PTPRE

PTPRE

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2JJD

Identifiers

PTPRE, HPTPE, PTPE, R-PTP-EPSILON, protein tyrosine phosphatase, receptor type E, protein tyrosine phosphatase receptor type E

External IDs

OMIM: 600926; MGI: 97813; HomoloGene: 31387; GeneCards: PTPRE; OMA:PTPRE - orthologs

Gene location (Human)

Chr.	Chromosome 10 (human)^[1]

Band	10q26.2	Start	127,907,103 bp^[1]
Band	10q26.2	End	128,085,855 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)^[2]

Band	7 F3\|7 81.27 cM	Start	135,139,210 bp^[2]
Band	7 F3\|7 81.27 cM	End	135,288,022 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

monocyte

blood

bone marrow cells

granulocyte

sural nerve

visceral pleura

trigeminal ganglion

right lung

appendix

upper lobe of left lung

Top expressed in

granulocyte

sciatic nerve

tibiofemoral joint

primary oocyte

CA3 field

subiculum

olfactory tubercle

bone marrow

right lung lobe

stroma of bone marrow

More reference expression data


More reference expression data

Gene ontology
Molecular function	protein tyrosine phosphatase activity phosphatase activity transmembrane receptor protein tyrosine phosphatase activity protein binding phosphoprotein phosphatase activity hydrolase activity
Cellular component	cytoplasm integral component of membrane plasma membrane membrane nucleus
Biological process	negative regulation of insulin receptor signaling pathway protein dephosphorylation peptidyl-tyrosine dephosphorylation dephosphorylation
Sources:Amigo / QuickGO

Species

Human

Mouse


5791


19267


ENSG00000132334


ENSMUSG00000041836


P23469


P49446

RefSeq (mRNA)

NM_006504 NM_130435 NM_001316676 NM_001316677 NM_001323354
NM_001323355 NM_001323356 NM_001323357


NM_011212 NM_001316678 NM_001316679 NM_001316680 NM_001316681

RefSeq (protein)

NP_001303605 NP_001303606 NP_001310283 NP_001310284 NP_001310285
NP_001310286 NP_006495 NP_569119


NP_001303607 NP_001303608 NP_001303609 NP_001303610 NP_035342

Location (UCSC)

Chr 10: 127.91 – 128.09 Mb

Chr 7: 135.14 – 135.29 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Receptor-type tyrosine-protein phosphatase epsilon is an enzyme that in humans is encoded by the PTPRE gene.^[5]^[6]

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.^[6]

Interactions

PTPRE has been shown to interact with KCNB1.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000132334 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000041836 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. hdl:2066/197648. PMID 8595895. S2CID 26498003.
^ ^a ^b "Entrez Gene: PTPRE protein tyrosine phosphatase, receptor type, E".
^ 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

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. doi:10.1002/j.1460-2075.1990.tb07523.x. PMC 552056. PMID 2170109.
Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (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.
Murakawa K, Matsubara K, Fukushima A, Yoshii J, Okubo K (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, Yoshii J, Matsubara K (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.
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 (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, Weremowicz S, Leder P (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, Shinder V, Attali B, Elson A (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.
Gil-Henn H, Volohonsky G, Toledano-Katchalski H, Gandre S, Elson A (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, Wiedlocha A, Aasheim H (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. S2CID 19787656.
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. S2CID 35703266.
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.
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, Granot-Attas S, Shohat G, Gil-Henn H, Yung Y, Elson A (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)

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

ACP1

Cdc25
- CDC25A
- CDC25B
- CDC25C

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