PTP4A2
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
Protein tyrosine phosphatase type IVA 2 is an enzyme that in humans is encoded by the PTP4A2 gene.{{cite journal | vauthors = Zhao Z, Lee CC, Monckton DG, Yazdani A, Coolbaugh MI, Li X, Bailey J, Shen Y, Caskey CT | title = Characterization and genomic mapping of genes and pseudogenes of a new human protein tyrosine phosphatase | journal = Genomics | volume = 35 | issue = 1 | pages = 172–81 |date=Sep 1996 | pmid = 8661118 | doi = 10.1006/geno.1996.0336 }}{{cite journal | vauthors = Zeng Q, Hong W, Tan YH | title = Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1 | journal = Biochem Biophys Res Commun | volume = 244 | issue = 2 | pages = 421–7 |date=Apr 1998 | pmid = 9514946 | doi = 10.1006/bbrc.1998.8291 }}{{cite web | title = Entrez Gene: PTP4A2 protein tyrosine phosphatase type IVA, member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8073}}
The protein encoded by this gene belongs to a small class of the protein tyrosine phosphatase (PTP) family. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif.
This PTP has been shown to primarily associate with plasmic and endosomal membrane through its C-terminal prenylation. This PTP was found to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), and thus may function as a regulator of GGT II activity.
Overexpression of this gene in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis. Alternatively spliced transcript variants that encode two distinct isoforms have been described.
References
{{reflist}}
Further reading
{{refbegin | 2}}
- {{cite journal |vauthors=Rommens JM, Durocher F, McArthur J, etal |title=Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21. |journal=Genomics |volume=28 |issue= 3 |pages= 530–42 |year= 1996 |pmid= 7490091 |doi=10.1006/geno.1995.1185 }}
- {{cite journal |vauthors=Montagna M, Serova O, Sylla BS, etal |title=A 100-kb physical and transcriptional map around the EDH17B2 gene: identification of three novel genes and a pseudogene of a human homologue of the rat PRL-1 tyrosine phosphatase. |journal=Hum. Genet. |volume=96 |issue= 5 |pages= 532–8 |year= 1996 |pmid= 8529999 |doi= 10.1007/bf00197407|s2cid=24567366 }}
- {{cite journal |vauthors=Cates CA, Michael RL, Stayrook KR, etal |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 |vauthors=Gjörloff-Wingren A, Saxena M, Han S, etal |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 |s2cid=8132613 }}
- {{cite journal | vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000 | pmc=310948 }}
- {{cite journal |vauthors=Si X, Zeng Q, Ng CH, etal |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 |doi-access= free }}
- {{cite journal |vauthors=Wang Q, Holmes DI, Powell SM, etal |title=Analysis of stromal-epithelial interactions in prostate cancer identifies PTPCAAX2 as a potential oncogene |journal=Cancer Lett. |volume=175 |issue= 1 |pages= 63–9 |year= 2002 |pmid= 11734337 |doi=10.1016/S0304-3835(01)00703-0 }}
- {{cite journal | vauthors=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 |doi-access= free }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
- {{cite journal |vauthors=Pathak MK, Dhawan D, Lindner DJ, etal |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 }}
- {{cite journal |vauthors=Werner SR, Lee PA, DeCamp MW, etal |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 |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 | pmc=528928 }}
- {{cite journal |vauthors=Wiemann S, Arlt D, Huber W, etal |title=From ORFeome to biology: a functional genomics pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 }}
- {{cite journal |vauthors=Mehrle A, Rosenfelder H, Schupp I, etal |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 | pmc=1347501 }}
- {{cite journal |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |bibcode=2006Natur.441..315G |doi-access= free }}
- {{cite journal |vauthors=Radke I, Götte M, Kersting C, etal |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.6603261 | pmc=2360632 }}
- {{cite journal | vauthors=Dumaual CM, Sandusky GE, Crowell PL, Randall SK |title=Cellular localization of PRL-1 and PRL-2 gene expression in normal adult human tissues |journal=J. Histochem. Cytochem. |volume=54 |issue= 12 |pages= 1401–12 |year= 2007 |pmid= 16957164 |doi= 10.1369/jhc.6A7019.2006 |pmc=3958126 }}
- {{cite journal |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein-protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 }}
{{refend}}
{{PDB Gallery|geneid=8073}}
{{Protein tyrosine phosphatases}}
{{gene-1-stub}}