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Q06180

- PTN2_MOUSE

UniProt

Q06180 - PTN2_MOUSE

Protein

Tyrosine-protein phosphatase non-receptor type 2

Gene

Ptpn2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3, STAT5A, STAT5B and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T-cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Plays also an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. Finally, it negatively regulates prolactin-mediated signaling pathway through dephosphorylation of STAT5A and STAT5B. May also bind DNA.11 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei182 – 1821SubstrateBy similarity
    Active sitei216 – 2161Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei260 – 2601SubstrateBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. B cell differentiation Source: UniProtKB
    2. erythrocyte differentiation Source: UniProtKB
    3. glucose homeostasis Source: UniProtKB
    4. insulin receptor signaling pathway Source: MGI
    5. negative regulation of cell proliferation Source: UniProtKB
    6. negative regulation of chemotaxis Source: UniProtKB
    7. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    8. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
    9. negative regulation of inflammatory response Source: UniProtKB
    10. negative regulation of insulin receptor signaling pathway Source: UniProtKB
    11. negative regulation of interferon-gamma-mediated signaling pathway Source: UniProtKB
    12. negative regulation of interleukin-2-mediated signaling pathway Source: UniProtKB
    13. negative regulation of interleukin-4-mediated signaling pathway Source: UniProtKB
    14. negative regulation of interleukin-6-mediated signaling pathway Source: UniProtKB
    15. negative regulation of lipid storage Source: UniProtKB
    16. negative regulation of macrophage colony-stimulating factor signaling pathway Source: UniProtKB
    17. negative regulation of macrophage differentiation Source: UniProtKB
    18. negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
    19. negative regulation of positive thymic T cell selection Source: UniProtKB
    20. negative regulation of prolactin signaling pathway Source: UniProtKB
    21. negative regulation of T cell receptor signaling pathway Source: UniProtKB
    22. negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
    23. negative regulation of type I interferon-mediated signaling pathway Source: UniProtKB
    24. negative regulation of tyrosine phosphorylation of Stat1 protein Source: UniProtKB
    25. negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
    26. negative regulation of tyrosine phosphorylation of Stat5 protein Source: UniProtKB
    27. negative regulation of tyrosine phosphorylation of Stat6 protein Source: UniProtKB
    28. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    29. positive regulation of gluconeogenesis Source: UniProtKB
    30. protein dephosphorylation Source: MGI
    31. regulation of hepatocyte growth factor receptor signaling pathway Source: UniProtKB
    32. T cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_198645. Regulation of IFNG signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 2 (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase PTP-2
    Alternative name(s):
    MPTP
    Gene namesi
    Name:Ptpn2
    Synonyms:Ptpt
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:97806. Ptpn2.

    Subcellular locationi

    Isoform 1 : Endoplasmic reticulum By similarity. Endoplasmic reticulum-Golgi intermediate compartment By similarity
    Note: Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region.By similarity
    Isoform 2 : Nucleus By similarity. Cytoplasm By similarity. Cell membrane By similarity
    Note: Predominantly localizes to chromatin. Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors. Recruited by activated ITGA1 at the plasma membrane By similarity.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Newborn mice are viable and do not display physical abnormalities. However, by 3 to 5 weeks of age they develop hunched posture, diarrhea and anemia. They do not survive beyond 5 weeks of age due to severe anemia, hematopoietic defects and the development of progressive systemic inflammatory disease. They display splenomegaly, lymphadenopathy and thymic atrophy, associated with altered B-cell differentiation, altered erythropoiesis, and impaired T- and B-cell functions. The inflammatory disease is characterized by high levels of circulating proinflammatory cytokines and lymphocytic infiltrates in non-lymphoid tissues. Heterozygous Ptpn2+/- mice exhibit decreased gluconeogenesis and hepatic glucose production while muscle-specific disruption of Ptpn2 has no effect on insulin signaling and glucose homeostasis in this tissue.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi182 – 1821D → A: Substrate-trapping mutant; catalytically inactive it forms a stable complex with physiological substrates including STAT5.
    Mutagenesisi216 – 2161C → S: Catalytically inactive. Unable to restore phosphatase activity toward PDGFRB. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Tyrosine-protein phosphatase non-receptor type 2PRO_0000094753Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei298 – 2981PhosphoserineBy similarity
    Modified residuei304 – 3041Phosphoserine; by CDK1 and CDK2; in isoform 2By similarity

    Post-translational modificationi

    Isoform 2: Specifically phosphorylated in a cell cycle-dependent manner by cyclin-dependent kinases. Probably activated through phosphorylation by PKR By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ06180.
    PRIDEiQ06180.

    PTM databases

    PhosphoSiteiQ06180.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. The highest expression levels were found in ovary, testis, thymus and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ06180.
    BgeeiQ06180.
    CleanExiMM_PTPN2.
    GenevestigatoriQ06180.

    Interactioni

    Subunit structurei

    Interacts with RMDN3. Isoform 1 interacts with TMED9. Isoform 1 interacts with STX17; dephosphorylates STX17. Interacts with ITGA1 (via cytoplasmic domain); activates the phosphatase activity towards EGFR. Interacts with TRAF2; probably involved in tumor necrosis factor-mediated signaling. Interacts with MET By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ06180. 2 interactions.
    MINTiMINT-5170362.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06180.
    SMRiQ06180. Positions 5-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 275271Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni216 – 2227Substrate bindingBy similarity
    Regioni341 – 40666Endoplasmic reticulum locationBy similarityAdd
    BLAST
    Regioni371 – 40636Mediates interaction with STX17By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00750000117312.
    HOGENOMiHOG000273908.
    HOVERGENiHBG008321.
    InParanoidiQ06180.
    KOiK18026.
    OMAiNTAQKVQ.
    PhylomeDBiQ06180.
    TreeFamiTF315897.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR012265. Ptpn1/Ptpn2.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q06180-1) [UniParc]FASTAAdd to Basket

    Also known as: PTPB, TC-PTPb

    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

    MSATIEREFE ELDAQCRWQP LYLEIRNESH DYPHRVAKFP ENRNRNRYRD    50
    VSPYDHSRVK LQSTENDYIN ASLVDIEEAQ RSYILTQGPL PNTCCHFWLM 100
    VWQQKTKAVV MLNRTVEKES VKCAQYWPTD DREMVFKETG FSVKLLSEDV 150
    KSYYTVHLLQ LENINTGETR TISHFHYTTW PDFGVPESPA SFLNFLFKVR 200
    ESGCLTPDHG PAVIHCSAGI GRSGTFSLVD TCLVLMEKGE DVNVKQLLLN 250
    MRKYRMGLIQ TPDQLRFSYM AIIEGAKYTK GDSNIQKRWK ELSKEDLSPI 300
    CDHSQNRVMV EKYNGKRIGS EDEKLTGLPS KVQDTVEESS ESILRKRIRE 350
    DRKATTAQKV QQMKQRLNET ERKRKRWLYW QPILTKMGFV SVILVGALVG 400
    WTLLFH 406
    Length:406
    Mass (Da):47,360
    Last modified:January 4, 2005 - v2
    Checksum:iDFB881DF3C800DC3
    GO
    Isoform 2 (identifier: Q06180-2) [UniParc]FASTAAdd to Basket

    Also known as: PTPA, TC-PTPa

    The sequence of this isoform differs from the canonical sequence as follows:
         377-406: WLYWQPILTKMGFVSVILVGALVGWTLLFH → PRLTDT

    Show »
    Length:382
    Mass (Da):44,573
    Checksum:iBFE174ABC0963929
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei377 – 40630WLYWQ…TLLFH → PRLTDT in isoform 2. 2 PublicationsVSP_012367Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81477 mRNA. Translation: AAA37446.1.
    S52655 mRNA. Translation: AAB25035.2.
    BC008269 mRNA. Translation: AAH08269.1.
    AK076072 mRNA. Translation: BAC36163.1.
    AK132013 mRNA. Translation: BAE20939.1.
    CCDSiCCDS37851.1. [Q06180-2]
    CCDS50311.1. [Q06180-1]
    PIRiA38191.
    RefSeqiNP_001120649.1. NM_001127177.1. [Q06180-1]
    NP_033003.1. NM_008977.3. [Q06180-2]
    UniGeneiMm.260433.

    Genome annotation databases

    EnsembliENSMUST00000025420; ENSMUSP00000025420; ENSMUSG00000024539. [Q06180-2]
    ENSMUST00000122412; ENSMUSP00000112675; ENSMUSG00000024539. [Q06180-1]
    GeneIDi19255.
    KEGGimmu:19255.
    UCSCiuc008fmu.2. mouse. [Q06180-2]
    uc008fmv.2. mouse. [Q06180-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81477 mRNA. Translation: AAA37446.1 .
    S52655 mRNA. Translation: AAB25035.2 .
    BC008269 mRNA. Translation: AAH08269.1 .
    AK076072 mRNA. Translation: BAC36163.1 .
    AK132013 mRNA. Translation: BAE20939.1 .
    CCDSi CCDS37851.1. [Q06180-2 ]
    CCDS50311.1. [Q06180-1 ]
    PIRi A38191.
    RefSeqi NP_001120649.1. NM_001127177.1. [Q06180-1 ]
    NP_033003.1. NM_008977.3. [Q06180-2 ]
    UniGenei Mm.260433.

    3D structure databases

    ProteinModelPortali Q06180.
    SMRi Q06180. Positions 5-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q06180. 2 interactions.
    MINTi MINT-5170362.

    PTM databases

    PhosphoSitei Q06180.

    Proteomic databases

    PaxDbi Q06180.
    PRIDEi Q06180.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025420 ; ENSMUSP00000025420 ; ENSMUSG00000024539 . [Q06180-2 ]
    ENSMUST00000122412 ; ENSMUSP00000112675 ; ENSMUSG00000024539 . [Q06180-1 ]
    GeneIDi 19255.
    KEGGi mmu:19255.
    UCSCi uc008fmu.2. mouse. [Q06180-2 ]
    uc008fmv.2. mouse. [Q06180-1 ]

    Organism-specific databases

    CTDi 5771.
    MGIi MGI:97806. Ptpn2.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00750000117312.
    HOGENOMi HOG000273908.
    HOVERGENi HBG008321.
    InParanoidi Q06180.
    KOi K18026.
    OMAi NTAQKVQ.
    PhylomeDBi Q06180.
    TreeFami TF315897.

    Enzyme and pathway databases

    Reactomei REACT_198645. Regulation of IFNG signaling.

    Miscellaneous databases

    NextBioi 296100.
    PROi Q06180.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06180.
    Bgeei Q06180.
    CleanExi MM_PTPN2.
    Genevestigatori Q06180.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR012265. Ptpn1/Ptpn2.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000926. Tyr-Ptase_nr1. 1 hit.
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase."
      Mosinger B. Jr., Tillmann U., Westphal H., Tremblay M.L.
      Proc. Natl. Acad. Sci. U.S.A. 89:499-503(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Molecular cloning, nucleotide sequence and expression of a cDNA encoding an intracellular protein tyrosine phosphatase, PTPase-2, from mouse testis and T-cells."
      Miyasaka H., Li S.S.-L.
      Mol. Cell. Biochem. 118:91-98(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/6N.
      Tissue: T-cell and Testis.
    3. "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 1).
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Mammary gland.
    5. "Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice."
      You-Ten K.E., Muise E.S., Itie A., Michaliszyn E., Wagner J., Jothy S., Lapp W.S., Tremblay M.L.
      J. Exp. Med. 186:683-693(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN IMMUNE SYSTEM DEVELOPMENT, TISSUE SPECIFICITY.
    6. "Murine embryonic fibroblasts lacking TC-PTP display delayed G1 phase through defective NF-kappaB activation."
      Ibarra-Sanchez M.J., Wagner J., Ong M.T., Lampron C., Tremblay M.L.
      Oncogene 20:4728-4739(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PDGF SIGNALING.
    7. "The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3."
      Simoncic P.D., Lee-Loy A., Barber D.L., Tremblay M.L., McGlade C.J.
      Curr. Biol. 12:446-453(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOKINE SIGNALING.
    8. Cited for: FUNCTION IN DEPHOSPHORYLATION OF STAT1.
    9. "A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus."
      Aoki N., Matsuda T.
      Mol. Endocrinol. 16:58-69(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF STAT5A AND STAT5B.
    10. "T-cell protein tyrosine phosphatase deletion results in progressive systemic inflammatory disease."
      Heinonen K.M., Nestel F.P., Newell E.W., Charette G., Seemayer T.A., Tremblay M.L., Lapp W.S.
      Blood 103:3457-3464(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    11. "Site-selective regulation of platelet-derived growth factor beta receptor tyrosine phosphorylation by T-cell protein tyrosine phosphatase."
      Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B., Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H., Roennstrand L., Ostman A., Hellberg C.
      Mol. Cell. Biol. 24:2190-2201(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF PDGFRB, MUTAGENESIS OF CYS-216.
    12. "Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase."
      van Vliet C., Bukczynska P.E., Puryer M.A., Sadek C.M., Shields B.J., Tremblay M.L., Tiganis T.
      Nat. Immunol. 6:253-260(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TUMOR NECROSIS FACTOR SIGNALING.
    13. "T-cell protein tyrosine phosphatase (Tcptp) is a negative regulator of colony-stimulating factor 1 signaling and macrophage differentiation."
      Simoncic P.D., Bourdeau A., Lee-Loy A., Rohrschneider L.R., Tremblay M.L., Stanley E.R., McGlade C.J.
      Mol. Cell. Biol. 26:4149-4160(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF CSF1R.
    14. "T-cell protein tyrosine phosphatase, distinctively expressed in activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of STAT6."
      Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T., Lossos I.S.
      Mol. Cell. Biol. 27:2166-2179(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF STAT6.
    15. "T-cell protein tyrosine phosphatase attenuates STAT3 and insulin signaling in the liver to regulate gluconeogenesis."
      Fukushima A., Loh K., Galic S., Fam B., Shields B., Wiede F., Tremblay M.L., Watt M.J., Andrikopoulos S., Tiganis T.
      Diabetes 59:1906-1914(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN GLUCOSE HOMEOSTASIS, TISSUE SPECIFICITY.
    16. "T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice."
      Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C., Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.
      J. Clin. Invest. 121:4758-4774(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN T-CELL RECEPTOR SIGNALING.
    17. "T cell protein tyrosine phosphatase (TCPTP) deficiency in muscle does not alter insulin signalling and glucose homeostasis in mice."
      Loh K., Merry T.L., Galic S., Wu B.J., Watt M.J., Zhang S., Zhang Z.Y., Neel B.G., Tiganis T.
      Diabetologia 55:468-478(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiPTN2_MOUSE
    AccessioniPrimary (citable) accession number: Q06180
    Secondary accession number(s): Q3V259, Q922E7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 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