PTP4A2

Protein tyrosine phosphatase type IVA 2 is an enzyme that in humans is encoded by the PTP4A2 gene.[5][6][7]

PTP4A2
Identifiers
Aliases	PTP4A2, HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, PTP4A, PTPCAAX2, ptp-IV1a, ptp-IV1b, protein tyrosine phosphatase type IVA, member 2, protein tyrosine phosphatase 4A2
External IDs	OMIM: 601584 MGI: 1277117 HomoloGene: 20744 GeneCards: PTP4A2
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p35.2 Start 31,906,421 bp[1] End 31,944,856 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D2.2 Start 129,811,219 bp[2] End 129,850,003 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • prenylated protein tyrosine phosphatase activity • protein tyrosine phosphatase activity • phosphatase activity • phosphoprotein phosphatase activity • hydrolase activity • GO:0001948 protein binding Cellular component • cytoplasm • endosome • cell membrane • early endosome • membrane • cell nucleus • cytosol Biological process • protein dephosphorylation • dephosphorylation • peptidyl-tyrosine dephosphorylation • post-translational modification Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8073	19244
Ensembl	ENSG00000184007	ENSMUSG00000028788
UniProt	Q12974	O70274
RefSeq (mRNA)	NM_001195100 NM_001195101 NM_003479 NM_080391 NM_080392 NM_001369858 NM_001369859 NM_001369860	NM_001164745 NM_008974
RefSeq (protein)	NP_001182029 NP_001182030 NP_536316 NP_001356787 NP_001356788 NP_001356789	NP_001158217 NP_033000
Location (UCSC)	Chr 1: 31.91 – 31.94 Mb	Chr 4: 129.81 – 129.85 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000184007 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028788 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "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.