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P49446

- PTPRE_MOUSE

UniProt

P49446 - PTPRE_MOUSE

Protein

Receptor-type tyrosine-protein phosphatase epsilon

Gene

Ptpre

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (15 Dec 2009)
      Previous versions | rss
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    Functioni

    Isoform 1 acts as a negative regulator of insulin receptor (IR) signaling and is involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver By similarity. 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.
    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 Ca2+.

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    Isoform 1 is inhibited by alendronate (ALN), orthovanadate, and phenylarsine oxide (PAO).1 Publication

    Kineticsi

    1. KM=70 µM for fluorescein diphosphate (isoform 1)1 Publication

    Vmax=6 µmol/min/mg enzyme for fluorescein diphosphate (isoform 1)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei302 – 3021SubstrateBy similarity
    Active sitei334 – 3341Phosphocysteine intermediateBy similarity
    Binding sitei378 – 3781SubstrateBy similarity
    Active sitei629 – 6291Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. protein homodimerization activity Source: MGI
    2. protein tyrosine phosphatase activity Source: MGI

    GO - Biological processi

    1. negative regulation of insulin receptor signaling pathway Source: UniProtKB
    2. peptidyl-tyrosine dephosphorylation Source: GOC
    3. regulation of mast cell activation Source: UniProtKB
    4. transmembrane receptor protein tyrosine phosphatase signaling pathway Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase epsilon (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase epsilon
    Short name:
    R-PTP-epsilon
    Gene namesi
    Name:Ptpre
    Synonyms:Ptpe
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:97813. Ptpre.

    Subcellular locationi

    Isoform 2 : Cytoplasm
    Note: Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin can induce translocation to the membrane.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW
    3. intermediate filament cytoskeleton Source: Ensembl
    4. nucleus Source: Ensembl
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice show greater insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1) in the skeletal muscle. Antigen- and IgE-mediated passive systemic anaphylactic reactions are enhanced. Erythrocytes exhibit abnormal morphology, increased Ca2+-activated-K+ channel activity and marked perturbation of the erythrocyte membrane tyrosine phosphoproteome.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 699680Receptor-type tyrosine-protein phosphatase epsilonPRO_0000025440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi23 – 231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis
    Modified residuei695 – 6951Phosphotyrosine2 Publications

    Post-translational modificationi

    A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3.1 Publication
    Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu.By similarity
    Isoform 1 is glycosylated.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP49446.
    PRIDEiP49446.

    PTM databases

    PhosphoSiteiP49446.

    Expressioni

    Tissue specificityi

    Isoform 2 is expressed in the spleen and thymus (at protein level). Detected in fibroblasts, myeloid cells, macrophages, and T-cells but not in B-cell lines. Isoform 1 and isoform 2 are expressed predominantly in the brain, testes, and lungs, with lower levels present in lymph nodes, thymus, spleen, heart and mammary glands. Isoform 1 is expressed in osteoclasts and not in osteoblasts and its expression is related to osteoclast differentiation. It is also expressed in the erythrocytes. Isoform 2 is strongly expressed in skeletal muscle and L6 skeletal muscle cell line.5 Publications

    Inductioni

    Isoform 2 is induced by 12-O-tetradecanoylphorbol-13-acetate (TPA) and its induction is dependent upon PKC activity.1 Publication

    Gene expression databases

    BgeeiP49446.
    CleanExiMM_PTPRE.
    GenevestigatoriP49446.

    Interactioni

    Subunit structurei

    Monomer By similarity. Isoform 2: Homodimer. Can form oligomers. Dimerization is increased by oxidative stress and decreased by EGFR. Isoform 2 interacts with GRB2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202496. 1 interaction.
    IntActiP49446. 6 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP49446.
    SMRiP49446. Positions 110-690.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 4526ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini69 – 699631CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei46 – 6823HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 393260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini425 – 688264Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni334 – 3407Substrate bindingBy similarity

    Domaini

    The tyrosine-protein phosphatase 2 domain (D2) mediates dimerization. The extreme N- and C- termini of the D2 domain act to inhibit dimerization and removal of these sequences increases dimerization and inhibits enzyme activity.1 Publication

    Sequence similaritiesi

    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00590000082937.
    HOVERGENiHBG053758.
    InParanoidiQ61042.
    KOiK18033.
    OMAiIVIDAMI.
    OrthoDBiEOG7B31M8.
    PhylomeDBiP49446.
    TreeFamiTF351829.

    Family and domain databases

    Gene3Di3.90.190.10. 2 hits.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    IPR016336. Tyr_Pase_rcpt_a/e-type.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PIRSFiPIRSF002006. PTPR_alpha_epsilon. 1 hit.
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 2 hits.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative promoter usage and alternative initiation. Align

    Isoform 1 (identifier: P49446-1) [UniParc]FASTAAdd to Basket

    Also known as: PTPeM, RPTPe, tm-PTPe

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEPFCPLLLA SFSLSLARAG QGNDTTPTES NWTSTTAGPP DPGASQPLLT    50
    WLLLPLLLLL FLLAAYFFRF RKQRKAVVSS NDKKMPNGIL EEQEQQRVML 100
    LSRSPSGPKK FFPIPVEHLE EEIRVRSADD CKRFREEFNS LPSGHIQGTF 150
    ELANKEENRE KNRYPNILPN DHCRVILSQV DGIPCSDYIN ASYIDGYKEK 200
    NKFIAAQGPK QETVNDFWRM VWEQRSATIV MLTNLKERKE EKCYQYWPDQ 250
    GCWTYGNIRV CVEDCVVLVD YTIRKFCIHP QLPDSCKAPR LVSQLHFTSW 300
    PDFGVPFTPI GMLKFLKKVK TLNPSHAGPI VVHCSAGVGR TGTFIVIDAM 350
    MDMIHSEQKV DVFEFVSRIR NQRPQMVQTD VQYTFIYQAL LEYYLYGDTE 400
    LDVSSLERHL QTLHSTATHF DKIGLEEEFR KLTNVRIMKE NMRTGNLPAN 450
    MKKARVIQII PYDFNRVILS MKRGQEFTDY INASFIDGYR QKDYFMATQG 500
    PLAHTVEDFW RMVWEWKSHT IVMLTEVQER EQDKCYQYWP TEGSVTHGDI 550
    TIEIKSDTLS EAISVRDFLV TFKQPLARQE EQVRMVRQFH FHGWPEVGIP 600
    AEGKGMIDLI AAVQKQQQQT GNHPITVHCS AGAGRTGTFI ALSNILERVK 650
    AEGLLDVFQA VKSLRLQRPH MVQTLEQYEF CYKVVQDFID IFSDYANFK 699

    Note: Produced by alternative promoter usage.

    Length:699
    Mass (Da):80,688
    Last modified:December 15, 2009 - v3
    Checksum:i581EF9CB881BC05B
    GO
    Isoform 2 (identifier: P49446-2) [UniParc]FASTAAdd to Basket

    Also known as: PTPeC, cyt-PTPe

    The sequence of this isoform differs from the canonical sequence as follows:
         1-69: MEPFCPLLLA...LFLLAAYFFR → MSSRKNFSRLTW

    Note: Produced by alternative promoter usage.

    Show »
    Length:642
    Mass (Da):74,735
    Checksum:i92F99E9729D8F1F3
    GO
    Isoform 3 (identifier: P49446-3) [UniParc]FASTAAdd to Basket

    Also known as: p67

    The sequence of this isoform differs from the canonical sequence as follows:
         1-84: Missing.

    Note: Produced by alternative initiation at Met-85 of isoform 1.

    Show »
    Length:615
    Mass (Da):71,467
    Checksum:i56E0BE70BB2BB59C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371E → K in BAE32920. (PubMed:16141072)Curated
    Sequence conflicti500 – 5001G → A in BAA11927. 1 PublicationCurated
    Sequence conflicti506 – 5061V → G in AAC52281. (PubMed:7592814)Curated
    Sequence conflicti506 – 5061V → G in AAC52331. (PubMed:8618876)Curated
    Sequence conflicti506 – 5061V → G in AAB04553. 1 PublicationCurated
    Sequence conflicti521 – 5222IV → ML in BAA11927. 1 PublicationCurated
    Sequence conflicti606 – 6061M → I in AAC52281. (PubMed:7592814)Curated
    Sequence conflicti606 – 6061M → I in AAC52331. (PubMed:8618876)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8484Missing in isoform 3. CuratedVSP_038491Add
    BLAST
    Alternative sequencei1 – 6969MEPFC…AYFFR → MSSRKNFSRLTW in isoform 2. 2 PublicationsVSP_038492Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35368 mRNA. Translation: AAC52281.1.
    U36758 mRNA. Translation: AAC52331.1.
    U40280 mRNA. Translation: AAB02190.1.
    D83484 mRNA. Translation: BAA11927.1.
    U62387 mRNA. Translation: AAB04553.1.
    AK154910 mRNA. Translation: BAE32920.1.
    CH466531 Genomic DNA. Translation: EDL17805.1.
    CH466531 Genomic DNA. Translation: EDL17807.1.
    Z23052 mRNA. Translation: CAA80587.1.
    Z23053 mRNA. Translation: CAA80588.1.
    CCDSiCCDS21944.1. [P49446-1]
    PIRiB61180.
    JC6132.
    S40284.
    RefSeqiNP_035342.3. NM_011212.3. [P49446-1]
    XP_006507522.1. XM_006507459.1. [P49446-1]
    XP_006507523.1. XM_006507460.1. [P49446-1]
    XP_006507524.1. XM_006507461.1. [P49446-2]
    UniGeneiMm.945.

    Genome annotation databases

    EnsembliENSMUST00000073961; ENSMUSP00000073616; ENSMUSG00000041836. [P49446-1]
    GeneIDi19267.
    KEGGimmu:19267.
    UCSCiuc009kee.1. mouse. [P49446-1]
    uc009kek.1. mouse. [P49446-2]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35368 mRNA. Translation: AAC52281.1 .
    U36758 mRNA. Translation: AAC52331.1 .
    U40280 mRNA. Translation: AAB02190.1 .
    D83484 mRNA. Translation: BAA11927.1 .
    U62387 mRNA. Translation: AAB04553.1 .
    AK154910 mRNA. Translation: BAE32920.1 .
    CH466531 Genomic DNA. Translation: EDL17805.1 .
    CH466531 Genomic DNA. Translation: EDL17807.1 .
    Z23052 mRNA. Translation: CAA80587.1 .
    Z23053 mRNA. Translation: CAA80588.1 .
    CCDSi CCDS21944.1. [P49446-1 ]
    PIRi B61180.
    JC6132.
    S40284.
    RefSeqi NP_035342.3. NM_011212.3. [P49446-1 ]
    XP_006507522.1. XM_006507459.1. [P49446-1 ]
    XP_006507523.1. XM_006507460.1. [P49446-1 ]
    XP_006507524.1. XM_006507461.1. [P49446-2 ]
    UniGenei Mm.945.

    3D structure databases

    ProteinModelPortali P49446.
    SMRi P49446. Positions 110-690.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202496. 1 interaction.
    IntActi P49446. 6 interactions.

    PTM databases

    PhosphoSitei P49446.

    Proteomic databases

    PaxDbi P49446.
    PRIDEi P49446.

    Protocols and materials databases

    DNASUi 19267.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000073961 ; ENSMUSP00000073616 ; ENSMUSG00000041836 . [P49446-1 ]
    GeneIDi 19267.
    KEGGi mmu:19267.
    UCSCi uc009kee.1. mouse. [P49446-1 ]
    uc009kek.1. mouse. [P49446-2 ]

    Organism-specific databases

    CTDi 5791.
    MGIi MGI:97813. Ptpre.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00590000082937.
    HOVERGENi HBG053758.
    InParanoidi Q61042.
    KOi K18033.
    OMAi IVIDAMI.
    OrthoDBi EOG7B31M8.
    PhylomeDBi P49446.
    TreeFami TF351829.

    Miscellaneous databases

    ChiTaRSi PTPRE. mouse.
    NextBioi 296146.
    PROi P49446.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49446.
    CleanExi MM_PTPRE.
    Genevestigatori P49446.

    Family and domain databases

    Gene3Di 3.90.190.10. 2 hits.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    IPR016336. Tyr_Pase_rcpt_a/e-type.
    [Graphical view ]
    Pfami PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF002006. PTPR_alpha_epsilon. 1 hit.
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 2 hits.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras OR neu."
      Elson A., Leder P.
      J. Biol. Chem. 270:26116-26122(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: FVB/N.
    2. "Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon."
      Elson A., Leder P.
      Proc. Natl. Acad. Sci. U.S.A. 92:12235-12239(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY.
    3. "Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate."
      Schmidt A., Rutledge S.J., Endo N., Opas E., Tanaka H., Wesolowski G., Leu C.T., Huang Z., Ramachandaran C., Rodan S.B., Rodan G.A.
      Proc. Natl. Acad. Sci. U.S.A. 93:3068-3073(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.
      Tissue: Osteoclast.
    4. Mukouyama Y.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: DBA/2.
    5. Hou E.W., Li S.L.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain and Lung.
    6. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: NOD.
    7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "Identification and typing of members of the protein-tyrosine phosphatase gene family expressed in mouse brain."
      Schepens J., Zeeuwen P., Wieringa B., Hendriks W.
      Mol. Biol. Rep. 16:241-248(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
      Strain: BALB/c.
      Tissue: Brain.
    9. "Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
      Yi T., Cleveland J.L., Ihle J.N.
      Blood 78:2222-2228(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Myeloid leukemia cell.
    10. "A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain."
      Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.
      Biochem. J. 305:499-504(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
      Strain: BALB/c.
      Tissue: Brain.
    11. "Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation."
      Tanuma N., Nakamura K., Kikuchi K.
      Eur. J. Biochem. 259:46-54(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE.
    12. "Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control."
      Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S., Elson A.
      Oncogene 19:4375-4384(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORM 3), ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    13. "Dimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilon."
      Toledano-Katchalski H., Tiran Z., Sines T., Shani G., Granot-Attas S., den Hertog J., Elson A.
      Mol. Cell. Biol. 23:5460-5471(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, DOMAIN.
    14. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    15. "Cytosolic protein tyrosine phosphatase-epsilon is a negative regulator of insulin signaling in skeletal muscle."
      Aga-Mizrachi S., Brutman-Barazani T., Jacob A.I., Bak A., Elson A., Sampson S.R.
      Endocrinology 149:605-614(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    16. "PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells."
      De Franceschi L., Biondani A., Carta F., Turrini F., Laudanna C., Deana R., Brunati A.M., Turretta L., Iolascon A., Perrotta S., Elson A., Bulato C., Brugnara C.
      Proteomics 8:4695-4708(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 1), DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    17. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Protein tyrosine phosphatase epsilon is a negative regulator of FcepsilonRI-mediated mast cell responses."
      Akimoto M., Mishra K., Lim K.-T., Tani N., Hisanaga S.-I., Katagiri T., Elson A., Mizuno K., Yakura H.
      Scand. J. Immunol. 69:401-411(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiPTPRE_MOUSE
    AccessioniPrimary (citable) accession number: P49446
    Secondary accession number(s): Q3U369
    , Q60986, Q61042, Q62134, Q62444, Q64496
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3