- PTPRM
Protein tyrosine phosphatase, receptor type, M, also known as PTPRM, is a human
gene .cite web | title = Entrez Gene: PTPRM protein tyrosine phosphatase, receptor type, M| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5797| accessdate = ]PBB_Summary
section_title =
summary_text = The protein encoded by this gene is a member of the proteintyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP has been shown to mediate cell-cell aggregation through the interaction with another molecule of this PTP on an adjacent cell. This PTP can interact with scaffolding protein RACK1/GNB2L1, which may be necessary for the downstream signaling in response to cell-cell adhesion.cite web | title = Entrez Gene: PTPRM protein tyrosine phosphatase, receptor type, M| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5797| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Gebbink MF, van Etten I, Hateboer G, "et al." |title=Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase. |journal=FEBS Lett. |volume=290 |issue= 1-2 |pages= 123–30 |year= 1991 |pmid= 1655529 |doi=
*cite journal | author=Brady-Kalnay SM, Rimm DL, Tonks NK |title=Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo. |journal=J. Cell Biol. |volume=130 |issue= 4 |pages= 977–86 |year= 1995 |pmid= 7642713 |doi=
*cite journal | author=Zondag GC, Koningstein GM, Jiang YP, "et al." |title=Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain. |journal=J. Biol. Chem. |volume=270 |issue= 24 |pages= 14247–50 |year= 1995 |pmid= 7782276 |doi=
*cite journal | author=Brady-Kalnay SM, Tonks NK |title=Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTP mu. |journal=J. Biol. Chem. |volume=269 |issue= 45 |pages= 28472–7 |year= 1994 |pmid= 7961788 |doi=
*cite journal | author=Brady-Kalnay SM, Flint AJ, Tonks NK |title=Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation. |journal=J. Cell Biol. |volume=122 |issue= 4 |pages= 961–72 |year= 1993 |pmid= 8394372 |doi=
*cite journal | author=Suijkerbuijk RF, Gebbink MF, Moolenaar WH, Geurts van Kessel A |title=Fine mapping of the human receptor-like protein tyrosine phosphatase gene (PTPRM) to 18p11.2 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=64 |issue= 3-4 |pages= 245–6 |year= 1993 |pmid= 8404049 |doi=
*cite journal | author=Campan M, Yoshizumi M, Seidah NG, "et al." |title=Increased proteolytic processing of protein tyrosine phosphatase mu in confluent vascular endothelial cells: the role of PC5, a member of the subtilisin family. |journal=Biochemistry |volume=35 |issue= 12 |pages= 3797–802 |year= 1996 |pmid= 8620001 |doi= 10.1021/bi952552d
*cite journal | author=Hoffmann KM, Tonks NK, Barford D |title=The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27505–8 |year= 1997 |pmid= 9346878 |doi=
*cite journal | author=Brady-Kalnay SM, Mourton T, Nixon JP, "et al." |title=Dynamic interaction of PTPmu with multiple cadherins in vivo. |journal=J. Cell Biol. |volume=141 |issue= 1 |pages= 287–96 |year= 1998 |pmid= 9531566 |doi=
*cite journal | author=Serra-Pagès C, Medley QG, Tang M, "et al." |title=Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15611–20 |year= 1998 |pmid= 9624153 |doi=
*cite journal | author=Bianchi C, Sellke FW, Del Vecchio RL, "et al." |title=Receptor-type protein-tyrosine phosphatase mu is expressed in specific vascular endothelial beds in vivo. |journal=Exp. Cell Res. |volume=248 |issue= 1 |pages= 329–38 |year= 1999 |pmid= 10094839 |doi= 10.1006/excr.1999.4428
*cite journal | author=Zondag GC, Reynolds AB, Moolenaar WH |title=Receptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates the catenin p120(ctn). |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11264–9 |year= 2000 |pmid= 10753936 |doi=
*cite journal | author=Blanchetot C, den Hertog J |title=Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12446–52 |year= 2000 |pmid= 10777529 |doi=
*cite journal | author=Feiken E, van Etten I, Gebbink MF, "et al." |title=Intramolecular interactions between the juxtamembrane domain and phosphatase domains of receptor protein-tyrosine phosphatase RPTPmu. Regulation of catalytic activity. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15350–6 |year= 2000 |pmid= 10809770 |doi=
*cite journal | author=Mourton T, Hellberg CB, Burden-Gulley SM, "et al." |title=The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 14896–901 |year= 2001 |pmid= 11278757 |doi= 10.1074/jbc.M010823200
*cite journal | author=Hellberg CB, Burden-Gulley SM, Pietz GE, Brady-Kalnay SM |title=Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 11165–73 |year= 2002 |pmid= 11801604 |doi= 10.1074/jbc.M112157200
*cite journal | author=Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J |title=Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47263–9 |year= 2003 |pmid= 12376545 |doi= 10.1074/jbc.M205810200
*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=Koop EA, Lopes SM, Feiken E, "et al." |title=Receptor protein tyrosine phosphatase mu expression as a marker for endothelial cell heterogeneity; analysis of RPTPmu gene expression using LacZ knock-in mice. |journal=Int. J. Dev. Biol. |volume=47 |issue= 5 |pages= 345–54 |year= 2004 |pmid= 12895029 |doi=
*cite journal | author=Del Vecchio RL, Tonks NK |title=The conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase mu. |journal=J. Biol. Chem. |volume=280 |issue= 2 |pages= 1603–12 |year= 2005 |pmid= 15491993 |doi= 10.1074/jbc.M410181200PBB_Controls
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