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Q06124 (PTN11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PTPN11
Synonyms:PTP2C, SHPTP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length597 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.17 Ref.31 Ref.32

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.44

Subunit structure

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. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33 Ref.35 Ref.36 Ref.38

Subcellular location

Cytoplasm.

Tissue specificity

Widely expressed, with highest levels in heart, brain, and skeletal muscle. Ref.2 Ref.3 Ref.4

Domain

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.

Post-translational modification

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. Ref.5 Ref.10 Ref.11 Ref.18 Ref.38

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.49 Ref.56 Ref.60 Ref.61 Ref.62 Ref.64 Ref.65

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.
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. Ref.45 Ref.48 Ref.50 Ref.51 Ref.52 Ref.53 Ref.55 Ref.57 Ref.58 Ref.59 Ref.63 Ref.66

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.58

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.39

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily.

Contains 2 SH2 domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
Disease mutation
   DomainRepeat
SH2 domain
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from electronic annotation. Source: Ensembl

ERBB signaling pathway

Inferred from direct assay PubMed 15133037. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

atrioventricular canal development

Inferred from mutant phenotype Ref.49. Source: BHF-UCL

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

brain development

Inferred from mutant phenotype Ref.45. Source: BHF-UCL

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

ephrin receptor signaling pathway

Inferred from direct assay Ref.17. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

face morphogenesis

Inferred from mutant phenotype Ref.45. Source: BHF-UCL

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

genitalia development

Inferred from mutant phenotype Ref.49. Source: BHF-UCL

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from mutant phenotype Ref.49. Source: BHF-UCL

hormone metabolic process

Inferred from electronic annotation. Source: Ensembl

hormone-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

inner ear development

Inferred from mutant phenotype Ref.49. Source: BHF-UCL

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

multicellular organismal reproductive process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cortisol secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of growth hormone secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

organ growth

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine dephosphorylation

Inferred from direct assay PubMed 15133037. Source: UniProtKB

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of glucose import in response to insulin stimulus

Inferred from direct assay PubMed 7493946. Source: BHF-UCL

positive regulation of hormone secretion

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion mediated by integrin

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

regulation of protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of type I interferon-mediated signaling pathway

Traceable author statement. Source: Reactome

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 10940933PubMed 15133037. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 15133037. Source: UniProtKB

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSH3/SH2 adaptor activity

Inferred from direct assay PubMed 7493946. Source: BHF-UCL

insulin receptor binding

Inferred from physical interaction PubMed 7493946. Source: BHF-UCL

non-membrane spanning protein tyrosine phosphatase activity

Inferred from mutant phenotype Ref.17. Source: UniProtKB

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 15133037. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay PubMed 15133037. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q06124-1)

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.
Isoform 2 (identifier: Q06124-2)

Also known as: PTP2C;

The sequence of this isoform differs from the canonical sequence as follows:
     408-411: Missing.
Isoform 3 (identifier: Q06124-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 597596Tyrosine-protein phosphatase non-receptor type 11
PRO_0000094767

Regions

Domain6 – 10297SH2 1
Domain112 – 216105SH2 2
Domain247 – 521275Tyrosine-protein phosphatase
Region463 – 4697Substrate binding By similarity

Sites

Active site4631Phosphocysteine intermediate
Binding site4291Substrate By similarity
Binding site5101Substrate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine Ref.34
Modified residue621Phosphotyrosine Ref.37
Modified residue631Phosphotyrosine
Modified residue661Phosphotyrosine By similarity
Modified residue2801N6-acetyllysine
Modified residue5461Phosphotyrosine; by PDGFR
Modified residue5621Phosphoserine
Modified residue5841Phosphotyrosine; by PDGFR Ref.37
Modified residue5951Phosphoserine

Natural variations

Alternative sequence408 – 4114Missing in isoform 2 and isoform 3.
VSP_016672
Alternative sequence4641S → R in isoform 3.
VSP_016673
Alternative sequence465 – 597133Missing in isoform 3.
VSP_016674
Natural variant21T → I in NS1. Ref.57
VAR_027183
Natural variant421T → A in NS1. Ref.48 Ref.57
VAR_015601
Natural variant581N → K in NS1. Ref.53
VAR_027184
Natural variant591T → A in NS1. Ref.66
VAR_066060
Natural variant601G → A in NS1. Ref.48
VAR_015602
Natural variant601G → V in myelodysplastic syndrome. Ref.58
VAR_015990
Natural variant611D → G in NS1. Ref.45 Ref.48 Ref.51 Ref.53
VAR_015603
Natural variant611D → N in NS1. Ref.48 Ref.53
VAR_015604
Natural variant611D → V in JMML; also in myelodysplastic syndrome. Ref.58
VAR_015991
Natural variant611D → Y in JMML. Ref.58
VAR_015992
Natural variant621Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. Ref.48 Ref.50 Ref.57 Ref.58
VAR_015605
Natural variant631Y → C in NS1. Ref.45 Ref.48 Ref.50 Ref.51 Ref.53 Ref.57
VAR_015606
Natural variant691E → K in JMML; also in myelodysplastic syndrome. Ref.58
VAR_015993
Natural variant691E → Q in NS1. Ref.53
VAR_027185
Natural variant711F → K in acute myeloid leukemia; requires 2 nucleotide substitutions. Ref.58
VAR_015994
Natural variant711F → L in myelodysplastic syndrome. Ref.53 Ref.58
VAR_015995
Natural variant721A → G in NS1. Ref.45 Ref.48 Ref.57
VAR_015607
Natural variant721A → S in NS1. Ref.45 Ref.51 Ref.53
VAR_015608
Natural variant721A → T in JMML. Ref.58
VAR_015996
Natural variant721A → V in JMML. Ref.58
VAR_015997
Natural variant731T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. Ref.48 Ref.51 Ref.53 Ref.58
Corresponds to variant rs28933387 [ dbSNP | Ensembl ].
VAR_015609
Natural variant761E → A in JMML; also in myelodysplastic syndrome. Ref.58
VAR_015998
Natural variant761E → D in NS1. Ref.45 Ref.48 Ref.53
VAR_015610
Natural variant761E → G in JMML. Ref.58
VAR_015999
Natural variant761E → K in JMML. Ref.58
Corresponds to variant rs28933388 [ dbSNP | Ensembl ].
VAR_016000
Natural variant761E → V in JMML. Ref.58
VAR_016001
Natural variant791Q → P in NS1. Ref.57
VAR_027186
Natural variant791Q → R in NS1. Ref.45 Ref.48 Ref.52 Ref.53
VAR_015611
Natural variant1061D → A in NS1. Ref.48 Ref.57
VAR_015612
Natural variant1391E → D in NS1. Ref.48 Ref.53
VAR_015613
Natural variant2561Q → R in NS1. Ref.53
VAR_027187
Natural variant2791Y → C in NS1 and LEOPARD1. Ref.48 Ref.49 Ref.57 Ref.61 Ref.62 Ref.65
VAR_015614
Natural variant2791Y → S in LEOPARD1. Ref.61 Ref.62
VAR_027188
Natural variant2821I → V in NS1. Ref.45 Ref.48 Ref.53
VAR_015615
Natural variant2851F → L in NS1. Ref.48
VAR_015617
Natural variant2851F → S in NS1. Ref.48 Ref.51
VAR_015616
Natural variant3081N → D in NS1; common mutation. Ref.45 Ref.48 Ref.51 Ref.53 Ref.57
VAR_015619
Natural variant3081N → S in NS1; some patients also manifest giant cell lesions of bone and soft tissue. Ref.48 Ref.57
VAR_015618
Natural variant3091I → V in NS1. Ref.48
VAR_015620
Natural variant4151T → M in NS1. Ref.59
VAR_027189
Natural variant4651A → T in LEOPARD1. Ref.60
VAR_027190
Natural variant4681G → A in LEOPARD1. Ref.60 Ref.62
VAR_027191
Natural variant4721T → M in LEOPARD1. Ref.49 Ref.57 Ref.61 Ref.62
VAR_015621
Natural variant5021R → L in LEOPARD1. Ref.62
VAR_027192
Natural variant5021R → W in LEOPARD1. Ref.62
VAR_027193
Natural variant5051R → K in NS1. Ref.48
VAR_015622
Natural variant5061S → T in NS1. Ref.50 Ref.55
VAR_015623
Natural variant5071G → A in JMML. Ref.58
VAR_016002
Natural variant5071G → R in patients with growth retardation, pulmonic stenosis and juvenile myelomonocytic leukemia. Ref.57 Ref.58
VAR_016003
Natural variant5081M → V in NS1. Ref.45 Ref.48 Ref.57
VAR_015624
Natural variant5101Q → P in LEOPARD1. Ref.56 Ref.62 Ref.64
VAR_027194
Natural variant5101Q → R in NS1. Ref.63
VAR_027195
Natural variant5141Q → P in LEOPARD1. Ref.61
VAR_027196
Natural variant5641L → F in NS1. Ref.57
VAR_027197

Experimental info

Mutagenesis4631C → S: Abolishes phosphatase activity. Ref.3
Sequence conflict5391S → R in BAA02740. Ref.3
Sequence conflict5521S → P in BAA02740. Ref.3

Secondary structure

........................................................................................... 597
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PTP2Ci) [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 37E8BFC7ECA2D03F

FASTA59768,436
        10         20         30         40         50         60 
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA VTHIKIQNTG 

        70         80         90        100        110        120 
DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY PLNCADPTSE RWFHGHLSGK 

       130        140        150        160        170        180 
EAEKLLTEKG KHGSFLVRES QSHPGDFVLS VRTGDDKGES NDGKSKVTHV MIRCQELKYD 

       190        200        210        220        230        240 
VGGGERFDSL TDLVEHYKKN PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT 

       250        260        270        280        290        300 
DKVKQGFWEE FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP 

       310        320        330        340        350        360 
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS RVIVMTTKEV 

       370        380        390        400        410        420 
ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE LKLSKVGQAL LQGNTERTVW 

       430        440        450        460        470        480 
QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ ESIMDAGPVV VHCSAGIGRT GTFIVIDILI 

       490        500        510        520        530        540 
DIIREKGVDC DIDVPKTIQM VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK 

       550        560        570        580        590 
RKGHEYTNIK YSLADQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQKSFR 

« Hide

Isoform 2 (PTP2C) [UniParc].

Checksum: 9CDBEFFA5E6CCB45
Show »

FASTA59368,011
Isoform 3 [UniParc].

Checksum: EB8E1553B37F1CC0
Show »

FASTA46052,828

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: INTERACTION WITH FER AND PECAM1.
[24]"The inhibitory potential of Fc receptor homolog 4 on memory B cells."
Ehrhardt G.R.A., Davis R.S., Hsu J.T., Leu C.-M., Ehrhardt A., Cooper M.D.
Proc. Natl. Acad. Sci. U.S.A. 100:13489-13494(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCRL4.
[25]"Signal transduction via the stem cell factor receptor/c-Kit."
Ronnstrand L.
Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[26]"Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
Wang J.F., Zhang X., Groopman J.E.
J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT4.
[27]"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].
[28]"ANKHD1, ankyrin repeat and KH domain containing 1, is overexpressed in acute leukemias and is associated with SHP2 in K562 cells."
Traina F., Favaro P.M.B., Medina Sde S., Duarte Ada S., Winnischofer S.M., Costa F.F., Saad S.T.O.
Biochim. Biophys. Acta 1762:828-834(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKHD1.
[29]"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.
[30]"FcRL6, a new ITIM-bearing receptor on cytolytic cells, is broadly expressed by lymphocytes following HIV-1 infection."
Wilson T.J., Presti R.M., Tassi I., Overton E.T., Cella M., Colonna M.
Blood 109:3786-3793(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCRL6.
[31]"Nuclear protein tyrosine phosphatase Shp-2 is one important negative regulator of nuclear export of telomerase reverse transcriptase."
Jakob S., Schroeder P., Lukosz M., Buchner N., Spyridopoulos I., Altschmied J., Haendeler J.
J. Biol. Chem. 283:33155-33161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERT, FUNCTION.
[32]"Regulation of RhoA-dependent ROCKII activation by Shp2."
Lee H.H., Chang Z.F.
J. Cell Biol. 181:999-1012(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[33]"An essential function for beta-arrestin 2 in the inhibitory signaling of natural killer cells."
Yu M.-C., Su L.-L., Zou L., Liu Y., Wu N., Kong L., Zhuang Z.-H., Sun L., Liu H.P., Hu J.-H., Li D., Strominger J.L., Zang J.-W., Pei G., Ge B.-X.
Nat. Immunol. 9:898-907(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIR2DL1.
[34]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"GAREM, a novel adaptor protein for growth factor receptor-bound protein 2, contributes to cellular transformation through the activation of extracellular signal-regulated kinase signaling."
Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E., Taniguchi H., Konishi H.
J. Biol. Chem. 284:20206-20214(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAREM.
[36]"A novel and critical role for tyrosine 663 in platelet endothelial cell adhesion molecule-1 trafficking and transendothelial migration."
Dasgupta B., Dufour E., Mamdouh Z., Muller W.A.
J. Immunol. 182:5041-5051(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PECAM1.
[37]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62 AND TYR-584, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[38]"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
Wardega P., Heldin C.H., Lennartsson J.
Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH PDGFRB.
[39]"Whole-genome sequencing of a single proband together with linkage analysis identifies a Mendelian disease gene."
Sobreira N.L., Cirulli E.T., Avramopoulos D., Wohler E., Oswald G.L., Stevens E.L., Ge D., Shianna K.V., Smith J.P., Maia J.M., Gumbs C.E., Pevsner J., Thomas G., Valle D., Hoover-Fong J.E., Goldstein D.B.
PLoS Genet. 6:E1000991-E1000991(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MC.
[40]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[41]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"Crystal structure of the tyrosine phosphatase SHP-2."
Hof P., Pluskey S., Dhe-Paganon S., Eck M.J., Shoelson S.E.
Cell 92:441-450(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-530 (ISOFORM 2).
[43]"Large-scale structural analysis of the classical human protein tyrosine phosphatome."
Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 237-533.
[44]"Salicylic acid based small molecule inhibitor for the oncogenic Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2)."
Zhang X., He Y., Liu S., Yu Z., Jiang Z.X., Yang Z., Dong Y., Nabinger S.C., Wu L., Gunawan A.M., Wang L., Chan R.J., Zhang Z.Y.
J. Med. Chem. 53:2482-2493(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 262-532 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY.
[45]"Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome."
Tartaglia M., Mehler E.L., Goldberg R., Zampino G., Brunner H.G., Kremer H., van der Burgt I., Crosby A.H., Ion A., Jeffery S., Kalidas K., Patton M.A., Kucherlapati R.S., Gelb B.D.
Nat. Genet. 29:465-468(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NS1 GLY-61; CYS-63; GLY-72; SER-72; ASP-76; ARG-79; VAL-282; ASP-308 AND VAL-508.
[46]Erratum
Tartaglia M., Mehler E.L., Goldberg R., Zampino G., Brunner H.G., Kremer H., van der Burgt I., Crosby A.H., Ion A., Jeffery S., Kalidas K., Patton M.A., Kucherlapati R.S., Gelb B.D.
Nat. Genet. 29:491-491(2001)
[47]Erratum
Tartaglia M., Mehler E.L., Goldberg R., Zampino G., Brunner H.G., Kremer H., van der Burgt I., Crosby A.H., Ion A., Jeffery S., Kalidas K., Patton M.A., Kucherlapati R.S., Gelb B.D.
Nat. Genet. 30:123-123(2001)
[48]"PTPN11 mutations in Noonan syndrome: molecular spectrum, genotype-phenotype correlation, and phenotypic heterogeneity."
Tartaglia M., Kalidas K., Shaw A., Song X., Musat D.L., van der Burgt I., Brunner H.G., Bertola D.R., Crosby A.H., Ion A., Kucherlapati R.S., Jeffery S., Patton M.A., Gelb B.D.
Am. J. Hum. Genet. 70:1555-1563(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NS1 ALA-42; ALA-60; ASN-61; GLY-61; ASP-62; CYS-63; GLY-72; ILE-73; ASP-76; ARG-79; ALA-106; ASP-139; CYS-279; VAL-282; LEU-285; SER-285; ASP-308; SER-308; VAL-309; LYS-505 AND VAL-508.
[49]"Grouping of multiple-lentigines/LEOPARD and Noonan syndromes on the PTPN11 gene."
Digilio M.C., Conti E., Sarkozy A., Mingarelli R., Dottorini T., Marino B., Pizzuti A., Dallapiccola B.
Am. J. Hum. Genet. 71:389-394(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEOPARD1 CYS-279 AND MET-472.
[50]"PTPN11 mutations in Noonan syndrome type I: detection of recurrent mutations in exons 3 and 13."
Maheshwari M., Belmont J., Fernbach S., Ho T., Molinari L., Yakub I., Yu F., Combes A., Towbin J.A., Craigen W.J., Gibbs R.A.
Hum. Mutat. 20:298-304(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NS1 ASP-62; CYS-63 AND THR-506.
[51]"PTPN11 (protein-tyrosine phosphatase, nonreceptor-type 11) mutations in seven Japanese patients with Noonan syndrome."
Kosaki K., Suzuki T., Muroya K., Hasegawa T., Sato S., Matsuo N., Kosaki R., Nagai T., Hasegawa Y., Ogata T.
J. Clin. Endocrinol. Metab. 87:3529-3533(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NS1 GLY-61; CYS-63; SER-72; ILE-73; SER-285 AND ASP-308.
[52]"PTPN11 mutation in a large family with Noonan syndrome and dizygous twinning."
Schollen E., Matthijs G., Gewillig M., Fryns J.-P., Legius E.
Eur. J. Hum. Genet. 11:85-88(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NS1 ARG-79.
[53]"Spectrum of mutations in PTPN11 and genotype-phenotype correlation in 96 patients with Noonan syndrome and five patients with cardio-facio-cutaneous syndrome."
Musante L., Kehl H.G., Majewski F., Meinecke P., Schweiger S., Gillessen-Kaesbach G., Wieczorek D., Hinkel G.K., Tinschert S., Hoeltzenbein M., Ropers H.-H., Kalscheuer V.M.
Eur. J. Hum. Genet. 11:201-206(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NS1 LYS-58; ASN-61; GLY-61; CYS-63; GLN-69; LEU-71; SER-72; ILE-73; ASP-76; ARG-79; ASP-139; ARG-256; VAL-282 AND ASP-308.
[54]Erratum
Musante L., Kehl H.G., Majewski F., Meinecke P., Schweiger S., Gillessen-Kaesbach G., Wieczorek D., Hinkel G.K., Tinschert S., Hoeltzenbein M., Ropers H.-H., Kalscheuer V.M.
Eur. J. Hum. Genet. 11:551-551(2003)
[55]"Noonan syndrome with leukaemoid reaction and overproduction of catecholamines: a case report."
Kondoh T., Ishii E., Aoki Y., Shimizu T., Zaitsu M., Matsubara Y., Moriuchi H.
Eur. J. Pediatr. 162:548-549(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NS1 THR-506.
[56]"A novel PTPN11 mutation in LEOPARD syndrome."
Conti E., Dottorini T., Sarkozy A., Tiller G.E., Esposito G., Pizzuti A., Dallapiccola B.
Hum. Mutat. 21:654-654(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEOPARD1 PRO-510.
[57]"Correlation between PTPN11 gene mutations and congenital heart defects in Noonan and LEOPARD syndromes."
Sarkozy A., Conti E., Seripa D., Digilio M.C., Grifone N., Tandoi C., Fazio V.M., Di Ciommo V., Marino B., Pizzuti A., Dallapiccola B.
J. Med. Genet. 40:704-708(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NS1 ILE-2; ALA-42; ASP-62; CYS-63; GLY-72; PRO-79; ALA-106; CYS-279; ASP-308; SER-308; MET-472; ARG-507; VAL-508 AND PHE-564.
[58]"Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia."
Tartaglia M., Niemeyer C.M., Fragale A., Song X., Buechner J., Jung A., Haehlen K., Hasle H., Licht J.D., Gelb B.D.
Nat. Genet. 34:148-150(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS JMML TYR-61; VAL-61; LYS-69; THR-72; VAL-72; ALA-76; GLY-76; LYS-76; VAL-76; ALA-507 AND ARG-507, VARIANTS MYELODYSPLASTIC SYNDROME VAL-60; VAL-61; LYS-69; LEU-71 AND ALA-76, VARIANTS NS1 ASP-62 AND ILE-73, VARIANT ACUTE MYELOID LEUKEMIA LYS-71.
[59]"Clinical variability in a Noonan syndrome family with a new PTPN11 gene mutation."
Bertola D.R., Pereira A.C., de Oliveira P.S.L., Kim C.A., Krieger J.E.
Am. J. Med. Genet. A 130:378-383(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NS1 MET-415.
[60]"Two novel and one recurrent PTPN11 mutations in LEOPARD syndrome."
Yoshida R., Nagai T., Hasegawa T., Kinoshita E., Tanaka T., Ogata T.
Am. J. Med. Genet. A 130:432-434(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEOPARD1 THR-465 AND ALA-468.
[61]"PTPN11 mutations in patients with LEOPARD syndrome: a French multicentric experience."
French collaborative Noonan study group
Keren B., Hadchouel A., Saba S., Sznajer Y., Bonneau D., Leheup B., Boute O., Gaillard D., Lacombe D., Layet V., Marlin S., Mortier G., Toutain A., Beylot C., Baumann C., Verloes A., Cave H.
J. Med. Genet. 41:E117-E117(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEOPARD1 CYS-279; SER-279; MET-472 AND PRO-514.
[62]"Clinical and molecular analysis of 30 patients with multiple lentigines LEOPARD syndrome."
Sarkozy A., Conti E., Digilio M.C., Marino B., Morini E., Pacileo G., Wilson M., Calabro R., Pizzuti A., Dallapiccola B.
J. Med. Genet. 41:E68-E68(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEOPARD1 CYS-279; SER-279; ALA-468; MET-472; TRP-502; LEU-502 AND PRO-510.
[63]"Neurofibromatosis-Noonan syndrome: molecular evidence of the concurrence of both disorders in a patient."
Bertola D.R., Pereira A.C., Passetti F., de Oliveira P.S.L., Messiaen L., Gelb B.D., Kim C.A., Krieger J.E.
Am. J. Med. Genet. A 136:242-245(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NS1 ARG-510.
[64]"Genetic heterogeneity in LEOPARD syndrome: two families with no mutations in PTPN11."
Kalidas K., Shaw A.C., Crosby A.H., Newbury-Ecob R., Greenhalgh L., Temple I.K., Law C., Patel A., Patton M.A., Jeffery S.
J. Hum. Genet. 50:21-25(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEOPARD1 PRO-510.
[65]"Acute myelomonocytic leukemia in a boy with LEOPARD syndrome (PTPN11 gene mutation positive)."
Ucar C., Calyskan U., Martini S., Heinritz W.
J. Pediatr. Hematol. Oncol. 28:123-125(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEOPARD1 CYS-279.
[66]"PTPN11, SOS1, KRAS, and RAF1 gene analysis, and genotype-phenotype correlation in Korean patients with Noonan syndrome."
Ko J.M., Kim J.M., Kim G.H., Yoo H.W.
J. Hum. Genet. 53:999-1006(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NS1 ALA-59.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJN0805.
RefSeqNP_002825.3. NM_002834.3.
NP_542168.1. NM_080601.1.
UniGeneHs.506852.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2SHPX-ray2.00A/B3-529[»]
3B7OX-ray1.60A237-533[»]
3MOWX-ray2.30A262-532[»]
3O5XX-ray2.00A262-532[»]
3TKZX-ray1.80A1-106[»]
3TL0X-ray2.05A1-106[»]
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[»]
ProteinModelPortalQ06124.
SMRQ06124. Positions 3-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111745. 97 interactions.
DIPDIP-516N.
IntActQ06124. 59 interactions.
MINTMINT-199832.
STRING9606.ENSP00000340944.

Chemistry

BindingDBQ06124.
ChEMBLCHEMBL3864.

PTM databases

PhosphoSiteQ06124.

Polymorphism databases

DMDM84028248.

Proteomic databases

PaxDbQ06124.
PRIDEQ06124.

Protocols and materials databases

DNASU5781.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351677; ENSP00000340944; ENSG00000179295. [Q06124-2]
ENST00000392597; ENSP00000376376; ENSG00000179295. [Q06124-3]
GeneID5781.
KEGGhsa:5781.
UCSCuc001ttw.1. human. [Q06124-3]
uc001ttx.3. human. [Q06124-2]

Organism-specific databases

CTD5781.
GeneCardsGC12P112856.
HGNCHGNC:9644. PTPN11.
HPACAB005377.
MIM151100. phenotype.
156250. phenotype.
163950. phenotype.
176876. gene.
607785. phenotype.
neXtProtNX_Q06124.
Orphanet86834. Juvenile myelomonocytic leukemia.
500. LEOPARD syndrome.
2499. Metachondromatosis.
648. Noonan syndrome.
PharmGKBPA33986.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000273907.
HOVERGENHBG000223.
InParanoidQ06124.
KOK07293.
OMAKEYGAMR.
OrthoDBEOG7NPFST.
PhylomeDBQ06124.
TreeFamTF351632.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ06124.

Gene expression databases

ArrayExpressQ06124.
BgeeQ06124.
CleanExHS_PTPN11.
GenevestigatorQ06124.

Family and domain databases

Gene3D3.30.505.10. 2 hits.
InterProIPR000980. 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]
PfamPF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTSM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]
SUPFAMSSF55550. SSF55550. 2 hits.
PROSITEPS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN11. human.
EvolutionaryTraceQ06124.
GeneWikiPTPN11.
GenomeRNAi5781.
NextBio22484.
PROQ06124.
SOURCESearch...

Entry information

Entry namePTN11_HUMAN
AccessionPrimary (citable) accession number: Q06124
Secondary accession number(s): A8K1D9, Q96HD7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM