYDG83 in chains alpha2(I), respectively | Homo sapiens | ? | - |
? | |
| 3.4.24.14 | additional information | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The murine enzyme ADAMTS2 cleaves at sites 148NFAS-/-QMSY155 in chain alpha1(I), at 178NFAA-/-QMAG185 in chain alpha1(II), and at 151NYSP-/-QFDS158 in chain alpha1(III), as well as at 81NFAA-/-QYSD89 in chains alpha2(I), respectively | Mus musculus | ? | - |
? | |
| 3.4.24.14 | additional information | sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The rat enzyme ADAMTS2 cleaves at sites 148NFAS-/-QMSY155 in chain alpha1(I), at 110NFAA-/-QMAG117 in chain alpha1(II), and at 15NYSP-/-QFDS158 in chain alpha1(III), as well as at 81NFAA-/-QYSD89 in chains alpha2(I), respectively | Rattus norvegicus | ? | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | - |
Gallus gallus | collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | - |
Bos taurus | collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | - |
Canis lupus familiaris | collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | - |
Homo sapiens | collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | - |
Mus musculus | collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | - |
Rattus norvegicus | collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | - |
Sus scrofa | collagen + collagen N-propeptide | - |
? | |
| 3.4.24.14 | pro-collagen + H2O | - |
Ovis aries | collagen + collagen N-propeptide | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.14 | ADAMTS14 | - |
Bos taurus |
| 3.4.24.14 | ADAMTS14 | - |
Homo sapiens |
| 3.4.24.14 | ADAMTS2 | - |
Gallus gallus |
| 3.4.24.14 | ADAMTS2 | - |
Bos taurus |
| 3.4.24.14 | ADAMTS2 | - |
Canis lupus familiaris |
| 3.4.24.14 | ADAMTS2 | - |
Homo sapiens |
| 3.4.24.14 | ADAMTS2 | - |
Mus musculus |
| 3.4.24.14 | ADAMTS2 | - |
Rattus norvegicus |
| 3.4.24.14 | ADAMTS2 | - |
Sus scrofa |
| 3.4.24.14 | ADAMTS2 | - |
Ovis aries |
| 3.4.24.14 | ADAMTS3 | - |
Bos taurus |
| 3.4.24.14 | ADAMTS3 | - |
Homo sapiens |
| 3.4.24.14 | procollagen N-proteinase | - |
Gallus gallus |
| 3.4.24.14 | procollagen N-proteinase | - |
Bos taurus |
| 3.4.24.14 | procollagen N-proteinase | - |
Canis lupus familiaris |
| 3.4.24.14 | procollagen N-proteinase | - |
Homo sapiens |
| 3.4.24.14 | procollagen N-proteinase | - |
Mus musculus |
| 3.4.24.14 | procollagen N-proteinase | - |
Rattus norvegicus |
| 3.4.24.14 | procollagen N-proteinase | - |
Sus scrofa |
| 3.4.24.14 | procollagen N-proteinase | - |
Ovis aries |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.14 | additional information | - |
the enzyme requires a neutral to slightly basic pH for activity | Gallus gallus |
| 3.4.24.14 | additional information | - |
the enzyme requires a neutral to slightly basic pH for activity | Bos taurus |
| 3.4.24.14 | additional information | - |
the enzyme requires a neutral to slightly basic pH for activity | Canis lupus familiaris |
| 3.4.24.14 | additional information | - |
the enzyme requires a neutral to slightly basic pH for activity | Homo sapiens |
| 3.4.24.14 | additional information | - |
the enzyme requires a neutral to slightly basic pH for activity | Mus musculus |
| 3.4.24.14 | additional information | - |
the enzyme requires a neutral to slightly basic pH for activity | Rattus norvegicus |
| 3.4.24.14 | additional information | - |
the enzyme requires a neutral to slightly basic pH for activity | Sus scrofa |
| 3.4.24.14 | additional information | - |
the enzyme requires a neutral to slightly basic pH for activity | Ovis aries |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 3.4.24.14 | Homo sapiens | enzyme exxpression is upregulated by glucocorticoids | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.24.14 | evolution | the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch | Bos taurus |
| 3.4.24.14 | evolution | the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch | Homo sapiens |
| 3.4.24.14 | evolution | the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch | Mus musculus |
| 3.4.24.14 | evolution | the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch | Gallus gallus |
| 3.4.24.14 | evolution | the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch | Rattus norvegicus |
| 3.4.24.14 | evolution | the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch | Sus scrofa |
| 3.4.24.14 | evolution | the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch | Ovis aries |
| 3.4.24.14 | malfunction | Adamts2-deficient mice phenotype, overview. The absence of ADAMTS2 activity leads to the dermatosparactic type of Ehlers-Danlos syndrome, also previously known as EDS-type VIIC | Mus musculus |
| 3.4.24.14 | malfunction | the absence of ADAMTS2 activity leads to the dermatosparactic type of Ehlers-Danlos syndrome, also previously known as EDS-type VIIC | Homo sapiens |
| 3.4.24.14 | additional information | the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components | Gallus gallus |
| 3.4.24.14 | additional information | the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components | Bos taurus |
| 3.4.24.14 | additional information | the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components | Canis lupus familiaris |
| 3.4.24.14 | additional information | the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components | Homo sapiens |
| 3.4.24.14 | additional information | the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components | Mus musculus |
| 3.4.24.14 | additional information | the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components | Rattus norvegicus |
| 3.4.24.14 | additional information | the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components | Sus scrofa |
| 3.4.24.14 | additional information | the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components | Ovis aries |
| 3.4.24.14 | physiological function | ADAMTS14, which is coexpressed with ADAMTS2 in different connective tissues, might be responsible for this partial alternative aminoprocollagen endopeptidase activity | Bos taurus |
| 3.4.24.14 | physiological function | ADAMTS14, which is coexpressed with ADAMTS2 in different connective tissues, might be responsible for this partial alternative aminoprocollagen endopeptidase activity. Adamts14 gene is potentially implicated in knee osteoarthritis in women. The Adamts14 gene seem to be linked to the predisposition to multiple sclerosis | Homo sapiens |
| 3.4.24.14 | physiological function | ADAMTS3 promotes the release of a proteolytically cleaved active form of VEGF-C, a process that increases VEGF-R3 signaling | Bos taurus |
| 3.4.24.14 | physiological function | ADAMTS3 promotes the release of a proteolytically cleaved active form of VEGF-C, a process that increases VEGF-R3 signaling | Homo sapiens |
| 3.4.24.14 | physiological function | enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview | Canis lupus familiaris |
| 3.4.24.14 | physiological function | enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor | Gallus gallus |
| 3.4.24.14 | physiological function | enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity | Bos taurus |
| 3.4.24.14 | physiological function | enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity | Mus musculus |
| 3.4.24.14 | physiological function | enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity | Rattus norvegicus |
| 3.4.24.14 | physiological function | enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity | Sus scrofa |
| 3.4.24.14 | physiological function | enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity | Ovis aries |
| 3.4.24.14 | physiological function | enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity. In vivo, the formation of tumors in nude mice by HEK cells is strongly reduced when they overexpress ADAMTS2, an observation that is correlated to a reduced intratumoral vascularization but that can also involve direct anti-tumor effects | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
