- ADAM19
ADAM metallopeptidase domain 19 (meltrin beta), also known as ADAM19, is a human
gene .cite web | title = Entrez Gene: ADAM19 ADAM metallopeptidase domain 19 (meltrin beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8728| accessdate = ]PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: ADAM19 ADAM metallopeptidase domain 19 (meltrin beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8728| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Adams MD, Kerlavage AR, Fields C, Venter JC |title=3,400 new expressed sequence tags identify diversity of transcripts in human brain. |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 256–67 |year= 1993 |pmid= 8358434 |doi= 10.1038/ng0793-256
*cite journal | author=Inoue D, Reid M, Lum L, "et al." |title=Cloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cells. |journal=J. Biol. Chem. |volume=273 |issue= 7 |pages= 4180–7 |year= 1998 |pmid= 9461614 |doi=
*cite journal | author=Hirohata S, Seldin MF, Apte SS |title=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. |journal=Genomics |volume=54 |issue= 1 |pages= 178–9 |year= 1999 |pmid= 9806848 |doi= 10.1006/geno.1998.5544
*cite journal | author=Fritsche J, Moser M, Faust S, "et al." |title=Molecular cloning and characterization of a human metalloprotease disintegrin--a novel marker for dendritic cell differentiation. |journal=Blood |volume=96 |issue= 2 |pages= 732–9 |year= 2000 |pmid= 10887142 |doi=
*cite journal | author=Shirakabe K, Wakatsuki S, Kurisaki T, Fujisawa-Sehara A |title=Roles of Meltrin beta /ADAM19 in the processing of neuregulin. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9352–8 |year= 2001 |pmid= 11116142 |doi= 10.1074/jbc.M007913200
*cite journal | author=Wei P, Zhao YG, Zhuang L, "et al." |title=Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 3 |pages= 744–55 |year= 2001 |pmid= 11162584 |doi= 10.1006/bbrc.2000.4200
*cite journal | author=Zhao YG, Wei P, Sang QX |title=Inhibitory antibodies against endopeptidase activity of human adamalysin 19. |journal=Biochem. Biophys. Res. Commun. |volume=289 |issue= 1 |pages= 288–94 |year= 2001 |pmid= 11708814 |doi= 10.1006/bbrc.2001.5958
*cite journal | author=Kang T, Zhao YG, Pei D, "et al." |title=Intracellular activation of human adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25583–91 |year= 2002 |pmid= 12006600 |doi= 10.1074/jbc.M203532200
*cite journal | author=Díaz-Rodríguez E, Montero JC, Esparís-Ogando A, "et al." |title=Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding. |journal=Mol. Biol. Cell |volume=13 |issue= 6 |pages= 2031–44 |year= 2002 |pmid= 12058067 |doi= 10.1091/mbc.01-11-0561
*cite journal | author=Kang T, Park HI, Suh Y, "et al." |title=Autolytic processing at Glu586-Ser587 within the cysteine-rich domain of human adamalysin 19/disintegrin-metalloproteinase 19 is necessary for its proteolytic activity. |journal=J. Biol. Chem. |volume=277 |issue= 50 |pages= 48514–22 |year= 2003 |pmid= 12393862 |doi= 10.1074/jbc.M208961200
*cite journal | author=Huang L, Feng L, Yang L, "et al." |title=Screen and identification of proteins interacting with ADAM19 cytoplasmic tail. |journal=Mol. Biol. Rep. |volume=29 |issue= 3 |pages= 317–23 |year= 2003 |pmid= 12463424 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Abram CL, Seals DF, Pass I, "et al." |title=The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells. |journal=J. Biol. Chem. |volume=278 |issue= 19 |pages= 16844–51 |year= 2003 |pmid= 12615925 |doi= 10.1074/jbc.M300267200
*cite journal | author=Chesneau V, Becherer JD, Zheng Y, "et al." |title=Catalytic properties of ADAM19. |journal=J. Biol. Chem. |volume=278 |issue= 25 |pages= 22331–40 |year= 2003 |pmid= 12682046 |doi= 10.1074/jbc.M302781200
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Kang T, Tschesche H, Amy Sang QX |title=Evidence for disulfide involvement in the regulation of intramolecular autolytic processing by human adamalysin19/ADAM19. |journal=Exp. Cell Res. |volume=298 |issue= 1 |pages= 285–95 |year= 2004 |pmid= 15242783 |doi= 10.1016/j.yexcr.2004.04.022
*cite journal | author=Ehrnsperger A, Rehli M, Thu-Hang P, Kreutz M |title=Epigenetic regulation of the dendritic cell-marker gene ADAM19. |journal=Biochem. Biophys. Res. Commun. |volume=332 |issue= 2 |pages= 456–64 |year= 2005 |pmid= 15896713 |doi= 10.1016/j.bbrc.2005.04.149
*cite journal | author=Melenhorst WB, van den Heuvel MC, Stegeman CA, "et al." |title=Upregulation of ADAM19 in chronic allograft nephropathy. |journal=Am. J. Transplant. |volume=6 |issue= 7 |pages= 1673–81 |year= 2006 |pmid= 16827870 |doi= 10.1111/j.1600-6143.2006.01384.x
*cite journal | author=Tanabe C, Hotoda N, Sasagawa N, "et al." |title=ADAM19 is tightly associated with constitutive Alzheimer's disease APP alpha-secretase in A172 cells. |journal=Biochem. Biophys. Res. Commun. |volume=352 |issue= 1 |pages= 111–7 |year= 2007 |pmid= 17112471 |doi= 10.1016/j.bbrc.2006.10.181PBB_Controls
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