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{{Infobox_gene}}
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'''Protein tyrosine phosphatase type IVA 1''' is an [[enzyme]] that in humans is encoded by the ''PTP4A1'' [[gene]].<ref name="pmid9642300">{{cite journal |vauthors=Peng Y, Genin A, Spinner NB, Diamond RH, Taub R | title = The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer | journal = J Biol Chem | volume = 273 | issue = 27 | pages = 17286–95 |date=Aug 1998 | pmid = 9642300 | pmc =  | doi =10.1074/jbc.273.27.17286 }}</ref><ref name="entrez"/>
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{{GNF_Protein_box
| image = PBB_Protein_PTP4A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rxd.
| PDB = {{PDB2|1rxd}}, {{PDB2|1x24}}, {{PDB2|1xm2}}, {{PDB2|1zck}}, {{PDB2|1zcl}}
| Name = Protein tyrosine phosphatase type IVA, member 1
| HGNCid = 9634
| Symbol = PTP4A1
| AltSymbols =; PRL1; DKFZp779M0721; HH72; PRL-1; PTP(CAAX1); PTPCAAX1
| OMIM = 601585
| ECnumber = 
| Homologene = 2587
| MGIid = 1277096
| GeneAtlas_image1 = PBB_GE_PTP4A1_200733_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTP4A1_200730_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTP4A1_200731_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030335 |text = positive regulation of cell migration}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7803
    | Hs_Ensembl = ENSG00000112245
    | Hs_RefseqProtein = NP_003454
    | Hs_RefseqmRNA = NM_003463
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 64339879
    | Hs_GenLoc_end = 64351447
    | Hs_Uniprot = Q93096
    | Mm_EntrezGene = 19243
    | Mm_Ensembl =   
    | Mm_RefseqmRNA = NM_011200
    | Mm_RefseqProtein = NP_035330
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot =   
  }}
}}
'''Protein tyrosine phosphatase type IVA, member 1''', also known as '''PTP4A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7803| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7803| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7803| accessdate = }}</ref>
}}
}}
==Interactions==
PTP4A1 has been shown to [[Protein-protein interaction|interact]] with [[ATF7]].<ref name=pmid11278933>{{cite journal |last=Peters |first=C S |authorlink= |author2=Liang X |author3=Li S |author4=Kannan S |author5=Peng Y |author6=Taub R |author7=Diamond R H  |date=Apr 2001 |title=ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase |journal=J. Biol. Chem. |volume=276 |issue=17 |pages=13718–26 |publisher= |location = United States| issn = 0021-9258| pmid = 11278933 |doi = 10.1074/jbc.M011562200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Cates CA, Michael RL, Stayrook KR, ''et al.'' |title=Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases. |journal=Cancer Lett. |volume=110 |issue= 1-2 |pages= 49-55 |year= 1997 |pmid= 9018080 |doi=  }}
*{{cite journal   |vauthors=Cates CA, Michael RL, Stayrook KR, etal |title=Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases |journal=Cancer Lett. |volume=110 |issue= 1–2 |pages= 49–55 |year= 1997 |pmid= 9018080 |doi=10.1016/S0304-3835(96)04459-X }}
*{{cite journal  | author=Dayton MA, Knobloch TJ |title=Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38. |journal=Receptors & signal transduction |volume=7 |issue= 4 |pages= 241-56 |year= 1998 |pmid= 9633825 |doi=  }}
*{{cite journal  |vauthors=Dayton MA, Knobloch TJ |title=Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38 |journal=Receptors & signal transduction |volume=7 |issue= 4 |pages= 241–56 |year= 1998 |pmid= 9633825 |doi=  }}
*{{cite journal  | author=Peng Y, Genin A, Spinner NB, ''et al.'' |title=The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer. |journal=J. Biol. Chem. |volume=273 |issue= 27 |pages= 17286-95 |year= 1998 |pmid= 9642300 |doi= }}
*{{cite journal  |vauthors=Tsujimoto H, Nishizuka S, Redpath JL, Stanbridge EJ |title=Differential gene expression in tumorigenic and nontumorigenic HeLa x normal human fibroblast hybrid cells |journal=Mol. Carcinog. |volume=26 |issue= 4 |pages= 298–304 |year= 1999 |pmid= 10569806 |doi=10.1002/(SICI)1098-2744(199912)26:4<298::AID-MC8>3.0.CO;2-M  }}
*{{cite journal | author=Tsujimoto H, Nishizuka S, Redpath JL, Stanbridge EJ |title=Differential gene expression in tumorigenic and nontumorigenic HeLa x normal human fibroblast hybrid cells. |journal=Mol. Carcinog. |volume=26 |issue= 4 |pages= 298-304 |year= 1999 |pmid= 10569806 |doi= }}
*{{cite journal   |vauthors=Zeng Q, Si X, Horstmann H, etal |title=Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21444–52 |year= 2000 |pmid= 10747914 |doi= 10.1074/jbc.M000453200 }}
*{{cite journal | author=Zeng Q, Si X, Horstmann H, ''et al.'' |title=Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21444-52 |year= 2000 |pmid= 10747914 |doi= 10.1074/jbc.M000453200 }}
*{{cite journal   |vauthors=Gjörloff-Wingren A, Saxena M, Han S, etal |title=Subcellular localization of intracellular protein tyrosine phosphatases in T cells |journal=Eur. J. Immunol. |volume=30 |issue= 8 |pages= 2412–21 |year= 2000 |pmid= 10940933 |doi=10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J  }}
*{{cite journal | author=Gjörloff-Wingren A, Saxena M, Han S, ''et al.'' |title=Subcellular localization of intracellular protein tyrosine phosphatases in T cells. |journal=Eur. J. Immunol. |volume=30 |issue= 8 |pages= 2412-21 |year= 2000 |pmid= 10940933 |doi= }}
*{{cite journal   |vauthors=Peters CS, Liang X, Li S, etal |title=ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 13718–26 |year= 2001 |pmid= 11278933 |doi= 10.1074/jbc.M011562200 }}
*{{cite journal | author=Peters CS, Liang X, Li S, ''et al.'' |title=ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 13718-26 |year= 2001 |pmid= 11278933 |doi= 10.1074/jbc.M011562200 }}
*{{cite journal   |vauthors=Si X, Zeng Q, Ng CH, etal |title=Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 32875–82 |year= 2001 |pmid= 11447212 |doi= 10.1074/jbc.M010400200 }}
*{{cite journal | author=Si X, Zeng Q, Ng CH, ''et al.'' |title=Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II. |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 32875-82 |year= 2001 |pmid= 11447212 |doi= 10.1074/jbc.M010400200 }}
*{{cite journal   |vauthors=Nicolas G, Fournier CM, Galand C, etal |title=Tyrosine Phosphorylation Regulates Alpha II Spectrin Cleavage by Calpain |journal=Mol. Cell. Biol. |volume=22 |issue= 10 |pages= 3527–36 |year= 2002 |pmid= 11971983 |doi=10.1128/MCB.22.10.3527-3536.2002  | pmc=133798  }}
*{{cite journal  | author=Nicolas G, Fournier CM, Galand C, ''et al.'' |title=Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain. |journal=Mol. Cell. Biol. |volume=22 |issue= 10 |pages= 3527-36 |year= 2002 |pmid= 11971983 |doi= }}
*{{cite journal  |vauthors=Wang J, Kirby CE, Herbst R |title=The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 46659–68 |year= 2003 |pmid= 12235145 |doi= 10.1074/jbc.M206407200 }}
*{{cite journal | author=Wang J, Kirby CE, Herbst R |title=The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis. |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 46659-68 |year= 2003 |pmid= 12235145 |doi= 10.1074/jbc.M206407200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Pathak MK, Dhawan D, Lindner DJ, etal |title=Pentamidine is an inhibitor of PRL phosphatases with anticancer activity |journal=Mol. Cancer Ther. |volume=1 |issue= 14 |pages= 1255–64 |year= 2003 |pmid= 12516958 |doi= }}
*{{cite journal | author=Pathak MK, Dhawan D, Lindner DJ, ''et al.'' |title=Pentamidine is an inhibitor of PRL phosphatases with anticancer activity. |journal=Mol. Cancer Ther. |volume=1 |issue= 14 |pages= 1255-64 |year= 2003 |pmid= 12516958 |doi=  }}
*{{cite journal   |vauthors=Zeng Q, Dong JM, Guo K, etal |title=PRL-3 and PRL-1 promote cell migration, invasion, and metastasis |journal=Cancer Res. |volume=63 |issue= 11 |pages= 2716–22 |year= 2003 |pmid= 12782572 |doi=  }}
*{{cite journal | author=Zeng Q, Dong JM, Guo K, ''et al.'' |title=PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. |journal=Cancer Res. |volume=63 |issue= 11 |pages= 2716-22 |year= 2003 |pmid= 12782572 |doi= }}
*{{cite journal   |vauthors=Mungall AJ, Palmer SA, Sims SK, etal |title=The DNA sequence and analysis of human chromosome 6 |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 }}
*{{cite journal | author=Mungall AJ, Palmer SA, Sims SK, ''et al.'' |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805-11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 }}
*{{cite journal   |vauthors=Werner SR, Lee PA, DeCamp MW, etal |title=Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases |journal=Cancer Lett. |volume=202 |issue= 2 |pages= 201–11 |year= 2004 |pmid= 14643450 |doi=10.1016/S0304-3835(03)00517-2  }}
*{{cite journal | author=Werner SR, Lee PA, DeCamp MW, ''et al.'' |title=Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases. |journal=Cancer Lett. |volume=202 |issue= 2 |pages= 201-11 |year= 2004 |pmid= 14643450 |doi=  }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Raghavendra Prasad HS, Qi Z, Srinivasan KN, Gopalakrishnakone P |title=Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach |journal=Toxicon |volume=44 |issue= 6 |pages= 597–608 |year= 2005 |pmid= 15501285 |doi= 10.1016/j.toxicon.2004.07.018 }}
*{{cite journal | author=Raghavendra Prasad HS, Qi Z, Srinivasan KN, Gopalakrishnakone P |title=Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach. |journal=Toxicon |volume=44 |issue= 6 |pages= 597-608 |year= 2005 |pmid= 15501285 |doi= 10.1016/j.toxicon.2004.07.018 }}
*{{cite journal   |vauthors=Jeong DG, Kim SJ, Kim JH, etal |title=Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms |journal=J. Mol. Biol. |volume=345 |issue= 2 |pages= 401–13 |year= 2005 |pmid= 15571731 |doi= 10.1016/j.jmb.2004.10.061 }}
*{{cite journal | author=Jeong DG, Kim SJ, Kim JH, ''et al.'' |title=Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms. |journal=J. Mol. Biol. |volume=345 |issue= 2 |pages= 401-13 |year= 2005 |pmid= 15571731 |doi= 10.1016/j.jmb.2004.10.061 }}
*{{cite journal   |vauthors=Sun JP, Wang WQ, Yang H, etal |title=Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion |journal=Biochemistry |volume=44 |issue= 36 |pages= 12009–21 |year= 2005 |pmid= 16142898 |doi= 10.1021/bi0509191 }}
*{{cite journal | author=Sun JP, Wang WQ, Yang H, ''et al.'' |title=Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion. |journal=Biochemistry |volume=44 |issue= 36 |pages= 12009-21 |year= 2005 |pmid= 16142898 |doi= 10.1021/bi0509191 }}
*{{cite journal   |vauthors=Radke I, Götte M, Kersting C, etal |title=Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer |journal=Br. J. Cancer |volume=95 |issue= 3 |pages= 347–54 |year= 2006 |pmid= 16832410 |doi= 10.1038/sj.bjc.6603261 | pmc=2360632 }}
*{{cite journal | author=Radke I, Götte M, Kersting C, ''et al.'' |title=Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer. |journal=Br. J. Cancer |volume=95 |issue= 3 |pages= 347-54 |year= 2006 |pmid= 16832410 |doi= 10.1038/sj.bjc.6603261 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=7803}}
{{Protein tyrosine phosphatases}}
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Revision as of 18:56, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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Wikidata
View/Edit Human

Protein tyrosine phosphatase type IVA 1 is an enzyme that in humans is encoded by the PTP4A1 gene.[1][2]

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.[2]

Interactions

PTP4A1 has been shown to interact with ATF7.[3]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1".
  3. ↑ 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. United States. 276 (17): 13718–26. doi:10.1074/jbc.M011562200. ISSN 0021-9258. PMID 11278933.

Further reading



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