PTP4A2: Difference between revisions
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| | '''Protein tyrosine phosphatase type IVA 2''' is an [[enzyme]] that in humans is encoded by the ''PTP4A2'' [[gene]].<ref name="pmid8661118">{{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 | pmc = | doi = 10.1006/geno.1996.0336 }}</ref><ref name="pmid9514946">{{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 | pmc = | doi = 10.1006/bbrc.1998.8291 }}</ref><ref name="entrez">{{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| accessdate = }}</ref> | ||
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| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: PTP4A2 protein tyrosine phosphatase type IVA, member 2| url = | | summary_text = 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.<ref name="entrez">{{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| accessdate = }}</ref> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | *{{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 | *{{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}} | ||
*{{cite journal | *{{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 | *{{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 }} | ||
*{{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 | *{{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 }} | ||
*{{cite journal | *{{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 | | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | *{{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 |doi= }} | ||
*{{cite journal | *{{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 | *{{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 | *{{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 | *{{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 | *{{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 }} | ||
*{{cite journal | *{{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 | | *{{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 | *{{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}} | {{refend}} | ||
{{PDB Gallery|geneid=8073}} | |||
{{Protein tyrosine phosphatases}} | |||
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Latest revision as of 18:05, 15 December 2018
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Protein tyrosine phosphatase type IVA 2 is an enzyme that in humans is encoded by the PTP4A2 gene.[1][2][3]
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.[3]
References
- ↑ Zhao Z, Lee CC, Monckton DG, Yazdani A, Coolbaugh MI, Li X, Bailey J, Shen Y, Caskey CT (Sep 1996). "Characterization and genomic mapping of genes and pseudogenes of a new human protein tyrosine phosphatase". Genomics. 35 (1): 172–81. doi:10.1006/geno.1996.0336. PMID 8661118.
- ↑ Zeng Q, Hong W, Tan YH (Apr 1998). "Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1". Biochem Biophys Res Commun. 244 (2): 421–7. doi:10.1006/bbrc.1998.8291. PMID 9514946.
- ↑ 3.0 3.1 "Entrez Gene: PTP4A2 protein tyrosine phosphatase type IVA, member 2".
Further reading
- Rommens JM, Durocher F, McArthur J, et al. (1996). "Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21". Genomics. 28 (3): 530–42. doi:10.1006/geno.1995.1185. PMID 7490091.
- Montagna M, Serova O, Sylla BS, et al. (1996). "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". Hum. Genet. 96 (5): 532–8. doi:10.1007/bf00197407. PMID 8529999.
- Cates CA, Michael RL, Stayrook KR, et al. (1997). "Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases". Cancer Lett. 110 (1–2): 49–55. doi:10.1016/S0304-3835(96)04459-X. PMID 9018080.
- Gjörloff-Wingren A, Saxena M, Han S, et al. (2000). "Subcellular localization of intracellular protein tyrosine phosphatases in T cells". Eur. J. Immunol. 30 (8): 2412–21. doi:10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J. PMID 10940933.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Si X, Zeng Q, Ng CH, et al. (2001). "Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II". J. Biol. Chem. 276 (35): 32875–82. doi:10.1074/jbc.M010400200. PMID 11447212.
- Wang Q, Holmes DI, Powell SM, et al. (2002). "Analysis of stromal-epithelial interactions in prostate cancer identifies PTPCAAX2 as a potential oncogene". Cancer Lett. 175 (1): 63–9. doi:10.1016/S0304-3835(01)00703-0. PMID 11734337.
- Wang J, Kirby CE, Herbst R (2003). "The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis". J. Biol. Chem. 277 (48): 46659–68. doi:10.1074/jbc.M206407200. PMID 12235145.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Pathak MK, Dhawan D, Lindner DJ, et al. (2003). "Pentamidine is an inhibitor of PRL phosphatases with anticancer activity". Mol. Cancer Ther. 1 (14): 1255–64. PMID 12516958.
- Werner SR, Lee PA, DeCamp MW, et al. (2004). "Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases". Cancer Lett. 202 (2): 201–11. doi:10.1016/S0304-3835(03)00517-2. PMID 14643450.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
- Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
- Radke I, Götte M, Kersting C, et al. (2006). "Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer". Br. J. Cancer. 95 (3): 347–54. doi:10.1038/sj.bjc.6603261. PMC 2360632. PMID 16832410.
- Dumaual CM, Sandusky GE, Crowell PL, Randall SK (2007). "Cellular localization of PRL-1 and PRL-2 gene expression in normal adult human tissues". J. Histochem. Cytochem. 54 (12): 1401–12. doi:10.1369/jhc.6A7019.2006. PMC 3958126. PMID 16957164.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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