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ADAM9

Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.[1][2]

Function

Function

This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene interacts with SH3 domain-containing proteins, binds mitotic arrest deficient 2 beta protein, and is also involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. Two alternative splice variants have been identified, encoding distinct isoforms.[2]

Interactions

Interactions

ADAM9 has been shown to interact with:

References

References

  1. Weskamp G, Kratzschmar J, Reid MS, Blobel CP (Jul 1996). “MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains”. J Cell Biol. 132 (4): 717–26. doi:10.1083/jcb.132.4.717. PMC 2199860. PMID 8647900.
  2. 2.0 2.1 “Entrez Gene: ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma)”.
  3. Nelson KK, Schlöndorff J, Blobel CP (Nov 1999). “Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta”. Biochem. J. 343 (Pt 3): 673–80. doi:10.1042/0264-6021:3430673. PMC 1220601. PMID 10527948.
  4. 4.0 4.1 Howard L, Nelson KK, Maciewicz RA, Blobel CP (Oct 1999). “Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1”. J. Biol. Chem. 274 (44): 31693–9. doi:10.1074/jbc.274.44.31693. PMID 10531379.
Further reading

Further reading

External links


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