Receptor-type tyrosine-protein phosphatase epsilon

Details

Name
Receptor-type tyrosine-protein phosphatase epsilon
Synonyms
  • 3.1.3.48
  • Protein-tyrosine phosphatase epsilon
Gene Name
PTPRE
Organism
Humans
Amino acid sequence
>lcl|BSEQ0006873|Receptor-type tyrosine-protein phosphatase epsilon
MEPLCPLLLVGFSLPLARALRGNETTADSNETTTTSGPPDPGASQPLLAWLLLPLLLLLL
VLLLAAYFFRFRKQRKAVVSTSDKKMPNGILEEQEQQRVMLLSRSPSGPKKYFPIPVEHL
EEEIRIRSADDCKQFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHSRVILSQ
LDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERK
EEKCHQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLVSQLHFTS
WPDFGVPFTPIGMLKFLKKVKTLNPVHAGPIVVHCSAGVGRTGTFIVIDAMMAMMHAEQK
VDVFEFVSRIRNQRPQMVQTDMQYTFIYQALLEYYLYGDTELDVSSLEKHLQTMHGTTTH
FDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEYTD
YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMIWEWKSHTIVMLTEVQEREQDKCYQYW
PTEGSVTHGEITIEIKNDTLSEAISIRDFLVTLNQPQARQEEQVRVVRQFHFHGWPEIGI
PAEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQ
AVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIFSDYANFK
Number of residues
700
Molecular Weight
80641.165
Theoretical pI
7.02
GO Classification
Functions
transmembrane receptor protein tyrosine phosphatase activity
Processes
negative regulation of insulin receptor signaling pathway / peptidyl-tyrosine dephosphorylation / protein dephosphorylation / regulation of mast cell activation / transmembrane receptor protein tyrosine phosphatase signaling pathway
Components
cytoplasm / integral component of membrane / nucleus / plasma membrane
General Function
Transmembrane receptor protein tyrosine phosphatase activity
Specific Function
Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity).Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake (By similarity).Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+).
Pfam Domain Function
Transmembrane Regions
47-69
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0012481|Receptor-type tyrosine-protein phosphatase epsilon (PTPRE)
ATGGAGCCCTTGTGTCCACTCCTGCTGGTGGGTTTTAGCTTGCCGCTCGCCAGGGCTCTC
AGGGGCAACGAGACCACTGCCGACAGCAACGAGACAACCACGACCTCAGGCCCTCCGGAC
CCGGGCGCCTCCCAGCCGCTGCTGGCCTGGCTGCTACTGCCGCTGCTGCTCCTCCTCCTC
GTGCTCCTTCTCGCCGCCTACTTCTTCAGGTTCAGGAAGCAGAGGAAAGCTGTGGTCAGC
ACCAGCGACAAGAAGATGCCCAACGGAATCTTGGAGGAGCAAGAGCAGCAAAGGGTGATG
CTGCTCAGCAGGTCACCCTCAGGGCCCAAGAAGTATTTTCCCATCCCCGTGGAGCACCTG
GAGGAGGAGATCCGTATCAGATCCGCCGACGACTGCAAGCAGTTTCGGGAGGAGTTCAAC
TCATTGCCATCTGGACACATACAAGGAACTTTTGAACTGGCAAATAAAGAAGAAAACAGA
GAAAAAAACAGATATCCCAACATCCTTCCCAATGACCATTCTAGGGTGATTCTGAGCCAA
CTGGATGGAATTCCCTGTTCAGACTACATCAATGCTTCCTACATAGATGGTTACAAAGAG
AAGAATAAATTCATAGCAGCTCAAGGTCCCAAACAGGAAACGGTTAACGACTTCTGGAGA
ATGGTCTGGGAGCAAAAGTCTGCGACCATCGTCATGTTAACAAACTTGAAAGAAAGGAAA
GAGGAAAAGTGCCATCAGTACTGGCCCGACCAAGGCTGCTGGACCTATGGAAACATCCGG
GTGTGCGTGGAGGACTGCGTGGTTTTGGTCGACTACACCATCCGGAAGTTCTGCATACAG
CCACAGCTCCCCGACGGCTGCAAAGCCCCCAGGCTGGTCTCACAGCTGCACTTCACCAGC
TGGCCCGACTTCGGAGTGCCTTTTACCCCCATTGGGATGCTGAAGTTCCTCAAGAAAGTA
AAGACGCTCAACCCCGTGCACGCTGGGCCCATCGTGGTCCACTGTAGCGCGGGCGTGGGC
CGGACGGGCACCTTCATTGTGATCGATGCCATGATGGCCATGATGCACGCGGAGCAGAAG
GTGGATGTGTTTGAATTTGTGTCTCGAATCCGTAATCAGCGCCCTCAGATGGTTCAAACG
GATATGCAGTACACGTTCATCTACCAAGCCTTACTCGAGTACTACCTCTACGGGGACACA
GAGCTGGACGTGTCCTCCCTGGAGAAGCACCTGCAGACCATGCACGGCACCACCACCCAC
TTCGACAAGATCGGGCTGGAGGAGGAGTTCAGGAAATTGACAAATGTCCGGATCATGAAG
GAGAACATGAGGACGGGCAACTTGCCGGCAAACATGAAGAAGGCCAGGGTCATCCAGATC
ATCCCGTATGACTTCAACCGAGTGATCCTTTCCATGAAAAGGGGTCAAGAATACACAGAC
TACATCAACGCATCCTTCATAGACGGCTACCGACAGAAGGACTATTTCATCGCCACCCAG
GGGCCACTGGCACACACGGTTGAGGACTTCTGGAGGATGATCTGGGAATGGAAATCCCAC
ACTATCGTGATGCTGACGGAGGTGCAGGAGAGAGAGCAGGATAAATGCTACCAGTATTGG
CCAACCGAGGGCTCAGTTACTCATGGAGAAATAACGATTGAGATAAAGAATGATACCCTT
TCAGAAGCCATCAGTATACGAGACTTTCTGGTCACTCTCAATCAGCCCCAGGCCCGCCAG
GAGGAGCAGGTCCGAGTAGTGCGCCAGTTTCACTTCCACGGCTGGCCTGAGATCGGGATT
CCCGCCGAGGGCAAAGGCATGATTGACCTCATCGCAGCCGTGCAGAAGCAGCAGCAGCAG
ACAGGCAACCACCCCATCACCGTGCACTGCAGTGCCGGAGCTGGGCGAACAGGTACATTC
ATAGCCCTCAGCAACATTTTGGAGCGAGTAAAAGCCGAGGGACTTTTAGATGTATTTCAA
GCTGTGAAGAGTTTACGACTTCAGAGACCACATATGGTGCAAACCCTGGAACAGTATGAA
TTCTGCTACAAAGTGGTACAAGATTTTATTGATATATTTTCTGATTATGCTAATTTCAAA
TGA
Chromosome Location
10
Locus
10q26
External Identifiers
ResourceLink
UniProtKB IDP23469
UniProtKB Entry NamePTPRE_HUMAN
GenBank Protein ID35792
GenBank Gene IDX54134
HGNC IDHGNC:9669
General References
  1. Krueger NX, Streuli M, Saito H: Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J. 1990 Oct;9(10):3241-52. [Article]
  2. Wabakken T, Hauge H, Finne EF, Wiedlocha A, Aasheim H: Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase. Scand J Immunol. 2002 Aug;56(2):195-203. [Article]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
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  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  6. Elson A, Leder P: Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon. Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):12235-9. [Article]
  7. Schmidt A, Rutledge SJ, Endo N, Opas EE, Tanaka H, Wesolowski G, Leu CT, Huang Z, Ramachandaran C, Rodan SB, Rodan GA: Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate. Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):3068-73. [Article]
  8. Tanuma N, Nakamura K, Kikuchi K: Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation. Eur J Biochem. 1999 Jan;259(1-2):46-54. [Article]
  9. Gil-Henn H, Volohonsky G, Toledano-Katchalski H, Gandre S, Elson A: Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control. Oncogene. 2000 Sep 7;19(38):4375-84. [Article]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00630Alendronic acidapprovedunknowninhibitorDetails
DB01133Tiludronic acidapproved, investigational, vet_approvedunknowninhibitorDetails