Biology:ADAM19
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
ADAM19 (A Disintegrin And Metalloproteinase 19, MADDAM, meltrin beta), is a human gene.[1]
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. This member is a type I transmembrane protein and serves as a marker for dendritic cell differentiation. It has also been demonstrated to be an active metalloproteinase, which may be involved in normal physiological and pathological processes such as cells migration, cell adhesion, cell-cell and cell-matrix interactions, and signal transduction. Alternative splicing results in two transcript variants.[1]
Interactions
ADAM19 has been shown to interact with ABI2.[2]
References
- ↑ 1.0 1.1 "Entrez Gene: ADAM19 ADAM metallopeptidase domain 19 (meltrin beta)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8728.
- ↑ "Screen and identification of proteins interacting with ADAM19 cytoplasmic tail". Molecular Biology Reports 29 (3): 317–23. Sep 2002. doi:10.1023/A:1020409217215. PMID 12463424.
External links
- Human ADAM19 genome location and ADAM19 gene details page in the UCSC Genome Browser.
Further reading
- "3,400 new expressed sequence tags identify diversity of transcripts in human brain". Nature Genetics 4 (3): 256–67. Jul 1993. doi:10.1038/ng0793-256. PMID 8358434.
- "Cloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cells". The Journal of Biological Chemistry 273 (7): 4180–7. Feb 1998. doi:10.1074/jbc.273.7.4180. PMID 9461614.
- "Chromosomal assignment of two ADAM genes, TACE (ADAM17) and MLTNB (ADAM19), to human chromosomes 2 and 5, respectively, and of Mltnb to mouse chromosome 11". Genomics 54 (1): 178–9. Nov 1998. doi:10.1006/geno.1998.5544. PMID 9806848.
- "Molecular cloning and characterization of a human metalloprotease disintegrin--a novel marker for dendritic cell differentiation". Blood 96 (2): 732–9. Jul 2000. doi:10.1182/blood.V96.2.732. PMID 10887142.
- "Roles of Meltrin beta /ADAM19 in the processing of neuregulin". The Journal of Biological Chemistry 276 (12): 9352–8. Mar 2001. doi:10.1074/jbc.M007913200. PMID 11116142.
- "Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta". Biochemical and Biophysical Research Communications 280 (3): 744–55. Jan 2001. doi:10.1006/bbrc.2000.4200. PMID 11162584.
- "Inhibitory antibodies against endopeptidase activity of human adamalysin 19". Biochemical and Biophysical Research Communications 289 (1): 288–94. Nov 2001. doi:10.1006/bbrc.2001.5958. PMID 11708814.
- "Intracellular activation of human adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites". The Journal of Biological Chemistry 277 (28): 25583–91. Jul 2002. doi:10.1074/jbc.M203532200. PMID 12006600.
- "Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding". Molecular Biology of the Cell 13 (6): 2031–44. Jun 2002. doi:10.1091/mbc.01-11-0561. PMID 12058067.
- "Autolytic processing at Glu586-Ser587 within the cysteine-rich domain of human adamalysin 19/disintegrin-metalloproteinase 19 is necessary for its proteolytic activity". The Journal of Biological Chemistry 277 (50): 48514–22. Dec 2002. doi:10.1074/jbc.M208961200. PMID 12393862.
- "Screen and identification of proteins interacting with ADAM19 cytoplasmic tail". Molecular Biology Reports 29 (3): 317–23. Sep 2002. doi:10.1023/A:1020409217215. PMID 12463424.
- "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells". The Journal of Biological Chemistry 278 (19): 16844–51. May 2003. doi:10.1074/jbc.M300267200. PMID 12615925.
- "Catalytic properties of ADAM19". The Journal of Biological Chemistry 278 (25): 22331–40. Jun 2003. doi:10.1074/jbc.M302781200. PMID 12682046.
- "Evidence for disulfide involvement in the regulation of intramolecular autolytic processing by human adamalysin19/ADAM19". Experimental Cell Research 298 (1): 285–95. Aug 2004. doi:10.1016/j.yexcr.2004.04.022. PMID 15242783.
- "Epigenetic regulation of the dendritic cell-marker gene ADAM19". Biochemical and Biophysical Research Communications 332 (2): 456–64. Jul 2005. doi:10.1016/j.bbrc.2005.04.149. PMID 15896713.
- "Upregulation of ADAM19 in chronic allograft nephropathy". American Journal of Transplantation 6 (7): 1673–81. Jul 2006. doi:10.1111/j.1600-6143.2006.01384.x. PMID 16827870.
- "ADAM19 is tightly associated with constitutive Alzheimer's disease APP alpha-secretase in A172 cells". Biochemical and Biophysical Research Communications 352 (1): 111–7. Jan 2007. doi:10.1016/j.bbrc.2006.10.181. PMID 17112471.
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