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P35235

- PTN11_MOUSE

UniProt

P35235 - PTN11_MOUSE

Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene

Ptpn11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      Previous versions | rss
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    Functioni

    Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei429 – 4291SubstrateBy similarity
    Active sitei463 – 4631Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei510 – 5101SubstrateBy similarity

    GO - Molecular functioni

    1. non-membrane spanning protein tyrosine phosphatase activity Source: UniProtKB
    2. peptide hormone receptor binding Source: MGI
    3. phosphoprotein phosphatase activity Source: MGI
    4. protein binding Source: UniProtKB
    5. receptor tyrosine kinase binding Source: UniProtKB

    GO - Biological processi

    1. abortive mitotic cell cycle Source: MGI
    2. activation of MAPK activity Source: MGI
    3. atrioventricular canal development Source: Ensembl
    4. axonogenesis Source: MGI
    5. brain development Source: Ensembl
    6. DNA damage checkpoint Source: MGI
    7. ephrin receptor signaling pathway Source: UniProtKB
    8. ERBB signaling pathway Source: Ensembl
    9. face morphogenesis Source: Ensembl
    10. genitalia development Source: Ensembl
    11. glucose homeostasis Source: MGI
    12. hormone-mediated signaling pathway Source: MGI
    13. hormone metabolic process Source: MGI
    14. inner ear development Source: Ensembl
    15. integrin-mediated signaling pathway Source: MGI
    16. lipid metabolic process Source: MGI
    17. megakaryocyte development Source: MGI
    18. multicellular organismal reproductive process Source: MGI
    19. negative regulation of cell adhesion mediated by integrin Source: MGI
    20. negative regulation of cortisol secretion Source: MGI
    21. negative regulation of growth hormone secretion Source: MGI
    22. negative regulation of hormone secretion Source: MGI
    23. negative regulation of insulin secretion Source: MGI
    24. neurotrophin TRK receptor signaling pathway Source: MGI
    25. organ growth Source: MGI
    26. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    27. platelet formation Source: MGI
    28. positive regulation of glucose import in response to insulin stimulus Source: Ensembl
    29. positive regulation of hormone secretion Source: MGI
    30. positive regulation of signal transduction Source: MGI
    31. regulation of cell adhesion mediated by integrin Source: UniProtKB
    32. regulation of multicellular organism growth Source: MGI
    33. regulation of protein export from nucleus Source: MGI
    34. triglyceride metabolic process Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_169390. Signaling by Leptin.
    REACT_188529. Signaling by Leptin.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198525. Negative regulation of FGFR signaling.
    REACT_198526. Spry regulation of FGF signaling.
    REACT_198561. Prolactin receptor signaling.
    REACT_198622. Interferon alpha/beta signaling.
    REACT_198627. Regulation of IFNA signaling.
    REACT_199118. Interleukin-6 signaling.
    REACT_206286. GAB1 signalosome.
    REACT_211860. Tie2 Signaling.
    REACT_223993. PI-3K cascade.
    REACT_225477. Costimulation by the CD28 family.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226341. PIP3 activates AKT signaling.
    SABIO-RKP35235.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 11 (EC:3.1.3.48)
    Alternative name(s):
    Protein-tyrosine phosphatase SYP
    SH-PTP2
    Short name:
    SHP-2
    Short name:
    Shp2
    Gene namesi
    Name:Ptpn11
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:99511. Ptpn11.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: Ensembl
    3. nucleus Source: Ensembl
    4. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 597596Tyrosine-protein phosphatase non-receptor type 11PRO_0000094768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity
    Modified residuei62 – 621Phosphotyrosine2 Publications
    Modified residuei63 – 631PhosphotyrosineBy similarity
    Modified residuei66 – 661Phosphotyrosine1 Publication
    Modified residuei546 – 5461Phosphotyrosine; by PDGFR1 Publication
    Modified residuei562 – 5621PhosphoserineBy similarity
    Modified residuei584 – 5841Phosphotyrosine; by PDGFR1 Publication
    Modified residuei595 – 5951PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated by activated PDGFRB By similarity. Phosphorylated upon activation of the receptor-type kinase PDGFRA.By similarity5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP35235.
    PaxDbiP35235.
    PRIDEiP35235.

    PTM databases

    PhosphoSiteiP35235.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, heart and kidney.1 Publication

    Gene expression databases

    ArrayExpressiP35235.
    BgeeiP35235.
    GenevestigatoriP35235.

    Interactioni

    Subunit structurei

    Interacts with CD84 and with phosphorylated SIT1 and MZPL1. Interacts with FCRL3, FCRL4, FCRL6 and ANKHD1. Interacts with GAREM (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation By similarity. Interacts with PTPNS1 and BCAR3. Interacts with phosphorylated LIME1. Interacts with SHB and INPP5D/SHIP1. Interacts with KIR2DL1; the interaction is enhanced by ARRB2 By similarity. Interacts with GAB2. Interacts with TERT; the interaction retains TERT in the nucleus. Interacts with PECAM1 and FER. Interacts with EPHA2 (activated); participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream signaling By similarity. Interacts with MILR1 (tyrosine phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2. Interacts with ROS1; mediates PTPN11 phosphorylation. Interacts with PDGFRA (tyrosine phosphorylated). Interacts with PDGFRB (tyrosine phosphorylated); this interaction increases the PTPN11 phosphatase activity. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated).By similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ctnnd1P309993EBI-397236,EBI-529924
    FesP168792EBI-397236,EBI-771815
    GRB2P629937EBI-397236,EBI-401755From a different organism.
    Grb2Q606313EBI-397236,EBI-1688
    Ido1P287765EBI-397236,EBI-4410822
    KITP107212EBI-397236,EBI-1379503From a different organism.
    Ntrk2P152092EBI-397236,EBI-309647
    PirbQ8K4V63EBI-397236,EBI-8602514
    Traf6P701962EBI-397236,EBI-448028

    Protein-protein interaction databases

    BioGridi202477. 22 interactions.
    DIPiDIP-29669N.
    IntActiP35235. 29 interactions.
    MINTiMINT-4110032.

    Structurei

    Secondary structure

    1
    597
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2210
    Beta strandi28 – 336
    Beta strandi35 – 373
    Beta strandi41 – 477
    Beta strandi50 – 556
    Beta strandi63 – 686
    Beta strandi71 – 733
    Helixi74 – 8310
    Helixi85 – 873
    Turni91 – 933

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AYAX-ray2.05A/B4-103[»]
    1AYBX-ray3.00A4-103[»]
    1AYCX-ray2.30A4-103[»]
    1AYDX-ray2.20A4-103[»]
    ProteinModelPortaliP35235.
    SMRiP35235. Positions 3-595.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35235.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 10297SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini112 – 216105SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini247 – 525279Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni463 – 4697Substrate bindingBy similarity

    Domaini

    The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme.

    Sequence similaritiesi

    Contains 2 SH2 domains.PROSITE-ProRule annotation
    Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00750000117233.
    HOGENOMiHOG000273907.
    HOVERGENiHBG000223.
    InParanoidiP35235.
    KOiK07293.
    OMAiKEYGAMR.
    OrthoDBiEOG7NPFST.
    PhylomeDBiP35235.
    TreeFamiTF351632.

    Family and domain databases

    Gene3Di3.30.505.10. 2 hits.
    3.90.190.10. 1 hit.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR000980. SH2.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00017. SH2. 2 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000929. Tyr-Ptase_nr_6. 1 hit.
    PRINTSiPR00700. PRTYPHPHTASE.
    PR00401. SH2DOMAIN.
    SMARTiSM00194. PTPc. 1 hit.
    SM00252. SH2. 2 hits.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    SSF55550. SSF55550. 2 hits.
    PROSITEiPS50001. SH2. 2 hits.
    PS00383. 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.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35235-1) [UniParc]FASTAAdd to Basket

    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

    MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA    50
    VTHIKIQNTG DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY 100
    PLNCADPTSE RWFHGHLSGK EAEKLLTEKG KHGSFLVRES QSHPGDFVLS 150
    VRTGDDKGES NDGKSKVTHV MIRCQELKYD VGGGERFDSL TDLVEHYKKN 200
    PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT DKVKQGFWEE 250
    FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP 300
    VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS 350
    RVIVMTTKEV ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE 400
    LKLSKVGQAL LQGNTERTVW QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ 450
    ESIVDAGPVV VHCSAGIGRT GTFIVIDILI DIIREKGVDC DIDVPKTIQM 500
    VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK RKGHEYTNIK 550
    YSLVDQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQRSFR 597
    Length:597
    Mass (Da):68,460
    Last modified:December 20, 2005 - v2
    Checksum:iC742BED37E39EA23
    GO
    Isoform 2 (identifier: P35235-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         408-411: Missing.

    Show »
    Length:593
    Mass (Da):68,035
    Checksum:i6C71EEEECCF7F159
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti390 – 3901E → G in BAE37500. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei408 – 4114Missing in isoform 2. 2 PublicationsVSP_016675

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84372 mRNA. Translation: BAA12328.1.
    AK159501 mRNA. Translation: BAE35134.1.
    AK159587 mRNA. Translation: BAE35207.1.
    AK163809 mRNA. Translation: BAE37500.1.
    BC057398 mRNA. Translation: AAH57398.1.
    BC059278 mRNA. Translation: AAH59278.1.
    L08663 mRNA. No translation available.
    CCDSiCCDS39247.1. [P35235-1]
    CCDS51637.1. [P35235-2]
    PIRiA46209.
    RefSeqiNP_001103462.1. NM_001109992.1. [P35235-2]
    NP_035332.1. NM_011202.3. [P35235-1]
    UniGeneiMm.8681.

    Genome annotation databases

    EnsembliENSMUST00000054547; ENSMUSP00000058757; ENSMUSG00000043733. [P35235-1]
    ENSMUST00000100770; ENSMUSP00000098333; ENSMUSG00000043733. [P35235-2]
    GeneIDi19247.
    KEGGimmu:19247.
    UCSCiuc008zio.2. mouse. [P35235-1]
    uc008zip.2. mouse. [P35235-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84372 mRNA. Translation: BAA12328.1 .
    AK159501 mRNA. Translation: BAE35134.1 .
    AK159587 mRNA. Translation: BAE35207.1 .
    AK163809 mRNA. Translation: BAE37500.1 .
    BC057398 mRNA. Translation: AAH57398.1 .
    BC059278 mRNA. Translation: AAH59278.1 .
    L08663 mRNA. No translation available.
    CCDSi CCDS39247.1. [P35235-1 ]
    CCDS51637.1. [P35235-2 ]
    PIRi A46209.
    RefSeqi NP_001103462.1. NM_001109992.1. [P35235-2 ]
    NP_035332.1. NM_011202.3. [P35235-1 ]
    UniGenei Mm.8681.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AYA X-ray 2.05 A/B 4-103 [» ]
    1AYB X-ray 3.00 A 4-103 [» ]
    1AYC X-ray 2.30 A 4-103 [» ]
    1AYD X-ray 2.20 A 4-103 [» ]
    ProteinModelPortali P35235.
    SMRi P35235. Positions 3-595.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202477. 22 interactions.
    DIPi DIP-29669N.
    IntActi P35235. 29 interactions.
    MINTi MINT-4110032.

    Chemistry

    ChEMBLi CHEMBL2620.

    PTM databases

    PhosphoSitei P35235.

    Proteomic databases

    MaxQBi P35235.
    PaxDbi P35235.
    PRIDEi P35235.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000054547 ; ENSMUSP00000058757 ; ENSMUSG00000043733 . [P35235-1 ]
    ENSMUST00000100770 ; ENSMUSP00000098333 ; ENSMUSG00000043733 . [P35235-2 ]
    GeneIDi 19247.
    KEGGi mmu:19247.
    UCSCi uc008zio.2. mouse. [P35235-1 ]
    uc008zip.2. mouse. [P35235-2 ]

    Organism-specific databases

    CTDi 5781.
    MGIi MGI:99511. Ptpn11.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00750000117233.
    HOGENOMi HOG000273907.
    HOVERGENi HBG000223.
    InParanoidi P35235.
    KOi K07293.
    OMAi KEYGAMR.
    OrthoDBi EOG7NPFST.
    PhylomeDBi P35235.
    TreeFami TF351632.

    Enzyme and pathway databases

    Reactomei REACT_169390. Signaling by Leptin.
    REACT_188529. Signaling by Leptin.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198525. Negative regulation of FGFR signaling.
    REACT_198526. Spry regulation of FGF signaling.
    REACT_198561. Prolactin receptor signaling.
    REACT_198622. Interferon alpha/beta signaling.
    REACT_198627. Regulation of IFNA signaling.
    REACT_199118. Interleukin-6 signaling.
    REACT_206286. GAB1 signalosome.
    REACT_211860. Tie2 Signaling.
    REACT_223993. PI-3K cascade.
    REACT_225477. Costimulation by the CD28 family.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226341. PIP3 activates AKT signaling.
    SABIO-RK P35235.

    Miscellaneous databases

    ChiTaRSi PTPN11. mouse.
    EvolutionaryTracei P35235.
    NextBioi 296074.
    PROi P35235.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35235.
    Bgeei P35235.
    Genevestigatori P35235.

    Family and domain databases

    Gene3Di 3.30.505.10. 2 hits.
    3.90.190.10. 1 hit.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000980. SH2.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00017. SH2. 2 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000929. Tyr-Ptase_nr_6. 1 hit.
    PRINTSi PR00700. PRTYPHPHTASE.
    PR00401. SH2DOMAIN.
    SMARTi SM00194. PTPc. 1 hit.
    SM00252. SH2. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    SSF55550. SSF55550. 2 hits.
    PROSITEi PS50001. SH2. 2 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule."
      Ohnishi H., Kubota M., Ohtake A., Sato K., Sano S.
      J. Biol. Chem. 271:25569-25574(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
      Tissue: Brain.
    2. "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: C57BL/6J.
      Tissue: Head.
    3. "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 2).
      Strain: C57BL/6.
      Tissue: Brain and Mammary tumor.
    4. "SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases."
      Feng G.-S., Hui C.-C., Pawson T.
      Science 259:1607-1611(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-552 (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Mammary gland.
    5. "Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation."
      Vogel W., Lammers R., Huang J., Ullrich A.
      Science 259:1611-1614(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation."
      Bazenet C.E., Gelderloos J.A., Kazlauskas A.
      Mol. Cell. Biol. 16:6926-6936(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRA AND GRB2, PHOSPHORYLATION.
    7. "Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2."
      Liu L., Damen J.E., Ware M.D., Krystal G.
      J. Biol. Chem. 272:10998-11001(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    8. "A family of proteins that inhibit signalling through tyrosine kinase receptors."
      Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A.
      Nature 386:181-186(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPNS1.
    9. "The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the protein tyrosine phosphatase SHP-2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors."
      Sattler M., Salgia R., Shrikhande G., Verma S., Choi J.-L., Rohrschneider L.R., Griffin J.D.
      Oncogene 15:2379-2384(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    10. "Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
      Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
      J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT1.
    11. "SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain."
      Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., Siminovitch K.A.
      Mol. Cell. Biol. 18:2089-2099(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIT.
    12. "Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors."
      Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T., Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.
      Blood 93:1809-1816(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAB2.
    13. "Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration."
      Jones N., Master Z., Jones J., Bouchard D., Gunji Y., Sasaki H., Daly R., Alitalo K., Dumont D.J.
      J. Biol. Chem. 274:30896-30905(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TEK/TIE2.
    14. "Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells."
      Zhang S., Mantel C., Broxmeyer H.E.
      J. Leukoc. Biol. 65:372-380(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH GRB2.
    15. "p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras guanine nucleotide exchange factor."
      Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.
      J. Biol. Chem. 275:30118-30123(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCAR3.
    16. "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells."
      Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M., Claesson-Welsh L.
      Mol. Biol. Cell 13:2881-2893(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    17. "LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation."
      Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.
      J. Exp. Med. 198:1463-1473(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIME1.
    18. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
      Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
      Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT3.
    20. "ROS fusion tyrosine kinase activates a SH2 domain-containing phosphatase-2/phosphatidylinositol 3-kinase/mammalian target of rapamycin signaling axis to form glioblastoma in mice."
      Charest A., Wilker E.W., McLaughlin M.E., Lane K., Gowda R., Coven S., McMahon K., Kovach S., Feng Y., Yaffe M.B., Jacks T., Housman D.
      Cancer Res. 66:7473-7481(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROS1, PHOSPHORYLATION AT TYR-546 AND TYR-584.
    21. "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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    22. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62 AND TYR-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    23. "An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E-mediated immediate hypersensitivity reactions."
      Hitomi K., Tahara-Hanaoka S., Someya S., Fujiki A., Tada H., Sugiyama T., Shibayama S., Shibuya K., Shibuya A.
      Nat. Immunol. 11:601-607(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MILR1.
    24. "Shp2 regulates SRC family kinase activity and Ras/Erk activation by controlling Csk recruitment."
      Zhang S.Q., Yang W., Kontaridis M.I., Bivona T.G., Wen G., Araki T., Luo J., Thompson J.A., Schraven B.L., Philips M.R., Neel B.G.
      Mol. Cell 13:341-355(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase."
      Lee C.-H., Kominos D., Jacques S., Margolis B., Schlessinger J., Shoelson S.E., Kuriyan J.
      Structure 2:423-438(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 4-103 IN COMPLEX WITH PDGFRB, INTERACTION WITH PDGFRB.

    Entry informationi

    Entry nameiPTN11_MOUSE
    AccessioniPrimary (citable) accession number: P35235
    Secondary accession number(s): Q3TQ84, Q64509, Q6PCL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 163 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

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3