PTP4A3

PTP4A3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1R6H, 1V3A, 2MBC
Identifiers
Aliases	PTP4A3 , PRL-3, PRL-R, PRL3, protein tyrosine phosphatase type IVA, member 3, protein tyrosine phosphatase 4A3
External IDs	OMIM: 606449 MGI: 1277098 HomoloGene: 22500 GeneCards: PTP4A3
Gene location (Human) Chr. Chromosome 8 (human) [1] Band 8q24.3 Start 141,391,995 bp [1] End 141,432,454 bp [1]
Gene location (Mouse) Chr. Chromosome 15 (mouse) [2] Band 15|15 D3 Start 73,723,145 bp [2] End 73,758,766 bp [2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein tyrosine phosphatase activity • prenylated protein tyrosine phosphatase activity • phosphatase activity • phosphoprotein phosphatase activity • hydrolase activity • protein tyrosine/serine/threonine phosphatase activity • GO:0001948 protein binding Cellular component • endosome • plasma membrane • early endosome • membrane • nucleus • cytoplasm Biological process • Notch signaling pathway • protein dephosphorylation • positive regulation of vascular permeability • regulation of vascular endothelial growth factor signaling pathway • endothelial cell migration • dephosphorylation • peptidyl-tyrosine dephosphorylation • regulation of transcription, DNA-templated • positive regulation of NIK/NF-kappaB signaling • positive regulation of establishment of protein localization • cellular response to leukemia inhibitory factor Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11156	19245
Ensembl	ENSG00000184489 ENSG00000275575	ENSMUSG00000059895
UniProt	O75365	Q9D658
RefSeq (mRNA)	NM_007079 NM_032611	NM_001166388 NM_001166389 NM_001166390 NM_008975 NM_001357591
RefSeq (protein)	NP_009010 NP_116000	NP_001159860 NP_001159861 NP_001159862 NP_033001 NP_001344520
Location (UCSC)	Chr 8: 141.39 – 141.43 Mb	Chr 15: 73.72 – 73.76 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Protein tyrosine phosphatase type IVA 3 is an enzyme that in humans is encoded by the PTP4A3 gene. ^[5]

The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs). PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This class of PTPs contain a PTP domain and a characteristic C-terminal prenylation motif. Studies of this class of PTPs in mice demonstrated that they were prenylated proteins in vivo, which suggested their association with cell plasma membrane. Overexpression of this gene in mammalian cells was reported to inhibit angiotensin-II induced cell calcium mobilization and promote cell growth. Two alternatively spliced variants exist. ^[5]

References

1. ENSG00000275575 GRCh38: Ensembl release 89: ENSG00000184489, ENSG00000275575 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000059895 - 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. "Entrez Gene: PTP4A3 protein tyrosine phosphatase type IVA, member 3".

Further reading

• Zeng Q, Hong W, Tan YH (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.
• 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.
• 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.
• Matter WF, Estridge T, Zhang C, et al. (2001). "Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling". Biochem. Biophys. Res. Commun. 283 (5): 1061–8. doi:10.1006/bbrc.2001.4881. PMID   11355880.
• Saha S, Bardelli A, Buckhaults P, et al. (2001). "A phosphatase associated with metastasis of colorectal cancer". Science. 294 (5545): 1343–6. Bibcode:2001Sci...294.1343S. doi:10.1126/science.1065817. PMID   11598267. S2CID   42104960.
• 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.
• 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.
• Bardelli A, Saha S, Sager JA, et al. (2004). "PRL-3 expression in metastatic cancers". Clin. Cancer Res. 9 (15): 5607–15. PMID   14654542.
• Kozlov G, Cheng J, Ziomek E, et al. (2004). "Structural insights into molecular function of the metastasis-associated phosphatase PRL-3". J. Biol. Chem. 279 (12): 11882–9. doi: 10.1074/jbc.M312905200 . PMID   14704153.
• Kim KA, Song JS, Jee J, et al. (2004). "Structure of human PRL-3, the phosphatase associated with cancer metastasis". FEBS Lett. 565 (1–3): 181–7. doi: 10.1016/j.febslet.2004.03.062 . PMID   15135076. S2CID   29552515.
• Wu X, Zeng H, Zhang X, et al. (2004). "Phosphatase of Regenerating Liver-3 Promotes Motility and Metastasis of Mouse Melanoma Cells". Am. J. Pathol. 164 (6): 2039–54. doi:10.1016/S0002-9440(10)63763-7. PMC   1615773 . PMID   15161639.
• 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.
• Kato H, Semba S, Miskad UA, et al. (2005). "High expression of PRL-3 promotes cancer cell motility and liver metastasis in human colorectal cancer: a predictive molecular marker of metachronous liver and lung metastases". Clin. Cancer Res. 10 (21): 7318–28. doi: 10.1158/1078-0432.CCR-04-0485 . PMID   15534108.
• Li J, Guo K, Koh VW, et al. (2005). "Generation of PRL-3- and PRL-1-specific monoclonal antibodies as potential diagnostic markers for cancer metastases". Clin. Cancer Res. 11 (6): 2195–204. doi: 10.1158/1078-0432.CCR-04-1984 . PMID   15788667.
• Polato F, Codegoni A, Fruscio R, et al. (2006). "PRL-3 phosphatase is implicated in ovarian cancer growth". Clin. Cancer Res. 11 (19 Pt 1): 6835–9. doi: 10.1158/1078-0432.CCR-04-2357 . PMID   16203771.
• Peng L, Jin G, Wang L, et al. (2006). "Identification of integrin alpha1 as an interacting protein of protein tyrosine phosphatase PRL-3". Biochem. Biophys. Res. Commun. 342 (1): 179–83. doi:10.1016/j.bbrc.2006.01.102. PMID   16472776.
• Rouleau C, Roy A, St Martin T, et al. (2006). "Protein tyrosine phosphatase PRL-3 in malignant cells and endothelial cells: expression and function". Mol. Cancer Ther. 5 (2): 219–29. doi: 10.1158/1535-7163.MCT-05-0289 . PMID   16505094.
• 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.