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Q06124

- PTN11_HUMAN

UniProt

Q06124 - PTN11_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene

PTPN11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (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.3 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation

    Sites

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

    GO - Molecular functioni

    1. insulin receptor binding Source: BHF-UCL
    2. non-membrane spanning protein tyrosine phosphatase activity Source: UniProtKB
    3. phosphoprotein phosphatase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein tyrosine phosphatase activity Source: UniProtKB
    6. SH3/SH2 adaptor activity Source: BHF-UCL

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. atrioventricular canal development Source: BHF-UCL
    3. axon guidance Source: Reactome
    4. blood coagulation Source: Reactome
    5. brain development Source: BHF-UCL
    6. cytokine-mediated signaling pathway Source: Reactome
    7. DNA damage checkpoint Source: Ensembl
    8. ephrin receptor signaling pathway Source: UniProtKB
    9. epidermal growth factor receptor signaling pathway Source: Reactome
    10. ERBB signaling pathway Source: UniProtKB
    11. face morphogenesis Source: BHF-UCL
    12. Fc-epsilon receptor signaling pathway Source: Reactome
    13. fibroblast growth factor receptor signaling pathway Source: Reactome
    14. genitalia development Source: BHF-UCL
    15. glucose homeostasis Source: Ensembl
    16. heart development Source: BHF-UCL
    17. hormone-mediated signaling pathway Source: Ensembl
    18. hormone metabolic process Source: Ensembl
    19. innate immune response Source: Reactome
    20. inner ear development Source: BHF-UCL
    21. insulin receptor signaling pathway Source: Reactome
    22. interferon-gamma-mediated signaling pathway Source: Reactome
    23. leukocyte migration Source: Reactome
    24. multicellular organismal reproductive process Source: Ensembl
    25. negative regulation of cortisol secretion Source: Ensembl
    26. negative regulation of growth hormone secretion Source: Ensembl
    27. negative regulation of insulin secretion Source: Ensembl
    28. neurotrophin TRK receptor signaling pathway Source: Reactome
    29. organ growth Source: Ensembl
    30. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    31. phosphatidylinositol-mediated signaling Source: Reactome
    32. positive regulation of glucose import in response to insulin stimulus Source: BHF-UCL
    33. positive regulation of hormone secretion Source: Ensembl
    34. regulation of cell adhesion mediated by integrin Source: UniProtKB
    35. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
    36. regulation of multicellular organism growth Source: Ensembl
    37. regulation of protein export from nucleus Source: Ensembl
    38. regulation of type I interferon-mediated signaling pathway Source: Reactome
    39. T cell costimulation Source: Reactome
    40. triglyceride metabolic process Source: Ensembl
    41. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_111080. Spry regulation of FGF signaling.
    REACT_111184. Negative regulation of FGFR signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_12519. PECAM1 interactions.
    REACT_12578. GAB1 signalosome.
    REACT_12621. Tie2 Signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_169118. Signaling by Leptin.
    REACT_17025. Downstream signal transduction.
    REACT_19324. PD-1 signaling.
    REACT_19344. Costimulation by the CD28 family.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_21247. FRS2-mediated cascade.
    REACT_21270. PI-3K cascade.
    REACT_22384. Netrin mediated repulsion signals.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23879. Platelet sensitization by LDL.
    REACT_23916. Signal regulatory protein (SIRP) family interactions.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    REACT_27307. Interleukin-6 signaling.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinkiQ06124.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 11 (EC:3.1.3.48)
    Alternative name(s):
    Protein-tyrosine phosphatase 1D
    Short name:
    PTP-1D
    Protein-tyrosine phosphatase 2C
    Short name:
    PTP-2C
    SH-PTP2
    Short name:
    SHP-2
    Short name:
    Shp2
    SH-PTP3
    Gene namesi
    Name:PTPN11
    Synonyms:PTP2C, SHPTP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9644. PTPN11.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    LEOPARD syndrome 1 (LEOPARD1) [MIM:151100]: A disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti279 – 2791Y → C in NS1 and LEOPARD1. 6 Publications
    VAR_015614
    Natural varianti279 – 2791Y → S in LEOPARD1. 2 Publications
    VAR_027188
    Natural varianti465 – 4651A → T in LEOPARD1. 1 Publication
    VAR_027190
    Natural varianti468 – 4681G → A in LEOPARD1. 2 Publications
    VAR_027191
    Natural varianti472 – 4721T → M in LEOPARD1. 4 Publications
    VAR_015621
    Natural varianti502 – 5021R → L in LEOPARD1. 1 Publication
    VAR_027192
    Natural varianti502 – 5021R → W in LEOPARD1. 1 Publication
    VAR_027193
    Natural varianti510 – 5101Q → P in LEOPARD1. 3 Publications
    VAR_027194
    Natural varianti514 – 5141Q → P in LEOPARD1. 1 Publication
    VAR_027196
    Noonan syndrome 1 (NS1) [MIM:163950]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. Some patients with NS1 develop multiple giant cell lesions of the jaw or other bony or soft tissues, which are classified as pigmented villonodular synovitis (PVNS) when occurring in the jaw or joints.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. Mutations in PTPN11 account for more than 50% of the cases.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21T → I in NS1. 1 Publication
    VAR_027183
    Natural varianti42 – 421T → A in NS1. 2 Publications
    VAR_015601
    Natural varianti58 – 581N → K in NS1. 1 Publication
    VAR_027184
    Natural varianti59 – 591T → A in NS1. 1 Publication
    VAR_066060
    Natural varianti60 – 601G → A in NS1. 1 Publication
    VAR_015602
    Natural varianti61 – 611D → G in NS1. 4 Publications
    VAR_015603
    Natural varianti61 – 611D → N in NS1. 2 Publications
    VAR_015604
    Natural varianti62 – 621Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications
    VAR_015605
    Natural varianti63 – 631Y → C in NS1. 6 Publications
    VAR_015606
    Natural varianti69 – 691E → Q in NS1. 1 Publication
    VAR_027185
    Natural varianti72 – 721A → G in NS1. 3 Publications
    VAR_015607
    Natural varianti72 – 721A → S in NS1. 3 Publications
    VAR_015608
    Natural varianti73 – 731T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications
    Corresponds to variant rs28933387 [ dbSNP | Ensembl ].
    VAR_015609
    Natural varianti76 – 761E → D in NS1. 3 Publications
    VAR_015610
    Natural varianti79 – 791Q → P in NS1. 1 Publication
    VAR_027186
    Natural varianti79 – 791Q → R in NS1. 4 Publications
    VAR_015611
    Natural varianti106 – 1061D → A in NS1. 2 Publications
    VAR_015612
    Natural varianti139 – 1391E → D in NS1. 2 Publications
    VAR_015613
    Natural varianti256 – 2561Q → R in NS1. 1 Publication
    VAR_027187
    Natural varianti279 – 2791Y → C in NS1 and LEOPARD1. 6 Publications
    VAR_015614
    Natural varianti282 – 2821I → V in NS1. 3 Publications
    VAR_015615
    Natural varianti285 – 2851F → L in NS1. 1 Publication
    VAR_015617
    Natural varianti285 – 2851F → S in NS1. 2 Publications
    VAR_015616
    Natural varianti308 – 3081N → D in NS1; common mutation. 5 Publications
    VAR_015619
    Natural varianti308 – 3081N → S in NS1; some patients also manifest giant cell lesions of bone and soft tissue. 2 Publications
    VAR_015618
    Natural varianti309 – 3091I → V in NS1; unknown pathological significance. 1 Publication
    Corresponds to variant rs201787206 [ dbSNP | Ensembl ].
    VAR_015620
    Natural varianti415 – 4151T → M in NS1. 1 Publication
    VAR_027189
    Natural varianti505 – 5051R → K in NS1. 1 Publication
    VAR_015622
    Natural varianti506 – 5061S → T in NS1. 2 Publications
    VAR_015623
    Natural varianti508 – 5081M → V in NS1. 3 Publications
    VAR_015624
    Natural varianti510 – 5101Q → R in NS1. 1 Publication
    VAR_027195
    Natural varianti564 – 5641L → F in NS1. 1 Publication
    VAR_027197
    Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611D → V in JMML; also in myelodysplastic syndrome. 1 Publication
    VAR_015991
    Natural varianti61 – 611D → Y in JMML. 1 Publication
    VAR_015992
    Natural varianti69 – 691E → K in JMML; also in myelodysplastic syndrome. 1 Publication
    VAR_015993
    Natural varianti72 – 721A → T in JMML. 1 Publication
    VAR_015996
    Natural varianti72 – 721A → V in JMML. 1 Publication
    VAR_015997
    Natural varianti76 – 761E → A in JMML; also in myelodysplastic syndrome. 1 Publication
    VAR_015998
    Natural varianti76 – 761E → G in JMML. 1 Publication
    VAR_015999
    Natural varianti76 – 761E → K in JMML. 1 Publication
    Corresponds to variant rs28933388 [ dbSNP | Ensembl ].
    VAR_016000
    Natural varianti76 – 761E → V in JMML. 1 Publication
    VAR_016001
    Natural varianti507 – 5071G → A in JMML. 1 Publication
    VAR_016002
    Metachondromatosis (MC) [MIM:156250]: A skeletal disorder with radiologic features of both multiple exostoses and Ollier disease, characterized by the presence of exostoses, commonly of the bones of the hands and feet, and enchondromas of the metaphyses of long bones and iliac crest.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi463 – 4631C → S: Abolishes phosphatase activity. 1 Publication

    Keywords - Diseasei

    Deafness, Disease mutation

    Organism-specific databases

    MIMi151100. phenotype.
    156250. phenotype.
    163950. phenotype.
    607785. phenotype.
    Orphaneti86834. Juvenile myelomonocytic leukemia.
    500. LEOPARD syndrome.
    2499. Metachondromatosis.
    648. Noonan syndrome.
    PharmGKBiPA33986.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 597596Tyrosine-protein phosphatase non-receptor type 11PRO_0000094767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei62 – 621Phosphotyrosine1 Publication
    Modified residuei63 – 631Phosphotyrosine
    Modified residuei66 – 661PhosphotyrosineBy similarity
    Modified residuei546 – 5461Phosphotyrosine; by PDGFR
    Modified residuei562 – 5621Phosphoserine
    Modified residuei584 – 5841Phosphotyrosine; by PDGFR1 Publication
    Modified residuei595 – 5951Phosphoserine

    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 upon activation of the receptor-type kinase PDGFRA By similarity. Phosphorylated by activated PDGFRB.By similarity5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ06124.
    PaxDbiQ06124.
    PRIDEiQ06124.

    PTM databases

    PhosphoSiteiQ06124.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest levels in heart, brain, and skeletal muscle.3 Publications

    Gene expression databases

    ArrayExpressiQ06124.
    BgeeiQ06124.
    CleanExiHS_PTPN11.
    GenevestigatoriQ06124.

    Organism-specific databases

    HPAiCAB005377.

    Interactioni

    Subunit structurei

    Interacts with phosphorylated LIME1 and BCAR3. Interacts with SHB and INPP5D/SHIP1 By similarity. Interacts with MILR1 (tyrosine-phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2. Interacts with PDGFRA (tyrosine phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) By similarity. Interacts with PTPNS1 and CD84. Interacts with phosphorylated SIT1 and MPZL1. Interacts with FCRL3, FCRL4, FCRL6 and ANKHD1. Interacts with KIR2DL1; the interaction is enhanced by ARRB2. 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. Interacts with ROS1; mediates PTPN11 phosphorylation. Interacts with PDGFRB (tyrosine phosphorylated); this interaction increases the PTPN11 phosphatase activity. Interacts with GAREM isoform 1 (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation.By similarity24 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP1027512EBI-297779,EBI-608057
    CCKBRP322395EBI-297779,EBI-1753137
    CD33P201385EBI-297779,EBI-3906571
    DDR1Q083454EBI-297779,EBI-711879
    EEF1A1P681052EBI-297779,EBI-7645934From a different organism.
    EEF1A2Q71V392EBI-297779,EBI-7645815From a different organism.
    ERBB2P046262EBI-297779,EBI-641062
    FLT1P179482EBI-297779,EBI-1026718
    GAB1Q1348039EBI-297779,EBI-517684
    GAB2Q9UQC24EBI-297779,EBI-975200
    GRB2P629936EBI-297779,EBI-401755
    IGF1RP080693EBI-297779,EBI-475981
    INSRP062132EBI-297779,EBI-475899
    IRS1P355683EBI-297779,EBI-517592
    Irs1P355703EBI-297779,EBI-520230From a different organism.
    KIR2DL3P436284EBI-297779,EBI-8632435
    KITP1072129EBI-297779,EBI-1379503
    METP0858113EBI-297779,EBI-1039152
    MPZL1O952974EBI-297779,EBI-963338
    PDGFRBP096198EBI-297779,EBI-641237
    PECAM1P162847EBI-297779,EBI-716404
    PXNP490233EBI-297779,EBI-702209
    SirpaP977103EBI-297779,EBI-7945080From a different organism.

    Protein-protein interaction databases

    BioGridi111745. 99 interactions.
    DIPiDIP-516N.
    IntActiQ06124. 61 interactions.
    MINTiMINT-199832.
    STRINGi9606.ENSP00000340944.

    Structurei

    Secondary structure

    1
    597
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2311
    Beta strandi28 – 336
    Beta strandi35 – 373
    Beta strandi41 – 477
    Beta strandi50 – 589
    Beta strandi59 – 613
    Beta strandi63 – 686
    Beta strandi71 – 733
    Helixi74 – 8310
    Beta strandi87 – 904
    Helixi107 – 1093
    Beta strandi113 – 1164
    Helixi119 – 12810
    Beta strandi134 – 1396
    Beta strandi141 – 1433
    Beta strandi147 – 1537
    Beta strandi166 – 17510
    Beta strandi178 – 1847
    Beta strandi187 – 1893
    Helixi190 – 19910
    Beta strandi203 – 2053
    Beta strandi208 – 2103
    Helixi223 – 2253
    Helixi226 – 2349
    Helixi251 – 2533
    Helixi259 – 2624
    Helixi266 – 2694
    Helixi271 – 2766
    Beta strandi277 – 2793
    Helixi286 – 2883
    Beta strandi289 – 2913
    Beta strandi304 – 3107
    Beta strandi327 – 3315
    Helixi335 – 3373
    Helixi338 – 34710
    Beta strandi352 – 3554
    Beta strandi359 – 3613
    Beta strandi364 – 3663
    Beta strandi376 – 3805
    Beta strandi383 – 39210
    Beta strandi394 – 40512
    Beta strandi417 – 4248
    Beta strandi429 – 4313
    Beta strandi434 – 4363
    Helixi437 – 45115
    Beta strandi459 – 4679
    Helixi468 – 48619
    Beta strandi490 – 4923
    Helixi494 – 5029
    Helixi512 – 52817
    Beta strandi585 – 5895

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2SHPX-ray2.00A/B1-529[»]
    3B7OX-ray1.60A237-533[»]
    3MOWX-ray2.30A262-532[»]
    3O5XX-ray2.00A262-532[»]
    3TKZX-ray1.80A1-106[»]
    3TL0X-ray2.05A1-106[»]
    3ZM0X-ray1.50A248-531[»]
    3ZM1X-ray1.40A248-531[»]
    3ZM2X-ray1.50A248-531[»]
    3ZM3X-ray1.50A248-531[»]
    4DGPX-ray2.30A1-532[»]
    4DGXX-ray2.30A1-532[»]
    4GWFX-ray2.10A/B1-543[»]
    4H1OX-ray2.20A1-543[»]
    4H34X-ray2.70A1-543[»]
    4JE4X-ray2.31A1-103[»]
    4JEGX-ray2.30A97-217[»]
    4JMGX-ray1.40B579-591[»]
    ProteinModelPortaliQ06124.
    SMRiQ06124. Positions 3-595.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06124.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 10297SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini112 – 216105SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini247 – 521275Tyrosine-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.
    HOGENOMiHOG000273907.
    HOVERGENiHBG000223.
    InParanoidiQ06124.
    KOiK07293.
    OMAiKEYGAMR.
    OrthoDBiEOG7NPFST.
    PhylomeDBiQ06124.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q06124-1) [UniParc]FASTAAdd to Basket

    Also known as: PTP2Ci

    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
    ESIMDAGPVV VHCSAGIGRT GTFIVIDILI DIIREKGVDC DIDVPKTIQM 500
    VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK RKGHEYTNIK 550
    YSLADQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQKSFR 597
    Length:597
    Mass (Da):68,436
    Last modified:December 20, 2005 - v2
    Checksum:i37E8BFC7ECA2D03F
    GO
    Isoform 2 (identifier: Q06124-2) [UniParc]FASTAAdd to Basket

    Also known as: PTP2C

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

    Show »
    Length:593
    Mass (Da):68,011
    Checksum:i9CDBEFFA5E6CCB45
    GO
    Isoform 3 (identifier: Q06124-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         408-411: Missing.
         464-464: S → R
         465-597: Missing.

    Show »
    Length:460
    Mass (Da):52,828
    Checksum:iEB8E1553B37F1CC0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti539 – 5391S → R in BAA02740. (PubMed:8216283)Curated
    Sequence conflicti552 – 5521S → P in BAA02740. (PubMed:8216283)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21T → I in NS1. 1 Publication
    VAR_027183
    Natural varianti42 – 421T → A in NS1. 2 Publications
    VAR_015601
    Natural varianti58 – 581N → K in NS1. 1 Publication
    VAR_027184
    Natural varianti59 – 591T → A in NS1. 1 Publication
    VAR_066060
    Natural varianti60 – 601G → A in NS1. 1 Publication
    VAR_015602
    Natural varianti60 – 601G → V in myelodysplastic syndrome. 1 Publication
    VAR_015990
    Natural varianti61 – 611D → G in NS1. 4 Publications
    VAR_015603
    Natural varianti61 – 611D → N in NS1. 2 Publications
    VAR_015604
    Natural varianti61 – 611D → V in JMML; also in myelodysplastic syndrome. 1 Publication
    VAR_015991
    Natural varianti61 – 611D → Y in JMML. 1 Publication
    VAR_015992
    Natural varianti62 – 621Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications
    VAR_015605
    Natural varianti63 – 631Y → C in NS1. 6 Publications
    VAR_015606
    Natural varianti69 – 691E → K in JMML; also in myelodysplastic syndrome. 1 Publication
    VAR_015993
    Natural varianti69 – 691E → Q in NS1. 1 Publication
    VAR_027185
    Natural varianti71 – 711F → K in acute myeloid leukemia; requires 2 nucleotide substitutions. 1 Publication
    VAR_015994
    Natural varianti71 – 711F → L in myelodysplastic syndrome. 2 Publications
    VAR_015995
    Natural varianti72 – 721A → G in NS1. 3 Publications
    VAR_015607
    Natural varianti72 – 721A → S in NS1. 3 Publications
    VAR_015608
    Natural varianti72 – 721A → T in JMML. 1 Publication
    VAR_015996
    Natural varianti72 – 721A → V in JMML. 1 Publication
    VAR_015997
    Natural varianti73 – 731T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications
    Corresponds to variant rs28933387 [ dbSNP | Ensembl ].
    VAR_015609
    Natural varianti76 – 761E → A in JMML; also in myelodysplastic syndrome. 1 Publication
    VAR_015998
    Natural varianti76 – 761E → D in NS1. 3 Publications
    VAR_015610
    Natural varianti76 – 761E → G in JMML. 1 Publication
    VAR_015999
    Natural varianti76 – 761E → K in JMML. 1 Publication
    Corresponds to variant rs28933388 [ dbSNP | Ensembl ].
    VAR_016000
    Natural varianti76 – 761E → V in JMML. 1 Publication
    VAR_016001
    Natural varianti79 – 791Q → P in NS1. 1 Publication
    VAR_027186
    Natural varianti79 – 791Q → R in NS1. 4 Publications
    VAR_015611
    Natural varianti106 – 1061D → A in NS1. 2 Publications
    VAR_015612
    Natural varianti139 – 1391E → D in NS1. 2 Publications
    VAR_015613
    Natural varianti256 – 2561Q → R in NS1. 1 Publication
    VAR_027187
    Natural varianti279 – 2791Y → C in NS1 and LEOPARD1. 6 Publications
    VAR_015614
    Natural varianti279 – 2791Y → S in LEOPARD1. 2 Publications
    VAR_027188
    Natural varianti282 – 2821I → V in NS1. 3 Publications
    VAR_015615
    Natural varianti285 – 2851F → L in NS1. 1 Publication
    VAR_015617
    Natural varianti285 – 2851F → S in NS1. 2 Publications
    VAR_015616
    Natural varianti308 – 3081N → D in NS1; common mutation. 5 Publications
    VAR_015619
    Natural varianti308 – 3081N → S in NS1; some patients also manifest giant cell lesions of bone and soft tissue. 2 Publications
    VAR_015618
    Natural varianti309 – 3091I → V in NS1; unknown pathological significance. 1 Publication
    Corresponds to variant rs201787206 [ dbSNP | Ensembl ].
    VAR_015620
    Natural varianti415 – 4151T → M in NS1. 1 Publication
    VAR_027189
    Natural varianti465 – 4651A → T in LEOPARD1. 1 Publication
    VAR_027190
    Natural varianti468 – 4681G → A in LEOPARD1. 2 Publications
    VAR_027191
    Natural varianti472 – 4721T → M in LEOPARD1. 4 Publications
    VAR_015621
    Natural varianti502 – 5021R → L in LEOPARD1. 1 Publication
    VAR_027192
    Natural varianti502 – 5021R → W in LEOPARD1. 1 Publication
    VAR_027193
    Natural varianti505 – 5051R → K in NS1. 1 Publication
    VAR_015622
    Natural varianti506 – 5061S → T in NS1. 2 Publications
    VAR_015623
    Natural varianti507 – 5071G → A in JMML. 1 Publication
    VAR_016002
    Natural varianti507 – 5071G → R in patients with growth retardation, pulmonic stenosis and juvenile myelomonocytic leukemia. 2 Publications
    VAR_016003
    Natural varianti508 – 5081M → V in NS1. 3 Publications
    VAR_015624
    Natural varianti510 – 5101Q → P in LEOPARD1. 3 Publications
    VAR_027194
    Natural varianti510 – 5101Q → R in NS1. 1 Publication
    VAR_027195
    Natural varianti514 – 5141Q → P in LEOPARD1. 1 Publication
    VAR_027196
    Natural varianti564 – 5641L → F in NS1. 1 Publication
    VAR_027197

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei408 – 4114Missing in isoform 2 and isoform 3. 7 PublicationsVSP_016672
    Alternative sequencei464 – 4641S → R in isoform 3. 2 PublicationsVSP_016673
    Alternative sequencei465 – 597133Missing in isoform 3. 2 PublicationsVSP_016674Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13540 mRNA. Translation: BAA02740.2.
    L03535 mRNA. Translation: AAA36611.1.
    L07527 mRNA. Translation: AAA17022.1.
    L08807 mRNA. No translation available.
    X70766 mRNA. Translation: CAA50045.1.
    BT007106 mRNA. Translation: AAP35770.1.
    AK289854 mRNA. Translation: BAF82543.1.
    CH471054 Genomic DNA. Translation: EAW98012.1.
    BC008692 mRNA. Translation: AAH08692.1.
    CCDSiCCDS58280.1. [Q06124-3]
    CCDS9163.1. [Q06124-2]
    PIRiJN0805.
    RefSeqiNP_002825.3. NM_002834.3. [Q06124-2]
    NP_542168.1. NM_080601.1. [Q06124-3]
    XP_006719589.1. XM_006719526.1. [Q06124-1]
    UniGeneiHs.506852.

    Genome annotation databases

    EnsembliENST00000351677; ENSP00000340944; ENSG00000179295. [Q06124-2]
    ENST00000392597; ENSP00000376376; ENSG00000179295. [Q06124-3]
    GeneIDi5781.
    KEGGihsa:5781.
    UCSCiuc001ttw.1. human. [Q06124-3]
    uc001ttx.3. human. [Q06124-2]

    Polymorphism databases

    DMDMi84028248.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13540 mRNA. Translation: BAA02740.2 .
    L03535 mRNA. Translation: AAA36611.1 .
    L07527 mRNA. Translation: AAA17022.1 .
    L08807 mRNA. No translation available.
    X70766 mRNA. Translation: CAA50045.1 .
    BT007106 mRNA. Translation: AAP35770.1 .
    AK289854 mRNA. Translation: BAF82543.1 .
    CH471054 Genomic DNA. Translation: EAW98012.1 .
    BC008692 mRNA. Translation: AAH08692.1 .
    CCDSi CCDS58280.1. [Q06124-3 ]
    CCDS9163.1. [Q06124-2 ]
    PIRi JN0805.
    RefSeqi NP_002825.3. NM_002834.3. [Q06124-2 ]
    NP_542168.1. NM_080601.1. [Q06124-3 ]
    XP_006719589.1. XM_006719526.1. [Q06124-1 ]
    UniGenei Hs.506852.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2SHP X-ray 2.00 A/B 1-529 [» ]
    3B7O X-ray 1.60 A 237-533 [» ]
    3MOW X-ray 2.30 A 262-532 [» ]
    3O5X X-ray 2.00 A 262-532 [» ]
    3TKZ X-ray 1.80 A 1-106 [» ]
    3TL0 X-ray 2.05 A 1-106 [» ]
    3ZM0 X-ray 1.50 A 248-531 [» ]
    3ZM1 X-ray 1.40 A 248-531 [» ]
    3ZM2 X-ray 1.50 A 248-531 [» ]
    3ZM3 X-ray 1.50 A 248-531 [» ]
    4DGP X-ray 2.30 A 1-532 [» ]
    4DGX X-ray 2.30 A 1-532 [» ]
    4GWF X-ray 2.10 A/B 1-543 [» ]
    4H1O X-ray 2.20 A 1-543 [» ]
    4H34 X-ray 2.70 A 1-543 [» ]
    4JE4 X-ray 2.31 A 1-103 [» ]
    4JEG X-ray 2.30 A 97-217 [» ]
    4JMG X-ray 1.40 B 579-591 [» ]
    ProteinModelPortali Q06124.
    SMRi Q06124. Positions 3-595.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111745. 99 interactions.
    DIPi DIP-516N.
    IntActi Q06124. 61 interactions.
    MINTi MINT-199832.
    STRINGi 9606.ENSP00000340944.

    Chemistry

    BindingDBi Q06124.
    ChEMBLi CHEMBL3864.

    PTM databases

    PhosphoSitei Q06124.

    Polymorphism databases

    DMDMi 84028248.

    Proteomic databases

    MaxQBi Q06124.
    PaxDbi Q06124.
    PRIDEi Q06124.

    Protocols and materials databases

    DNASUi 5781.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351677 ; ENSP00000340944 ; ENSG00000179295 . [Q06124-2 ]
    ENST00000392597 ; ENSP00000376376 ; ENSG00000179295 . [Q06124-3 ]
    GeneIDi 5781.
    KEGGi hsa:5781.
    UCSCi uc001ttw.1. human. [Q06124-3 ]
    uc001ttx.3. human. [Q06124-2 ]

    Organism-specific databases

    CTDi 5781.
    GeneCardsi GC12P112856.
    GeneReviewsi PTPN11.
    HGNCi HGNC:9644. PTPN11.
    HPAi CAB005377.
    MIMi 151100. phenotype.
    156250. phenotype.
    163950. phenotype.
    176876. gene.
    607785. phenotype.
    neXtProti NX_Q06124.
    Orphaneti 86834. Juvenile myelomonocytic leukemia.
    500. LEOPARD syndrome.
    2499. Metachondromatosis.
    648. Noonan syndrome.
    PharmGKBi PA33986.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000273907.
    HOVERGENi HBG000223.
    InParanoidi Q06124.
    KOi K07293.
    OMAi KEYGAMR.
    OrthoDBi EOG7NPFST.
    PhylomeDBi Q06124.
    TreeFami TF351632.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_111080. Spry regulation of FGF signaling.
    REACT_111184. Negative regulation of FGFR signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_12519. PECAM1 interactions.
    REACT_12578. GAB1 signalosome.
    REACT_12621. Tie2 Signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_169118. Signaling by Leptin.
    REACT_17025. Downstream signal transduction.
    REACT_19324. PD-1 signaling.
    REACT_19344. Costimulation by the CD28 family.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_21247. FRS2-mediated cascade.
    REACT_21270. PI-3K cascade.
    REACT_22384. Netrin mediated repulsion signals.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23879. Platelet sensitization by LDL.
    REACT_23916. Signal regulatory protein (SIRP) family interactions.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    REACT_27307. Interleukin-6 signaling.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinki Q06124.

    Miscellaneous databases

    ChiTaRSi PTPN11. human.
    EvolutionaryTracei Q06124.
    GeneWikii PTPN11.
    GenomeRNAii 5781.
    NextBioi 22484.
    PROi Q06124.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06124.
    Bgeei Q06124.
    CleanExi HS_PTPN11.
    Genevestigatori Q06124.

    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. "Molecular cloning of a novel protein-tyrosine phosphatase SH-PTP3 with sequence similarity to the src-homology region 2."
      Adachi M., Sekiya M., Miyachi T., Matsuno K., Hinoda Y., Imai K., Yachi A.
      FEBS Lett. 314:335-339(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: T-cell.
    2. "Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew."
      Freeman R.M. Jr., Plutzky J., Neel B.G.
      Proc. Natl. Acad. Sci. U.S.A. 89:11239-11243(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    3. "Cloning, expression and mutational analysis of SH-PTP2, human protein-tyrosine phosphatase."
      Bastien L., Ramachandran C., Liu S., Adam M.
      Biochem. Biophys. Res. Commun. 196:124-133(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF CYS-463, TISSUE SPECIFICITY.
    4. "A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains."
      Ahmad S., Banville D.L., Zhao Z., Fischer E.H., Shen S.H.
      Proc. Natl. Acad. Sci. U.S.A. 90:2197-2201(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Tissue: Umbilical cord.
    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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PHOSPHORYLATION.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    7. "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 2).
      Tissue: Brain.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 3).
      Tissue: Eye.
    10. "Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor."
      Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G.
      J. Biol. Chem. 268:21478-21481(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH PDGFRB.
    11. "Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras."
      Bennett A.M., Tang T.L., Sugimoto S., Walsh C.T., Neel B.G.
      Proc. Natl. Acad. Sci. U.S.A. 91:7335-7339(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PDGFRB.
    12. "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: INTERACTION WITH PTPNS1.
    13. "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.
    14. "Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
      Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
      Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT1.
    15. "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.
    16. "SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-linked dimer regulating human T-cell activation."
      Marie-Cardine A., Kirchgessner H., Bruyns E., Shevchenko A., Mann M., Autschbach F., Ratnofsky S., Meuer S., Schraven B.
      J. Exp. Med. 189:1181-1194(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIT1.
    17. "Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
      Miao H., Burnett E., Kinch M., Simon E., Wang B.
      Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EPHA2.
    18. "Dissecting the interaction of SHP-2 with PZR, an immunoglobulin family protein containing immunoreceptor tyrosine-based inhibitory motifs."
      Zhao R., Zhao Z.J.
      J. Biol. Chem. 275:5453-5459(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MZPL1, DEPHOSPHORYLATION OF MZPL1.
    19. "Molecular cloning and characterization of SPAP1, an inhibitory receptor."
      Xu M.-J., Zhao R., Zhao Z.J.
      Biochem. Biophys. Res. Commun. 280:768-775(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCRL3.
    20. "Cell surface receptors Ly-9 and CD84 recruit the X-linked lymphoproliferative disease gene product SAP."
      Sayos J., Martin M., Chen A., Simarro M., Howie D., Morra M., Engel P., Terhorst C.
      Blood 97:3867-3874(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD84.
    21. "Distinct interactions of the X-linked lymphoproliferative syndrome gene product SAP with cytoplasmic domains of members of the CD2 receptor family."
      Lewis J., Eiben L.J., Nelson D.L., Cohen J.I., Nichols K.E., Ochs H.D., Notarangelo L.D., Duckett C.S.
      Clin. Immunol. 100:15-23(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD84.
    22. "Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein)."
      Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A., Spicka J., Hilgert I., Scherer J., Schraven B.
      Eur. J. Immunol. 31:1825-1836(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIT1.
    23. "Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells."
      Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M., Mochizuki N.
      Mol. Biol. Cell 14:3553-3564(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for