PTPRE

Protein tyrosine phosphatase, receptor type, E

Identifiers

PTPRE; DKFZp313F1310; FLJ57799; FLJ58245; HPTPE; PTPE; R-PTP-EPSILON

External IDs

OMIM: 600926 MGI: 97813 HomoloGene: 31387 GeneCards: PTPRE Gene

3.1.3.48

Gene Ontology
Molecular function	• transmembrane receptor protein tyrosine phosphatase activity • protein binding • hydrolase activity • protein homodimerization activity
Cellular component	• nucleus • cytoplasm • plasma membrane • integral to membrane • intermediate filament cytoskeleton
Biological process	• protein phosphorylation • protein dephosphorylation • transmembrane receptor protein tyrosine phosphatase signaling pathway • regulation of mast cell activation • negative regulation of insulin receptor signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 10:
129.71 – 129.88 Mb

Chr 7:
142.73 – 142.88 Mb

PubMed search

[1]

[2]

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

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

^ van den Maagdenberg AM, van den Hurk HH, Weghuis D, Wieringa B, Geurts van Kessel A, Hendriks WJ (Apr 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.
^ ^a ^b "Entrez Gene: PTPRE protein tyrosine phosphatase, receptor type, E". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5791.
^ Peretz, A; Gil-Henn H, Sobko A, Shinder V, Attali B, Elson A (Aug. 2000). "Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon". EMBO J. (ENGLAND) 19 (15): 4036–45. doi:10.1093/emboj/19.15.4036. ISSN 0261-4189. PMC 306594. PMID 10921884. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=306594.

Roskoski R (2005). "Src kinase regulation by phosphorylation and dephosphorylation.". Biochem. Biophys. Res. Commun. 331 (1): 1–14. doi:10.1016/j.bbrc.2005.03.012. PMID 15845350.
Krueger NX, Streuli M, Saito H (1990). "Structural diversity and evolution of human receptor-like protein tyrosine phosphatases.". EMBO J. 9 (10): 3241–52. PMC 552056. PMID 2170109. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=552056.
Adams MD, Kerlavage AR, Fleischmann RD, et al. (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence." (PDF). Nature 377 (6547 Suppl): 3–174. PMID 7566098. http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf.
Murakawa K, Matsubara K, Fukushima A, et al. (1995). "Chromosomal assignments of 3'-directed partial cDNA sequences representing novel genes expressed in granulocytoid cells.". Genomics 23 (2): 379–89. doi:10.1006/geno.1994.1514. PMID 7835887.
Okubo K, Itoh K, Fukushima A, et al. (1996). "Monitoring cell physiology by expression profiles and discovering cell type-specific genes by compiled expression profiles.". Genomics 30 (2): 178–86. doi:10.1006/geno.1995.9887. PMID 8586417.
Elson A, Leder P (1996). "Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon.". Proc. Natl. Acad. Sci. U.S.A. 92 (26): 12235–9. doi:10.1073/pnas.92.26.12235. PMC 40331. PMID 8618876. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40331.
Gastier JM, Brody T, Pulido JC, et al. (1996). "Development of a screening set for new (CAG/CTG)n dynamic mutations.". Genomics 32 (1): 75–85. doi:10.1006/geno.1996.0078. PMID 8786123.
Elson A, Kozak CA, Morton CC, et al. (1997). "The protein tyrosine phosphatase epsilon gene maps to mouse chromosome 7 and human chromosome 10q26.". Genomics 31 (3): 373–5. doi:10.1006/geno.1996.0061. PMID 8838320.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Toledano-Katchalski H, Elson A (1999). "The transmembranal and cytoplasmic forms of protein tyrosine phosphatase epsilon physically associate with the adaptor molecule Grb2.". Oncogene 18 (36): 5024–31. doi:10.1038/sj.onc.1202883. PMID 10490839.
Tanuma N, Nakamura K, Shima H, Kikuchi K (2000). "Protein-tyrosine phosphatase PTPepsilon C inhibits Jak-STAT signaling and differentiation induced by interleukin-6 and leukemia inhibitory factor in M1 leukemia cells.". J. Biol. Chem. 275 (36): 28216–21. doi:10.1074/jbc.M003661200. PMID 10859312.
Peretz A, Gil-Henn H, Sobko A, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=306594.
Gil-Henn H, Volohonsky G, Toledano-Katchalski H, et al. (2000). "Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control.". Oncogene 19 (38): 4375–84. doi:10.1038/sj.onc.1203790. PMID 10980613.
Wabakken T, Hauge H, Finne EF, et al. (2002). "Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase.". Scand. J. Immunol. 56 (2): 195–203. doi:10.1046/j.1365-3083.2002.01126.x. PMID 12121439.
Wabakken T, Hauge H, Funderud S, Aasheim HC (2002). "Characterization, expression and functional aspects of a novel protein tyrosine phosphatase epsilon isoform.". Scand. J. Immunol. 56 (3): 276–85. doi:10.1046/j.1365-3083.2002.01127.x. PMID 12193229.
Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J (2003). "Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases.". J. Biol. Chem. 277 (49): 47263–9. doi:10.1074/jbc.M205810200. PMID 12376545.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Tiran Z, Peretz A, Attali B, Elson A (2003). "Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine 124 by Src and by protein-tyrosine phosphatase epsilon.". J. Biol. Chem. 278 (19): 17509–14. doi:10.1074/jbc.M212766200. PMID 12615930.
Toledano-Katchalski H, Kraut J, Sines T, et al. (2004). "Protein tyrosine phosphatase epsilon inhibits signaling by mitogen-activated protein kinases.". Mol. Cancer Res. 1 (7): 541–50. PMID 12754301.

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs	Receptor type PTPs (PTPRA, PTPRB, PTPRC, PTPRD, PTPRE, PTPRF, PTPRG, PTPRH, PTPRJ, PTPRK, PTPRM, PTPRN, PTPRN2, PTPRO, PTPRQ, PTPRR, PTPRS, PTPRT, PTPRU, PTPRZ1, PTPRZ2) Non receptor type PTPs (PTPN1, PTPN2, PTPN3, PTPN4, PTPN5, PTPN6, PTPN7, PTPN9, PTPN11, PTPN12, PTPN13, PTPN14, PTPN18, PTPN20, PTPN21, PTPN22, PTPN23

VH1-like or dual specific phosphatases (DSPs)	MAPK phosphatases (MKPs) (DUSP1, DUSP2, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8, DUSP9, DUSP10, DUSP16, MK-STYX) Slingshots (SSH1, SSH2, SSH3) PRLs (PTP4A1, PTP4A2, PTP4A3) CDC14s (CDC14A, CDC14B, CDKN3, PTP9Q22) Atypical DSPs (DUSP3, DUSP11, DUSP12, DUSP13A, DUSP13B, DUSP14, DUSP15, DUSP18, DUSP19, DUSP21, DUSP22, DUSP23, DUSP24, DUSP25, DUSP26, DUSP27, EMP2A, RNGTT, STYX) Phosphatase and tensin homologs (PTENs) (PTEN, TPIP, TPTE, TNS, TENC1) Myotubularins (MTM1, MTMR2, MTMR3, MTMR4, MTMR5, MTMR6, MTMR7, MTMR8, MTMR9, MTMR10, MTMR11, MTMR12, MTMR13, MTMR14, MTMR15)

Class II

ACP1

Class III

Cdc25: CDC25A, CDC25B, CDC25C

Class IV

Eyes absent homolog (EYA1, EYA2, EYA3, EYA4)

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

PTPRE

Interactions

References

Further reading