ADAM10 - ADAM metallopeptidase domain 10
Entrez Gene Name: ADAM metallopeptidase domain 10
Entrez GeneID: Human(102)
, Mouse(11487), Rat(29650)
, Mouse(11487), Rat(29650) Synonyms: 1700031C13Rik, AD10, ADAM10, ALPHA SECRETASE, CD156c, DISINTEGRIN-METALLOPROTEASE, HsT18717, Kuz, KUZBANIAN, MADM
Gene Summary
- Human (102): Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin. [provided by RefSeq]
- Rat (29650): may act as a disintegrin-metalloprotease related to the reprolysin family [RGD]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras
Cell Regulation
Biological Process
cell-cell signaling, constitutive protein ectodomain proteolysis, in utero embryonic development, integrin-mediated signaling pathway, membrane protein ectodomain proteolysis, monocyte activation, negative regulation of cell adhesion, Notch receptor processing, Notch signaling pathway, nucleocytoplasmic transport, PMA-inducible membrane protein ectodomain proteolysis, positive regulation of cell growth, positive regulation of cell migration, positive regulation of cell proliferation, positive regulation of T cell chemotaxis, protein amino acid phosphorylation, proteolysis, regulation of osteoclast differentiation, response to tumor necrosis factor
Cellular Components
cell surface, cytoplasm, endomembrane system, Golgi apparatus, Golgi-associated vesicle, integral to membrane, membrane, membrane fraction, nucleus, plasma membrane, postsynaptic density, proteinaceous extracellular matrix, trans-Golgi network
Literature References
- 19196476Prinzen C, Trümbach D, Wurst W, Endres K, Postina R, Fahrenholz F. Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice.BMC Genomics 2009 Jan 01;10:66
- 10958785Hattori M, Osterfield M, Flanagan JG. Regulated cleavage of a contact-mediated axon repellent.Science 2000 Aug 25;289(5483):1360-5
- 16199880Maretzky T, Schulte M, Ludwig A, Rose-John S, Blobel C, Hartmann D, Altevogt P, Saftig P, Reiss K. L1 Is Sequentially Processed by Two Differently Activated Metalloproteases and Presenilin/{gamma}-Secretase and Regulates Neural Cell Adhesion, Cell Migration, and Neurite Outgrowth.Mol Cell Biol 2005 Oct 01;25(20):9040-53 View 494 categorized literature findings and their references in IPA
Molecular Functions
endopeptidase activity, hydrolase activity, integrin binding, metal ion binding, metalloendopeptidase activity, metallopeptidase activity, peptidase activity, protein binding, protein homodimerization activity, protein kinase binding, SH2 domain binding, SH3 domain binding, zinc ion binding
Protein Domains
cytoplasmic domain, disintergrin domain, endopeptidase, kinase-like domain, Metalloendopeptidase, MLF1 binding domain, peptidase, protein binding, protein homodimerization, protein kinase binding
Subcellular Locations
cell surface, cellular membrane, centrosome, cytoplasm, Golgi membranes, membrane fraction, nucleus, perinuclear region, plasma membrane
