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Q06124

- PTN11_HUMAN

UniProt

Q06124 - PTN11_HUMAN

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Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene
PTPN11, PTP2C, SHPTP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei429 – 4291Substrate By similarity
Active sitei463 – 4631Phosphocysteine intermediate
Binding sitei510 – 5101Substrate By 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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.7 Publications
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.
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.12 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 – 11Removed
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 – 661Phosphotyrosine By 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.5 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.23 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.

Miscellaneous databases

EvolutionaryTraceiQ06124.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 10297SH2 1Add
BLAST
Domaini112 – 216105SH2 2Add
BLAST
Domaini247 – 521275Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni463 – 4697Substrate binding By 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.

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

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. VSP_016672
Alternative sequencei464 – 4641S → R in isoform 3. VSP_016673
Alternative sequencei465 – 597133Missing in isoform 3. VSP_016674Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti539 – 5391S → R in BAA02740. 1 Publication
Sequence conflicti552 – 5521S → P in BAA02740. 1 Publication

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

« Hide 'large scale' publications
  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: INTERACTION WITH FER AND PECAM1.
  24. 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. 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. 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. Cited for: VARIANTS NS1 GLY-61; CYS-63; GLY-72; SER-72; ASP-76; ARG-79; VAL-282; ASP-308 AND VAL-508.
  46. "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.
  47. "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.
  48. "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.
  49. "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.
  50. "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.
  51. "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.
  52. "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.
  53. Cited for: VARIANT LEOPARD1 PRO-510.
  54. "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.
  55. "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.
  56. "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.
  57. "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.
  58. Cited for: VARIANTS LEOPARD1 CYS-279; SER-279; MET-472 AND PRO-514.
  59. "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.
  60. "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.
  61. "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.
  62. "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.
  63. "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.

Entry informationi

Entry nameiPTN11_HUMAN
AccessioniPrimary (citable) accession number: Q06124
Secondary accession number(s): A8K1D9, Q96HD7