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Title: Adamts2  
Author: World Heritage Encyclopedia
Language: English
Subject: Procollagen peptidase, Ehlers–Danlos syndrome, EC 3.4.24, Chromosome 5 (human), ADAM2
Publisher: World Heritage Encyclopedia


ADAM metallopeptidase with thrombospondin type 1 motif, 2
External IDs IUPHAR: GeneCards:
EC number
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS2) also known as procollagen I N-proteinase (PC I-NP) is an enzyme[1] that in humans is encoded by the ADAMTS2 gene.[2][3]


  • Gene 1
  • Function 2
  • Clinical significance 3
  • See also 4
  • References 5
  • Further reading 6
  • External links 7


The ADAMTS2 gene is located on the long (q) arm of chromosome 5 at the end (terminus) of the arm, from base pair 178,473,473 to base pair 178,704,934.


ADAMTS2 is responsible for processing several types of procollagen proteins. Procollagens are the precursors of collagens, the proteins that add strength and support to many body tissues. Specifically, this enzyme clips a short chain of amino acids off one end of the procollagen. This clipping step is necessary for collagen molecules to function normally and assemble into fibrils outside cells.

Clinical significance

  • GeneCard
  • The MEROPS online database for peptidases and their inhibitors: M12.301

External links

  • Wang WM, Lee S, Steiglitz BM, Scott IC, Lebares CC, Allen ML, Brenner MC, Takahara K, Greenspan DS (May 2003). "Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase". J. Biol. Chem. 278 (21): 19549–57.  
  • Reardon W, Winter RM, Smith LT; et al. (1995). "The natural history of human dermatosparaxis (Ehlers-Danlos syndrome type VIIC)". Clin. Dysmorphol. 4 (1): 1–11.  
  • Colige A, Vandenberghe I, Thiry M; et al. (2002). "Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3". J. Biol. Chem. 277 (8): 5756–66.  
  • Kevorkian L, Young DA, Darrah C; et al. (2004). "Expression profiling of metalloproteinases and their inhibitors in cartilage". Arthritis Rheum. 50 (1): 131–41.  
  • Hurskainen TL, Hirohata S, Seldin MF, Apte SS (1999). "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family". J. Biol. Chem. 274 (36): 25555–63.  
  • Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65.  
  • Dubail J, Kesteloot F, Deroanne C; et al. (2010). "ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity". Cellular and molecular life sciences : CMLS 67 (24): 4213–32.  
  • Colige A, Sieron AL, Li SW; et al. (1999). "Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene". Am. J. Hum. Genet. 65 (2): 308–17.  
  • Hartley JL, Temple GF, Brasch MA (2000). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95.  
  • Tang BL (2001). "ADAMTS: a novel family of extracellular matrix proteases". Int. J. Biochem. Cell Biol. 33 (1): 33–44.  
  • Lasky-Su J, Anney RJ, Neale BM; et al. (2008). "Genome-wide association scan of the time to onset of Attention Deficit Hyperactivity Disorder". Am. J. Med. Genet. B Neuropsychiatr. Genet. 147B (8): 1355–8.  
  • Colige A, Ruggiero F, Vandenberghe I; et al. (2005). "Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of fibrillar procollagens types I-III and V". J. Biol. Chem. 280 (41): 34397–408.  
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903.  
  • Brandenberger R, Wei H, Zhang S; et al. (2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16.  
  • Tomii Y, Kamochi J, Yamazaki H; et al. (2002). "Human thrombospondin 2 inhibits proliferation of microvascular endothelial cells". Int. J. Oncol. 20 (2): 339–42.  

Further reading

  1. ^ Tang BL, Hong W (February 1999). "ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats". FEBS Lett. 445 (2–3): 223–5.  
  2. ^ "Entrez Gene: ADAM metallopeptidase with thrombospondin type 1 motif". 
  3. ^ a b Colige A, Nuytinck L, Hausser I, van Essen AJ, Thiry M, Herens C, Adès LC, Malfait F, Paepe AD, Franck P, Wolff G, Oosterwijk JC, Smitt JH, Lapière CM, Nusgens BV (October 2004). "Novel types of mutation responsible for the dermatosparactic type of Ehlers-Danlos syndrome (Type VIIC) and common polymorphisms in the ADAMTS2 gene". J. Invest. Dermatol. 123 (4): 656–63.  


See also
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