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P17706

- PTN2_HUMAN

UniProt

P17706 - PTN2_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 2

Gene

PTPN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      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.9 Publications

    Catalytic activityi

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

    Kineticsi

    1. KM=0.48 mM for p-nitrophenyl phosphate (at pH 6.5 and 25 degrees Celsius)1 Publication

    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. integrin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB
    4. protein tyrosine phosphatase activity Source: UniProtKB
    5. receptor tyrosine kinase binding Source: UniProtKB
    6. syntaxin binding Source: UniProtKB

    GO - Biological processi

    1. B cell differentiation Source: UniProtKB
    2. cytokine-mediated signaling pathway Source: Reactome
    3. erythrocyte differentiation Source: UniProtKB
    4. glucose homeostasis Source: UniProtKB
    5. insulin receptor signaling pathway Source: UniProtKB
    6. interferon-gamma-mediated signaling pathway Source: Reactome
    7. negative regulation of cell proliferation Source: UniProtKB
    8. negative regulation of chemotaxis Source: UniProtKB
    9. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    10. negative regulation of ERK1 and ERK2 cascade 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: Ensembl
    16. negative regulation of interleukin-6-mediated signaling pathway Source: Ensembl
    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 T cell receptor signaling pathway Source: UniProtKB
    24. negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
    25. negative regulation of type I interferon-mediated signaling pathway Source: UniProtKB
    26. negative regulation of tyrosine phosphorylation of Stat1 protein Source: UniProtKB
    27. negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
    28. negative regulation of tyrosine phosphorylation of Stat5 protein Source: UniProtKB
    29. negative regulation of tyrosine phosphorylation of Stat6 protein Source: Ensembl
    30. peptidyl-tyrosine dephosphorylation Source: GOC
    31. positive regulation of gluconeogenesis Source: UniProtKB
    32. regulation of hepatocyte growth factor receptor signaling pathway Source: UniProtKB
    33. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
    34. T cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_24980. Regulation of IFNG signaling.
    SignaLinkiP17706.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 2 (EC:3.1.3.48)
    Alternative name(s):
    T-cell protein-tyrosine phosphatase
    Short name:
    TCPTP
    Gene namesi
    Name:PTPN2
    Synonyms:PTPT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:9650. PTPN2.

    Subcellular locationi

    Isoform 1 : Endoplasmic reticulum 1 Publication. Endoplasmic reticulum-Golgi intermediate compartment 1 Publication
    Note: Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region.1 Publication
    Isoform 2 : Nucleus. Cytoplasm. Cell membrane
    Note: Predominantly localizes to chromatin By similarity. Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors (PubMed:9488479). Recruited by activated ITGA1 at the plasma membrane.By similarity1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi182 – 1821D → A: Substrate-trapping mutant; catalytically inactive it forms a stable complex with physiological substrates including INSR and EGFR. Accumulates in the cytoplasm upon stimulation by insulin or EGF; isoform 2. 2 Publications
    Mutagenesisi222 – 2221R → M: Impairs phosphatase activity.
    Mutagenesisi304 – 3041S → A: Alters phosphorylation by cyclin-dependent kinases of isoform 2 but has no effect on its phosphatase activity. 1 Publication
    Mutagenesisi350 – 3523RKR → QQQ: Alters location to the endoplasmic reticulum; isoform 1.
    Mutagenesisi380 – 3801K → Q: Prevents location to the nucleus; isoform 2. 1 Publication

    Organism-specific databases

    Orphaneti206. Crohn disease.
    85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    771. Ulcerative colitis.
    PharmGKBiPA33993.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 415415Tyrosine-protein phosphatase non-receptor type 2PRO_0000094752Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei298 – 2981Phosphoserine2 Publications
    Modified residuei304 – 3041Phosphoserine; by CDK1 and CDK2; in isoform 24 Publications

    Post-translational modificationi

    Isoform 2: Specifically phosphorylated in a cell cycle-dependent manner by cyclin-dependent kinases. Probably activated through phosphorylation by PKR.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP17706.
    PaxDbiP17706.
    PRIDEiP17706.

    PTM databases

    PhosphoSiteiP17706.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Isoform 2 is probably the major isoform. Isoform 1 is expressed in T-cells and in placenta.2 Publications

    Inductioni

    Up-regulated by IL4/interleukin-4 (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP17706.
    BgeeiP17706.
    CleanExiHS_PTPN2.
    GenevestigatoriP17706.

    Organism-specific databases

    HPAiHPA015004.
    HPA046176.

    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.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GHRP109128EBI-984930,EBI-286316
    TMED10P497555EBI-4409481,EBI-998422
    TMED9Q9BVK65EBI-4409481,EBI-1056827

    Protein-protein interaction databases

    BioGridi111737. 14 interactions.
    IntActiP17706. 14 interactions.
    MINTiMINT-3975566.
    STRINGi9606.ENSP00000311857.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 148
    Helixi19 – 2810
    Helixi35 – 384
    Helixi40 – 456
    Turni55 – 573
    Beta strandi58 – 603
    Beta strandi68 – 769
    Helixi77 – 793
    Beta strandi81 – 877
    Turni91 – 933
    Helixi94 – 10310
    Beta strandi108 – 1114
    Beta strandi129 – 1324
    Beta strandi134 – 1363
    Turni137 – 1404
    Beta strandi141 – 15010
    Beta strandi152 – 16312
    Turni164 – 1663
    Beta strandi169 – 1779
    Beta strandi182 – 1843
    Helixi190 – 20112
    Turni202 – 2054
    Beta strandi212 – 22110
    Helixi222 – 23514
    Beta strandi236 – 2394
    Helixi244 – 2518
    Turni252 – 2543
    Helixi262 – 27514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L8KX-ray2.56A1-314[»]
    ProteinModelPortaliP17706.
    SMRiP17706. Positions 5-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17706.

    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
    Regioni346 – 41570Endoplasmic reticulum locationAdd
    BLAST
    Regioni376 – 41540Mediates interaction with STX17Add
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000273908.
    HOVERGENiHBG008321.
    InParanoidiP17706.
    KOiK18026.
    OMAiNTAQKVQ.
    OrthoDBiEOG7RV9G4.
    PhylomeDBiP17706.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P17706-1) [UniParc]FASTAAdd to Basket

    Also known as: PTPB, p48TC, TC48, 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

    MPTTIEREFE ELDTQRRWQP LYLEIRNESH DYPHRVAKFP ENRNRNRYRD    50
    VSPYDHSRVK LQNAENDYIN ASLVDIEEAQ RSYILTQGPL PNTCCHFWLM 100
    VWQQKTKAVV MLNRIVEKES VKCAQYWPTD DQEMLFKETG FSVKLLSEDV 150
    KSYYTVHLLQ LENINSGETR TISHFHYTTW PDFGVPESPA SFLNFLFKVR 200
    ESGSLNPDHG PAVIHCSAGI GRSGTFSLVD TCLVLMEKGD DINIKQVLLN 250
    MRKYRMGLIQ TPDQLRFSYM AIIEGAKCIK GDSSIQKRWK ELSKEDLSPA 300
    FDHSPNKIMT EKYNGNRIGL EEEKLTGDRC TGLSSKMQDT MEENSESALR 350
    KRIREDRKAT TAQKVQQMKQ RLNENERKRK RWLYWQPILT KMGFMSVILV 400
    GAFVGWTLFF QQNAL 415

    Note: Minor isoform.

    Length:415
    Mass (Da):48,473
    Last modified:May 5, 2009 - v2
    Checksum:i0207694A4F058E68
    GO
    Isoform 2 (identifier: P17706-2) [UniParc]FASTAAdd to Basket

    Also known as: PTPA, p45TC, TC45, TC-PTPa

    The sequence of this isoform differs from the canonical sequence as follows:
         382-415: WLYWQPILTKMGFMSVILVGAFVGWTLFFQQNAL → PRLTDT

    Note: Major isoform. Contains a nuclear location signal at positions 377-381 (PubMed:7593185) and an autoinhibitory region acting through intramolecular interactions is found at positions 353-387.1 Publication

    Show »
    Length:387
    Mass (Da):45,168
    Checksum:i0F3E622EBA5A92CB
    GO
    Isoform 3 (identifier: P17706-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         347-380: Missing.
         382-415: WLYWQPILTKMGFMSVILVGAFVGWTLFFQQNAL → PRLTDT

    Note: No experimental confirmation available.

    Show »
    Length:353
    Mass (Da):40,990
    Checksum:i5AE668EB7D76CB93
    GO
    Isoform 4 (identifier: P17706-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         165-165: N → NYIENLWITLYLKLLMLDVKRSLK
         382-415: WLYWQPILTKMGFMSVILVGAFVGWTLFFQQNAL → PRLTDT

    Note: No experimental confirmation available. Gene prediction based on cDNA data.

    Show »
    Length:410
    Mass (Da):48,017
    Checksum:iD6463B9A0F952068
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti407 – 4071T → R in AAA65997. (PubMed:2546150)Curated
    Sequence conflicti407 – 4071T → R in M81478. (PubMed:1731319)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei165 – 1651N → NYIENLWITLYLKLLMLDVK RSLK in isoform 4. CuratedVSP_054821
    Alternative sequencei347 – 38034Missing in isoform 3. 1 PublicationVSP_043383Add
    BLAST
    Alternative sequencei382 – 41534WLYWQ…QQNAL → PRLTDT in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_005125Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25393 mRNA. Translation: AAA65997.1.
    AK292570 mRNA. Translation: BAF85259.1.
    EF445017 Genomic DNA. Translation: ACA06062.1.
    EF445017 Genomic DNA. Translation: ACA06064.1.
    AP001077 Genomic DNA. No translation available.
    AP002449 Genomic DNA. No translation available.
    AP005482 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01532.1.
    CH471113 Genomic DNA. Translation: EAX01539.1.
    BC008244 mRNA. Translation: AAH08244.1.
    BC016727 mRNA. Translation: AAH16727.1.
    M81478 mRNA. No translation available.
    CCDSiCCDS11863.1. [P17706-2]
    CCDS11864.1. [P17706-3]
    CCDS11865.1. [P17706-1]
    CCDS59306.1. [P17706-4]
    PIRiA33899.
    RefSeqiNP_001193942.1. NM_001207013.1. [P17706-4]
    NP_002819.2. NM_002828.3. [P17706-1]
    NP_536347.1. NM_080422.2. [P17706-2]
    NP_536348.1. NM_080423.2. [P17706-3]
    UniGeneiHs.654527.
    Hs.663373.

    Genome annotation databases

    EnsembliENST00000309660; ENSP00000311857; ENSG00000175354. [P17706-1]
    ENST00000327283; ENSP00000320298; ENSG00000175354. [P17706-2]
    ENST00000353319; ENSP00000320546; ENSG00000175354. [P17706-3]
    ENST00000591115; ENSP00000466936; ENSG00000175354. [P17706-4]
    GeneIDi5771.
    KEGGihsa:5771.
    UCSCiuc002krm.3. human. [P17706-3]
    uc002krp.3. human. [P17706-1]

    Polymorphism databases

    DMDMi229462762.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25393 mRNA. Translation: AAA65997.1 .
    AK292570 mRNA. Translation: BAF85259.1 .
    EF445017 Genomic DNA. Translation: ACA06062.1 .
    EF445017 Genomic DNA. Translation: ACA06064.1 .
    AP001077 Genomic DNA. No translation available.
    AP002449 Genomic DNA. No translation available.
    AP005482 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01532.1 .
    CH471113 Genomic DNA. Translation: EAX01539.1 .
    BC008244 mRNA. Translation: AAH08244.1 .
    BC016727 mRNA. Translation: AAH16727.1 .
    M81478 mRNA. No translation available.
    CCDSi CCDS11863.1. [P17706-2 ]
    CCDS11864.1. [P17706-3 ]
    CCDS11865.1. [P17706-1 ]
    CCDS59306.1. [P17706-4 ]
    PIRi A33899.
    RefSeqi NP_001193942.1. NM_001207013.1. [P17706-4 ]
    NP_002819.2. NM_002828.3. [P17706-1 ]
    NP_536347.1. NM_080422.2. [P17706-2 ]
    NP_536348.1. NM_080423.2. [P17706-3 ]
    UniGenei Hs.654527.
    Hs.663373.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L8K X-ray 2.56 A 1-314 [» ]
    ProteinModelPortali P17706.
    SMRi P17706. Positions 5-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111737. 14 interactions.
    IntActi P17706. 14 interactions.
    MINTi MINT-3975566.
    STRINGi 9606.ENSP00000311857.

    Chemistry

    BindingDBi P17706.
    ChEMBLi CHEMBL3807.

    PTM databases

    PhosphoSitei P17706.

    Polymorphism databases

    DMDMi 229462762.

    Proteomic databases

    MaxQBi P17706.
    PaxDbi P17706.
    PRIDEi P17706.

    Protocols and materials databases

    DNASUi 5771.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309660 ; ENSP00000311857 ; ENSG00000175354 . [P17706-1 ]
    ENST00000327283 ; ENSP00000320298 ; ENSG00000175354 . [P17706-2 ]
    ENST00000353319 ; ENSP00000320546 ; ENSG00000175354 . [P17706-3 ]
    ENST00000591115 ; ENSP00000466936 ; ENSG00000175354 . [P17706-4 ]
    GeneIDi 5771.
    KEGGi hsa:5771.
    UCSCi uc002krm.3. human. [P17706-3 ]
    uc002krp.3. human. [P17706-1 ]

    Organism-specific databases

    CTDi 5771.
    GeneCardsi GC18M012864.
    HGNCi HGNC:9650. PTPN2.
    HPAi HPA015004.
    HPA046176.
    MIMi 176887. gene.
    neXtProti NX_P17706.
    Orphaneti 206. Crohn disease.
    85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    771. Ulcerative colitis.
    PharmGKBi PA33993.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000273908.
    HOVERGENi HBG008321.
    InParanoidi P17706.
    KOi K18026.
    OMAi NTAQKVQ.
    OrthoDBi EOG7RV9G4.
    PhylomeDBi P17706.
    TreeFami TF315897.

    Enzyme and pathway databases

    Reactomei REACT_24980. Regulation of IFNG signaling.
    SignaLinki P17706.

    Miscellaneous databases

    ChiTaRSi PTPN2. human.
    EvolutionaryTracei P17706.
    GeneWikii PTPN2.
    GenomeRNAii 5771.
    NextBioi 22446.
    PROi P17706.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17706.
    Bgeei P17706.
    CleanExi HS_PTPN2.
    Genevestigatori P17706.

    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. "cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family."
      Cool D., Tonks N.K., Charbonneau H., Walsh K.A., Fischer E.H., Krebs E.G.
      Proc. Natl. Acad. Sci. U.S.A. 86:5257-5261(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: T-cell.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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 T.-O., 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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 3).
      Tissue: Brain and Eye.
    7. "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] OF 350-415 (ISOFORM 2), TISSUE SPECIFICITY.
    8. "COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus."
      Lorenzen J.A., Dadabay C.Y., Fischer E.H.
      J. Cell Biol. 131:631-643(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), MUTAGENESIS OF 350-ARG--ARG-352 AND LYS-380.
    9. "The noncatalytic C-terminal segment of the T cell protein tyrosine phosphatase regulates activity via an intramolecular mechanism."
      Hao L., Tiganis T., Tonks N.K., Charbonneau H.
      J. Biol. Chem. 272:29322-29329(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    10. "Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase."
      Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.
      Mol. Cell. Biol. 18:1622-1634(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF EGFR AND SHC1, MUTAGENESIS OF ASP-182, SUBCELLULAR LOCATION (ISOFORM 2).
    11. "Identification of tyrosine phosphatases that dephosphorylate the insulin receptor. A brute force approach based on 'substrate-trapping' mutants."
      Waelchli S., Curchod M.L., Gobert R.P., Arkinstall S., Hooft van Huijsduijnen R.
      J. Biol. Chem. 275:9792-9796(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF INSR.
    12. "The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation."
      Yamamoto T., Sekine Y., Kashima K., Kubota A., Sato N., Aoki N., Matsuda T.
      Biochem. Biophys. Res. Commun. 297:811-817(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF STAT3(ISOFORM 2).
    13. "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 DEPHOSPHORYLATION OF JAK1 AND JAK3, INTERACTION WITH JAK1 AND JAK3.
    14. Cited for: FUNCTION IN DEPHOSPHORYLATION OF STAT1.
    15. "Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP."
      Galic S., Klingler-Hoffmann M., Fodero-Tavoletti M.T., Puryer M.A., Meng T.C., Tonks N.K., Tiganis T.
      Mol. Cell. Biol. 23:2096-2108(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF INSR, MUTAGENESIS OF ASP-182, SUBCELLULAR LOCATION (ISOFORM 2).
    16. "The T-cell protein tyrosine phosphatase is phosphorylated on Ser-304 by cyclin-dependent protein kinases in mitosis."
      Bukczynska P., Klingler-Hoffmann M., Mitchelhill K.I., Lam M.H., Ciccomancini M., Tonks N.K., Sarcevic B., Kemp B.E., Tiganis T.
      Biochem. J. 380:939-949(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-304 BY CDK1 AND CDK2 (ISOFORM 2), MUTAGENESIS OF SER-304.
    17. "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.
    18. "The novel protein PTPIP51 exhibits tissue- and cell-specific expression."
      Stenzinger A., Kajosch T., Tag C., Porsche A., Welte I., Hofer H.W., Steger K., Wimmer M.
      Histochem. Cell Biol. 123:19-28(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RMDN3.
    19. "Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP."
      Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A., Ivaska J.
      Nat. Cell Biol. 7:78-85(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF EGFR, INTERACTION WITH ITGA1, SUBCELLULAR LOCATION.
    20. "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: INTERACTION WITH TRAF2.
    21. "The catalytic activity of the eukaryotic initiation factor-2alpha kinase PKR is required to negatively regulate Stat1 and Stat3 via activation of the T-cell protein-tyrosine phosphatase."
      Wang S., Raven J.F., Baltzis D., Kazemi S., Brunet D.V., Hatzoglou M., Tremblay M.L., Koromilas A.E.
      J. Biol. Chem. 281:9439-9449(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PKR.
    22. "Evidence for a role of transmembrane protein p25 in localization of protein tyrosine phosphatase TC48 to the ER."
      Gupta V., Swarup G.
      J. Cell Sci. 119:1703-1714(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMED9.
    23. "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 (ISOFORM 2), INDUCTION BY IL4.
    24. "Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase."
      Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L., Park M.
      J. Biol. Chem. 283:34374-34383(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF MET, INTERACTION WITH MET.
    25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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: FUNCTION IN DEPHOSPHORYLATION OF LCK AND FYN.
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: Implications for membrane trafficking in the early secretory pathway."
      Muppirala M., Gupta V., Swarup G.
      Biochim. Biophys. Acta 1823:2109-2119(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STX17, SUBCELLULAR LOCATION.
    31. Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 1-314, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiPTN2_HUMAN
    AccessioniPrimary (citable) accession number: P17706
    Secondary accession number(s): A8K955
    , A8MXU3, K7ENG3, Q96AU5, Q96HR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 158 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3