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- Table of Contents
Facts about A disintegrin and metalloproteinase with thrombospondin motifs 2.
May also play a role in growth that is independent of its role in collagen biosynthesis. .
| Human | |
|---|---|
| Gene Name: | ADAMTS2 |
| Uniprot: | O95450 |
| Entrez: | 9509 |

| Belongs to: |
|---|
| No superfamily |

A disintegrin and metalloproteinase with thrombospondin motifs 2; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondintype 1 motif, 2; ADAM metallopeptidase with thrombospondin type 1 motif, 2; ADAM-TS 2; ADAMTS-2; ADAM-TS2EC 3.4.24.14; ADAMTS-3; EC 3.4.24; NPIDKFZp686F12218; PC I-NP; PCI-NP; PCINPhPCPNI; PCPNI; PNPI; Procollagen I N-proteinase; Procollagen I/II amino propeptide-processing enzyme; Procollagen N-endopeptidase
Mass (kDA):
134.755 kDA

| Human | |
|---|---|
| Location: | 5q35.3 |
| Sequence: | 5; NC_000005.10 (179110853..179345461, complement) |
Expressed at high level in skin, bone, tendon and aorta and at low levels in thymus and brain.
Secreted, extracellular space, extracellular matrix.





PMID: 10417273 by Colige A., et al. Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene.
PMID: 31152061 by Rosell-Garcia T., et al. Differential cleavage of lysyl oxidase by the metalloproteinases BMP1 and ADAMTS2/14 regulates collagen binding through a tyrosine sulfate domain.