PTPRE: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
 
m (Bot: HTTP→HTTPS (v470))
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Receptor-type tyrosine-protein phosphatase epsilon''' is an [[enzyme]] that in humans is encoded by the ''PTPRE'' [[gene]].<ref name="pmid8595895">{{cite journal | vauthors = van den Maagdenberg AM, van den Hurk HH, Weghuis D, Wieringa B, Geurts van Kessel A, Hendriks WJ | title = Assignment of the human protein tyrosine phosphatase epsilon (PTPRE) gene to chromosome 10q26 by fluorescence in situ hybridization | journal = Genomics | volume = 30 | issue = 1 | pages = 128–9 | date = April 1996 | pmid = 8595895 | pmc = | doi = 10.1006/geno.1995.0026 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PTPRE protein tyrosine phosphatase, receptor type, E| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5791| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Protein tyrosine phosphatase, receptor type, E
| HGNCid = 9669
| Symbol = PTPRE
| AltSymbols =; DKFZp313F1310; HPTPE; PTPE; R-PTP-EPSILON
| OMIM = 600926
| ECnumber = 
| Homologene = 31387
| MGIid = 97813
| GeneAtlas_image1 = PBB_GE_PTPRE_221840_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005001 |text = transmembrane receptor protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0007185 |text = transmembrane receptor protein tyrosine phosphatase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5791
    | Hs_Ensembl = ENSG00000132334
    | Hs_RefseqProtein = NP_006495
    | Hs_RefseqmRNA = NM_006504
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 129595315
    | Hs_GenLoc_end = 129774155
    | Hs_Uniprot = P23469
    | Mm_EntrezGene = 19267
    | Mm_Ensembl = ENSMUSG00000041836
    | Mm_RefseqmRNA = NM_011212
    | Mm_RefseqProtein = NP_035342
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 135376167
    | Mm_GenLoc_end = 135524637
    | Mm_Uniprot = Q05CJ9
  }}
}}
'''Protein tyrosine phosphatase, receptor type, E''', also known as '''PTPRE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPRE protein tyrosine phosphatase, receptor type, E| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5791| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Two alternatively spliced transcript variants of this gene have been reported, one of which encodes a receptor-type PTP that possesses a short extracellular domain, a single transmembrane region, and two tandem intracytoplasmic catalytic domains; Another one encodes a PTP that contains a distinct hydrophilic N-terminus, and thus represents a nonreceptor-type isoform of this PTP. Studies of the similar gene in mice suggested the regulatory roles of this PTP in RAS related signal transduction pathways, cytokines induced SATA signaling, as well as the activation of voltage-gated K+ channels.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Two alternatively spliced transcript variants of this gene have been reported, one of which encodes a receptor-type PTP that possesses a short extracellular domain, a single transmembrane region, and two tandem intracytoplasmic catalytic domains; Another one encodes a PTP that contains a distinct hydrophilic N-terminus, and thus represents a nonreceptor-type isoform of this PTP. Studies of the similar gene in mice suggested the regulatory roles of this PTP in RAS related signal transduction pathways, cytokines induced SATA signaling, as well as the activation of voltage-gated K+ channels.<ref name="entrez">{{cite web | title = Entrez Gene: PTPRE protein tyrosine phosphatase, receptor type, E| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5791| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
PTPRE has been shown to [[Protein-protein interaction|interact]] with [[KCNB1]].<ref name=pmid10921884>{{cite journal | vauthors = Peretz A, Gil-Henn H, Sobko A, Shinder V, Attali B, Elson A | title = Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon | journal = EMBO J. | volume = 19 | issue = 15 | pages = 4036–45 | date = August 2000 | pmid = 10921884 | pmc = 306594 | doi = 10.1093/emboj/19.15.4036 }}</ref>
 
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Roskoski R | title = Src kinase regulation by phosphorylation and dephosphorylation. | journal = Biochem. Biophys. Res. Commun. | volume = 331 | issue = 1 | pages = 1–14 | year = 2005 | pmid = 15845350 | doi = 10.1016/j.bbrc.2005.03.012 }}
| citations =
* {{cite journal | vauthors = Krueger NX, Streuli M, Saito H | title = Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. | journal = EMBO J. | volume = 9 | issue = 10 | pages = 3241–52 | year = 1990 | pmid = 2170109 | pmc = 552056 | doi =  }}
*{{cite journal | author=Roskoski R |title=Src kinase regulation by phosphorylation and dephosphorylation. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 1 |pages= 1-14 |year= 2005 |pmid= 15845350 |doi= 10.1016/j.bbrc.2005.03.012 }}
* {{cite journal | vauthors = Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O | title = Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. | journal = Nature | volume = 377 | issue = 6547 Suppl | pages = 3–174 | year = 1995 | pmid = 7566098 | doi = <!-- none available --> | url = http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf | format = PDF }}
*{{cite journal | author=Krueger NX, Streuli M, Saito H |title=Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3241-52 |year= 1990 |pmid= 2170109 |doi=  }}
* {{cite journal | vauthors = Murakawa K, Matsubara K, Fukushima A, Yoshii J, Okubo K | title = Chromosomal assignments of 3'-directed partial cDNA sequences representing novel genes expressed in granulocytoid cells. | journal = Genomics | volume = 23 | issue = 2 | pages = 379–89 | year = 1995 | pmid = 7835887 | doi = 10.1006/geno.1994.1514 }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
* {{cite journal | vauthors = Okubo K, Itoh K, Fukushima A, Yoshii J, Matsubara K | title = Monitoring cell physiology by expression profiles and discovering cell type-specific genes by compiled expression profiles. | journal = Genomics | volume = 30 | issue = 2 | pages = 178–86 | year = 1996 | pmid = 8586417 | doi = 10.1006/geno.1995.9887 }}
*{{cite journal | author=Murakawa K, Matsubara K, Fukushima A, ''et al.'' |title=Chromosomal assignments of 3'-directed partial cDNA sequences representing novel genes expressed in granulocytoid cells. |journal=Genomics |volume=23 |issue= 2 |pages= 379-89 |year= 1995 |pmid= 7835887 |doi= 10.1006/geno.1994.1514 }}
* {{cite journal | vauthors = Elson A, Leder P | title = Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 26 | pages = 12235–9 | year = 1996 | pmid = 8618876 | pmc = 40331 | doi = 10.1073/pnas.92.26.12235 }}
*{{cite journal | author=Okubo K, Itoh K, Fukushima A, ''et al.'' |title=Monitoring cell physiology by expression profiles and discovering cell type-specific genes by compiled expression profiles. |journal=Genomics |volume=30 |issue= 2 |pages= 178-86 |year= 1996 |pmid= 8586417 |doi= 10.1006/geno.1995.9887 }}
* {{cite journal | vauthors = Gastier JM, Brody T, Pulido JC, Businga T, Sunden S, Hu X, Maitra S, Buetow KH, Murray JC, Sheffield VC, Boguski M, Duyk GM, Hudson TJ | title = Development of a screening set for new (CAG/CTG)n dynamic mutations. | journal = Genomics | volume = 32 | issue = 1 | pages = 75–85 | year = 1996 | pmid = 8786123 | doi = 10.1006/geno.1996.0078 }}
*{{cite journal | author=van den Maagdenberg AM, van den Hurk HH, Weghuis D, ''et al.'' |title=Assignment of the human protein tyrosine phosphatase epsilon (PTPRE) gene to chromosome 10q26 by fluorescence in situ hybridization. |journal=Genomics |volume=30 |issue= 1 |pages= 128-9 |year= 1996 |pmid= 8595895 |doi= }}
* {{cite journal | vauthors = Elson A, Kozak CA, Morton CC, Weremowicz S, Leder P | title = The protein tyrosine phosphatase epsilon gene maps to mouse chromosome 7 and human chromosome 10q26. | journal = Genomics | volume = 31 | issue = 3 | pages = 373–5 | year = 1997 | pmid = 8838320 | doi = 10.1006/geno.1996.0061 }}
*{{cite journal | author=Elson A, Leder P |title=Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 26 |pages= 12235-9 |year= 1996 |pmid= 8618876 |doi= }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery. | journal = Genome Res. | volume = 6 | issue = 9 | pages = 791–806 | year = 1997 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal | author=Gastier JM, Brody T, Pulido JC, ''et al.'' |title=Development of a screening set for new (CAG/CTG)n dynamic mutations. |journal=Genomics |volume=32 |issue= 1 |pages= 75-85 |year= 1996 |pmid= 8786123 |doi= 10.1006/geno.1996.0078 }}
* {{cite journal | vauthors = Toledano-Katchalski H, Elson A | title = The transmembranal and cytoplasmic forms of protein tyrosine phosphatase epsilon physically associate with the adaptor molecule Grb2. | journal = Oncogene | volume = 18 | issue = 36 | pages = 5024–31 | year = 1999 | pmid = 10490839 | doi = 10.1038/sj.onc.1202883 }}
*{{cite journal | author=Elson A, Kozak CA, Morton CC, ''et al.'' |title=The protein tyrosine phosphatase epsilon gene maps to mouse chromosome 7 and human chromosome 10q26. |journal=Genomics |volume=31 |issue= 3 |pages= 373-5 |year= 1997 |pmid= 8838320 |doi= }}
* {{cite journal | vauthors = Tanuma N, Nakamura K, Shima H, Kikuchi K | title = Protein-tyrosine phosphatase PTPepsilon C inhibits Jak-STAT signaling and differentiation induced by interleukin-6 and leukemia inhibitory factor in M1 leukemia cells. | journal = J. Biol. Chem. | volume = 275 | issue = 36 | pages = 28216–21 | year = 2000 | pmid = 10859312 | doi = 10.1074/jbc.M003661200 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Peretz A, Gil-Henn H, Sobko A, Shinder V, Attali B, Elson A | title = Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon. | journal = EMBO J. | volume = 19 | issue = 15 | pages = 4036–45 | year = 2000 | pmid = 10921884 | pmc = 306594 | doi = 10.1093/emboj/19.15.4036 }}
*{{cite journal | author=Toledano-Katchalski H, Elson A |title=The transmembranal and cytoplasmic forms of protein tyrosine phosphatase epsilon physically associate with the adaptor molecule Grb2. |journal=Oncogene |volume=18 |issue= 36 |pages= 5024-31 |year= 1999 |pmid= 10490839 |doi= 10.1038/sj.onc.1202883 }}
* {{cite journal | vauthors = Gil-Henn H, Volohonsky G, Toledano-Katchalski H, Gandre S, Elson A | title = Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control. | journal = Oncogene | volume = 19 | issue = 38 | pages = 4375–84 | year = 2000 | pmid = 10980613 | doi = 10.1038/sj.onc.1203790 }}
*{{cite journal | author=Tanuma N, Nakamura K, Shima H, Kikuchi K |title=Protein-tyrosine phosphatase PTPepsilon C inhibits Jak-STAT signaling and differentiation induced by interleukin-6 and leukemia inhibitory factor in M1 leukemia cells. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 28216-21 |year= 2000 |pmid= 10859312 |doi= 10.1074/jbc.M003661200 }}
* {{cite journal | vauthors = Wabakken T, Hauge H, Finne EF, Wiedlocha A, Aasheim H | title = Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase. | journal = Scand. J. Immunol. | volume = 56 | issue = 2 | pages = 195–203 | year = 2002 | pmid = 12121439 | doi = 10.1046/j.1365-3083.2002.01126.x }}
*{{cite journal | author=Peretz A, Gil-Henn H, Sobko A, ''et al.'' |title=Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon. |journal=EMBO J. |volume=19 |issue= 15 |pages= 4036-45 |year= 2000 |pmid= 10921884 |doi= 10.1093/emboj/19.15.4036 }}
* {{cite journal | vauthors = Wabakken T, Hauge H, Funderud S, Aasheim HC | title = Characterization, expression and functional aspects of a novel protein tyrosine phosphatase epsilon isoform. | journal = Scand. J. Immunol. | volume = 56 | issue = 3 | pages = 276–85 | year = 2002 | pmid = 12193229 | doi = 10.1046/j.1365-3083.2002.01127.x }}
*{{cite journal | author=Gil-Henn H, Volohonsky G, Toledano-Katchalski H, ''et al.'' |title=Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control. |journal=Oncogene |volume=19 |issue= 38 |pages= 4375-84 |year= 2000 |pmid= 10980613 |doi= 10.1038/sj.onc.1203790 }}
* {{cite journal | vauthors = Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J | title = Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases. | journal = J. Biol. Chem. | volume = 277 | issue = 49 | pages = 47263–9 | year = 2003 | pmid = 12376545 | doi = 10.1074/jbc.M205810200 }}
*{{cite journal | author=Wabakken T, Hauge H, Finne EF, ''et al.'' |title=Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase. |journal=Scand. J. Immunol. |volume=56 |issue= 2 |pages= 195-203 |year= 2002 |pmid= 12121439 |doi= }}
* {{cite journal | vauthors = Tiran Z, Peretz A, Attali B, Elson A | title = Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine 124 by Src and by protein-tyrosine phosphatase epsilon. | journal = J. Biol. Chem. | volume = 278 | issue = 19 | pages = 17509–14 | year = 2003 | pmid = 12615930 | doi = 10.1074/jbc.M212766200 }}
*{{cite journal | author=Wabakken T, Hauge H, Funderud S, Aasheim HC |title=Characterization, expression and functional aspects of a novel protein tyrosine phosphatase epsilon isoform. |journal=Scand. J. Immunol. |volume=56 |issue= 3 |pages= 276-85 |year= 2002 |pmid= 12193229 |doi= }}
* {{cite journal | vauthors = Toledano-Katchalski H, Kraut J, Sines T, Granot-Attas S, Shohat G, Gil-Henn H, Yung Y, Elson A | title = Protein tyrosine phosphatase epsilon inhibits signaling by mitogen-activated protein kinases. | journal = Mol. Cancer Res. | volume = 1 | issue = 7 | pages = 541–50 | year = 2004 | pmid = 12754301 | doi =  }}
*{{cite journal | author=Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J |title=Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47263-9 |year= 2003 |pmid= 12376545 |doi= 10.1074/jbc.M205810200 }}
*{{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  | author=Tiran Z, Peretz A, Attali B, Elson A |title=Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine 124 by Src and by protein-tyrosine phosphatase epsilon. |journal=J. Biol. Chem. |volume=278 |issue= 19 |pages= 17509-14 |year= 2003 |pmid= 12615930 |doi= 10.1074/jbc.M212766200 }}
*{{cite journal  | author=Toledano-Katchalski H, Kraut J, Sines T, ''et al.'' |title=Protein tyrosine phosphatase epsilon inhibits signaling by mitogen-activated protein kinases. |journal=Mol. Cancer Res. |volume=1 |issue= 7 |pages= 541-50 |year= 2004 |pmid= 12754301 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Protein tyrosine phosphatases}}
{{WikiDoc Sources}}
 
 
{{gene-10-stub}}

Latest revision as of 01:55, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Receptor-type tyrosine-protein phosphatase epsilon is an enzyme that in humans is encoded by the PTPRE gene.[1][2]

Function

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Two alternatively spliced transcript variants of this gene have been reported, one of which encodes a receptor-type PTP that possesses a short extracellular domain, a single transmembrane region, and two tandem intracytoplasmic catalytic domains; Another one encodes a PTP that contains a distinct hydrophilic N-terminus, and thus represents a nonreceptor-type isoform of this PTP. Studies of the similar gene in mice suggested the regulatory roles of this PTP in RAS related signal transduction pathways, cytokines induced SATA signaling, as well as the activation of voltage-gated K+ channels.[2]

Interactions

PTPRE has been shown to interact with KCNB1.[3]

References

  1. van den Maagdenberg AM, van den Hurk HH, Weghuis D, Wieringa B, Geurts van Kessel A, Hendriks WJ (April 1996). "Assignment of the human protein tyrosine phosphatase epsilon (PTPRE) gene to chromosome 10q26 by fluorescence in situ hybridization". Genomics. 30 (1): 128–9. doi:10.1006/geno.1995.0026. PMID 8595895.
  2. 2.0 2.1 "Entrez Gene: PTPRE protein tyrosine phosphatase, receptor type, E".
  3. Peretz A, Gil-Henn H, Sobko A, Shinder V, Attali B, Elson A (August 2000). "Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon". EMBO J. 19 (15): 4036–45. doi:10.1093/emboj/19.15.4036. PMC 306594. PMID 10921884.

Further reading