- PTP4A1
Protein tyrosine phosphatase type IVA, member 1, also known as PTP4A1, is a human
gene .PBB_Summary
section_title =
summary_text = The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs), which contains a PTP domain and a characteristic C-terminal prenylation motif. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This tyrosine phosphatase is a nuclear protein, but may primarily associate with plasma membrane. The surface membrane association of this protein depends on its C-terminal prenylation. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which implicated its role in the tumorigenesis. Studies in rat suggested that this gene may be an immediate-early gene in mitogen-stimulated cells.cite web | title = Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7803| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Cates CA, Michael RL, Stayrook KR, "et al." |title=Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases. |journal=Cancer Lett. |volume=110 |issue= 1-2 |pages= 49–55 |year= 1997 |pmid= 9018080 |doi=10.1016/S0304-3835(96)04459-X
*cite journal | author=Dayton MA, Knobloch TJ |title=Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38. |journal=Receptors & signal transduction |volume=7 |issue= 4 |pages= 241–56 |year= 1998 |pmid= 9633825 |doi=
*cite journal | author=Peng Y, Genin A, Spinner NB, "et al." |title=The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer. |journal=J. Biol. Chem. |volume=273 |issue= 27 |pages= 17286–95 |year= 1998 |pmid= 9642300 |doi=10.1074/jbc.273.27.17286
*cite journal | author=Tsujimoto H, Nishizuka S, Redpath JL, Stanbridge EJ |title=Differential gene expression in tumorigenic and nontumorigenic HeLa x normal human fibroblast hybrid cells. |journal=Mol. Carcinog. |volume=26 |issue= 4 |pages= 298–304 |year= 1999 |pmid= 10569806 |doi=10.1002/(SICI)1098-2744(199912)26:4<298::AID-MC8>3.0.CO;2-M
*cite journal | author=Zeng Q, Si X, Horstmann H, "et al." |title=Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21444–52 |year= 2000 |pmid= 10747914 |doi= 10.1074/jbc.M000453200
*cite journal | author=Gjörloff-Wingren A, Saxena M, Han S, "et al." |title=Subcellular localization of intracellular protein tyrosine phosphatases in T cells. |journal=Eur. J. Immunol. |volume=30 |issue= 8 |pages= 2412–21 |year= 2000 |pmid= 10940933 |doi=10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J
*cite journal | author=Peters CS, Liang X, Li S, "et al." |title=ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 13718–26 |year= 2001 |pmid= 11278933 |doi= 10.1074/jbc.M011562200
*cite journal | author=Si X, Zeng Q, Ng CH, "et al." |title=Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II. |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 32875–82 |year= 2001 |pmid= 11447212 |doi= 10.1074/jbc.M010400200
*cite journal | author=Nicolas G, Fournier CM, Galand C, "et al." |title=Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain. |journal=Mol. Cell. Biol. |volume=22 |issue= 10 |pages= 3527–36 |year= 2002 |pmid= 11971983 |doi=10.1128/MCB.22.10.3527-3536.2002
*cite journal | author=Wang J, Kirby CE, Herbst R |title=The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis. |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 46659–68 |year= 2003 |pmid= 12235145 |doi= 10.1074/jbc.M206407200
*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=Pathak MK, Dhawan D, Lindner DJ, "et al." |title=Pentamidine is an inhibitor of PRL phosphatases with anticancer activity. |journal=Mol. Cancer Ther. |volume=1 |issue= 14 |pages= 1255–64 |year= 2003 |pmid= 12516958 |doi=
*cite journal | author=Zeng Q, Dong JM, Guo K, "et al." |title=PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. |journal=Cancer Res. |volume=63 |issue= 11 |pages= 2716–22 |year= 2003 |pmid= 12782572 |doi=
*cite journal | author=Mungall AJ, Palmer SA, Sims SK, "et al." |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055
*cite journal | author=Werner SR, Lee PA, DeCamp MW, "et al." |title=Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases. |journal=Cancer Lett. |volume=202 |issue= 2 |pages= 201–11 |year= 2004 |pmid= 14643450 |doi=10.1016/S0304-3835(03)00517-2
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Raghavendra Prasad HS, Qi Z, Srinivasan KN, Gopalakrishnakone P |title=Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach. |journal=Toxicon |volume=44 |issue= 6 |pages= 597–608 |year= 2005 |pmid= 15501285 |doi= 10.1016/j.toxicon.2004.07.018
*cite journal | author=Jeong DG, Kim SJ, Kim JH, "et al." |title=Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms. |journal=J. Mol. Biol. |volume=345 |issue= 2 |pages= 401–13 |year= 2005 |pmid= 15571731 |doi= 10.1016/j.jmb.2004.10.061
*cite journal | author=Sun JP, Wang WQ, Yang H, "et al." |title=Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion. |journal=Biochemistry |volume=44 |issue= 36 |pages= 12009–21 |year= 2005 |pmid= 16142898 |doi= 10.1021/bi0509191
*cite journal | author=Radke I, Götte M, Kersting C, "et al." |title=Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer. |journal=Br. J. Cancer |volume=95 |issue= 3 |pages= 347–54 |year= 2006 |pmid= 16832410 |doi= 10.1038/sj.bjc.6603261PBB_Controls
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