PTP4A1

Protein tyrosine phosphatase type IVA, member 1
File:PBB Protein PTP4A1 image.jpg PDB rendering based on 1rxd.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1rxd​, 1x24​, 1xm2​, 1zck​, 1zcl​
Identifiers
Symbols	PTP4A1 ; PRL1; DKFZp779M0721; HH72; PRL-1; PTP(CAAX1); PTPCAAX1
External IDs	Template:OMIM5 Template:MGI HomoloGene: 2587
Gene ontology Molecular function Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PTP4A1 200733 s at tn.png
File:PBB GE PTP4A1 200730 s at tn.png
File:PBB GE PTP4A1 200731 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Protein tyrosine phosphatase type IVA, member 1, also known as PTP4A1, is a human gene.

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.

Further reading

• 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. PMID 9018080.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Dayton MA, Knobloch TJ (1998). "Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38". Receptors & signal transduction. 7 (4): 241–56. PMID 9633825.
• Peng Y, Genin A, Spinner NB; et al. (1998). "The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer". J. Biol. Chem. 273 (27): 17286–95. PMID 9642300.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tsujimoto H, Nishizuka S, Redpath JL, Stanbridge EJ (1999). "Differential gene expression in tumorigenic and nontumorigenic HeLa x normal human fibroblast hybrid cells". Mol. Carcinog. 26 (4): 298–304. PMID 10569806.CS1 maint: Multiple names: authors list (link)
• Zeng Q, Si X, Horstmann H; et al. (2000). "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome". J. Biol. Chem. 275 (28): 21444–52. doi:10.1074/jbc.M000453200. PMID 10747914.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 10940933.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Peters CS, Liang X, Li S; et al. (2001). "ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase". J. Biol. Chem. 276 (17): 13718–26. doi:10.1074/jbc.M011562200. PMID 11278933.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nicolas G, Fournier CM, Galand C; et al. (2002). "Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain". Mol. Cell. Biol. 22 (10): 3527–36. PMID 11971983.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zeng Q, Dong JM, Guo K; et al. (2003). "PRL-3 and PRL-1 promote cell migration, invasion, and metastasis". Cancer Res. 63 (11): 2716–22. PMID 12782572.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mungall AJ, Palmer SA, Sims SK; et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 14643450.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Raghavendra Prasad HS, Qi Z, Srinivasan KN, Gopalakrishnakone P (2005). "Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach". Toxicon. 44 (6): 597–608. doi:10.1016/j.toxicon.2004.07.018. PMID 15501285.CS1 maint: Multiple names: authors list (link)
• Jeong DG, Kim SJ, Kim JH; et al. (2005). "Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms". J. Mol. Biol. 345 (2): 401–13. doi:10.1016/j.jmb.2004.10.061. PMID 15571731.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sun JP, Wang WQ, Yang H; et al. (2005). "Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion". Biochemistry. 44 (36): 12009–21. doi:10.1021/bi0509191. PMID 16142898.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 16832410.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)