PTP4A1

PTP4A1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1RXD, 1XM2
Identifiers
Aliases	PTP4A1, HH72, PRL-1, PRL1, PTP(CAAX1), PTPCAAX1, protein tyrosine phosphatase type IVA, member 1, protein tyrosine phosphatase 4A1
External IDs	OMIM: 601585; MGI: 1277096; HomoloGene: 2587; GeneCards: PTP4A1; OMA:PTP4A1 - orthologs
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6q12 Start 63,521,746 bp[1] End 63,583,436 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in islet of Langerhans muscle of thigh liver right lobe of liver rectum gastrocnemius muscle ganglionic eminence skeletal muscle tissue ventricular zone smooth muscle tissue n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphoprotein phosphatase activity phosphatase activity protein tyrosine phosphatase activity hydrolase activity protein tyrosine/serine/threonine phosphatase activity protein binding Cellular component cytoplasm endosome membrane plasma membrane spindle early endosome endoplasmic reticulum cytoplasmic side of plasma membrane cytoskeleton nucleus Biological process positive regulation of cell migration protein dephosphorylation multicellular organism development cell cycle dephosphorylation peptidyl-tyrosine dephosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7803 19243 Ensembl ENSG00000112245 ENSMUSG00000026064 UniProt Q93096 Q63739 RefSeq (mRNA) NM_003463 NM_011200 RefSeq (protein) NP_003454 NP_035330 Location (UCSC) Chr 6: 63.52 – 63.58 Mb n/a PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Protein tyrosine phosphatase type IVA 1 is an enzyme that in humans is encoded by the PTP4A1 gene.[4][5]

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.[5]

Interactions

PTP4A1 has been shown to interact with ATF7.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000112245 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Peng Y, Genin A, Spinner NB, Diamond RH, Taub R (Aug 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. doi:10.1074/jbc.273.27.17286. PMID 9642300.
5. "Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1".
6. Peters, C S; Liang X; Li S; Kannan S; Peng Y; Taub R; Diamond R H (Apr 2001). "ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase". J. Biol. Chem. 276 (17). United States: 13718–26. doi:10.1074/jbc.M011562200. ISSN 0021-9258. PMID 11278933.

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. doi:10.1016/S0304-3835(96)04459-X. 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.
• 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. doi:10.1002/(SICI)1098-2744(199912)26:4<298::AID-MC8>3.0.CO;2-M. PMID 10569806. S2CID 21209686.
• 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. doi:10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J. PMID 10940933. S2CID 8132613.
• 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. doi:10.1128/MCB.22.10.3527-3536.2002. PMC 133798. 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. 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.
• 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. Bibcode:2003Natur.425..805M. 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. 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.
• 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. PMC 2360632. PMID 16832410.