PTP4A2

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 129,705,012 bp [2] End 129,743,796 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in corpus callosum internal globus pallidus inferior ganglion of vagus nerve palpebral conjunctiva middle frontal gyrus optic nerve external globus pallidus parotid gland medulla oblongata ventral tegmental area Top expressed in extensor digitorum longus muscle triceps brachii muscle vastus lateralis muscle plantaris muscle gastrocnemius muscle skeletal muscle tissue extraocular muscle tibialis anterior muscle ankle sternocleidomastoid muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function prenylated protein tyrosine phosphatase activity protein tyrosine phosphatase activity phosphatase activity phosphoprotein phosphatase activity hydrolase activity protein binding Cellular component cytoplasm endosome plasma membrane early endosome membrane nucleus cytosol Biological process protein dephosphorylation dephosphorylation peptidyl-tyrosine dephosphorylation post-translational protein 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: 129.71 – 129.74 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. S2CID   24567366.
• 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. S2CID   8132613.
• 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2006Natur.441..315G. 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.