PTP4A1

From Wikipedia, the free encyclopedia

Protein tyrosine phosphatase type IVA, member 1

PDB rendering based on 1rxd.

Available structures: 1rxd, 1x24, 1xm2, 1zck, 1zcl

Identifiers

Symbol(s)

PTP4A1; PRL1; DKFZp779M0721; HH72; PRL-1; PTP(CAAX1); PTPCAAX1

External IDs

OMIM: 601585 MGI: 1277096 HomoloGene: 2587

Gene ontology
Molecular Function:	• protein tyrosine phosphatase activity • hydrolase activity
Cellular Component:	• endoplasmic reticulum • membrane
Biological Process:	• protein amino acid dephosphorylation • cell cycle • multicellular organismal development • positive regulation of cell migration

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_003463 (mRNA)
NP_003454 (protein)

NM_011200 (mRNA)
NP_035330 (protein)

Location

Chr 6: 64.34 - 64.35 Mb

n/a

Pubmed search

[1]

[2]

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

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1.

[edit] 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.
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.
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.
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.
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.
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.
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.
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.
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. 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.
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.
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.
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.
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.
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.
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.
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.
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.