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Q06180

- PTN2_MOUSE

UniProt

Q06180 - PTN2_MOUSE

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Protein
Tyrosine-protein phosphatase non-receptor type 2
Gene
Ptpn2, Ptpt
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. Beside 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei182 – 1821Substrate By similarity
Active sitei216 – 2161Phosphocysteine intermediate By similarity
Binding sitei260 – 2601Substrate By 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. T cell differentiation Source: UniProtKB
  3. erythrocyte differentiation Source: UniProtKB
  4. glucose homeostasis Source: UniProtKB
  5. insulin receptor signaling pathway Source: MGI
  6. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  7. negative regulation of T cell receptor signaling pathway Source: UniProtKB
  8. negative regulation of cell proliferation Source: UniProtKB
  9. negative regulation of chemotaxis Source: UniProtKB
  10. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  11. negative regulation of inflammatory response Source: UniProtKB
  12. negative regulation of insulin receptor signaling pathway Source: UniProtKB
  13. negative regulation of interferon-gamma-mediated signaling pathway Source: UniProtKB
  14. negative regulation of interleukin-2-mediated signaling pathway Source: UniProtKB
  15. negative regulation of interleukin-4-mediated signaling pathway Source: UniProtKB
  16. negative regulation of interleukin-6-mediated signaling pathway Source: UniProtKB
  17. negative regulation of lipid storage Source: UniProtKB
  18. negative regulation of macrophage colony-stimulating factor signaling pathway Source: UniProtKB
  19. negative regulation of macrophage differentiation Source: UniProtKB
  20. negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  21. negative regulation of positive thymic T cell selection Source: UniProtKB
  22. negative regulation of prolactin signaling pathway Source: UniProtKB
  23. negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
  24. negative regulation of type I interferon-mediated signaling pathway Source: UniProtKB
  25. negative regulation of tyrosine phosphorylation of Stat1 protein Source: UniProtKB
  26. negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  27. negative regulation of tyrosine phosphorylation of Stat5 protein Source: UniProtKB
  28. negative regulation of tyrosine phosphorylation of Stat6 protein Source: UniProtKB
  29. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  30. positive regulation of gluconeogenesis Source: UniProtKB
  31. protein dephosphorylation Source: MGI
  32. regulation of hepatocyte growth factor receptor signaling pathway Source: UniProtKB
Complete GO annotation...

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.

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
Complete GO annotation...

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 2
PRO_0000094753Add
BLAST

Amino acid modifications

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

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.

Protein-protein interaction databases

IntActiQ06180. 2 interactions.
MINTiMINT-5170362.

Structurei

3D structure databases

ProteinModelPortaliQ06180.
SMRiQ06180. Positions 5-277.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 275271Tyrosine-protein phosphatase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni216 – 2227Substrate binding By similarity
Regioni341 – 40666Endoplasmic reticulum location By similarity
Add
BLAST
Regioni371 – 40636Mediates interaction with STX17 By similarity
Add
BLAST

Sequence similaritiesi

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.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 130 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

Similar proteinsi