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Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene

Ptpn11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  1. insulin receptor binding Source: MGI
  2. non-membrane spanning protein tyrosine phosphatase activity Source: UniProtKB
  3. peptide hormone receptor binding Source: MGI
  4. phosphoprotein phosphatase activity Source: MGI
  5. protein tyrosine phosphatase activity Source: MGI
  6. receptor tyrosine kinase binding Source: UniProtKB
  7. SH3/SH2 adaptor activity Source: MGI

GO - Biological processi

  1. abortive mitotic cell cycle Source: MGI
  2. activation of MAPK activity Source: MGI
  3. atrioventricular canal development Source: MGI
  4. axonogenesis Source: MGI
  5. brain development Source: MGI
  6. DNA damage checkpoint Source: MGI
  7. ephrin receptor signaling pathway Source: UniProtKB
  8. epidermal growth factor receptor signaling pathway Source: MGI
  9. ERBB signaling pathway Source: MGI
  10. face morphogenesis Source: MGI
  11. genitalia development Source: MGI
  12. glucose homeostasis Source: MGI
  13. heart development Source: MGI
  14. hormone-mediated signaling pathway Source: MGI
  15. hormone metabolic process Source: MGI
  16. inner ear development Source: MGI
  17. integrin-mediated signaling pathway Source: MGI
  18. lipid metabolic process Source: MGI
  19. megakaryocyte development Source: MGI
  20. multicellular organismal reproductive process Source: MGI
  21. negative regulation of cell adhesion mediated by integrin Source: MGI
  22. negative regulation of cortisol secretion Source: MGI
  23. negative regulation of growth hormone secretion Source: MGI
  24. negative regulation of hormone secretion Source: MGI
  25. negative regulation of insulin secretion Source: MGI
  26. neurotrophin TRK receptor signaling pathway Source: MGI
  27. organ growth Source: MGI
  28. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  29. platelet-derived growth factor receptor signaling pathway Source: MGI
  30. platelet formation Source: MGI
  31. positive regulation of ERK1 and ERK2 cascade Source: MGI
  32. positive regulation of glucose import in response to insulin stimulus Source: MGI
  33. positive regulation of hormone secretion Source: MGI
  34. positive regulation of mitotic cell cycle Source: MGI
  35. positive regulation of signal transduction Source: MGI
  36. regulation of cell adhesion mediated by integrin Source: UniProtKB
  37. regulation of multicellular organism growth Source: MGI
  38. regulation of protein export from nucleus Source: MGI
  39. triglyceride metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_169390. Signaling by Leptin.
REACT_188529. Signaling by Leptin.
REACT_188578. Signaling by SCF-KIT.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198525. Negative regulation of FGFR signaling.
REACT_198526. Spry regulation of FGF signaling.
REACT_198561. Prolactin receptor signaling.
REACT_198622. Interferon alpha/beta signaling.
REACT_198627. Regulation of IFNA signaling.
REACT_199118. Interleukin-6 signaling.
REACT_206286. GAB1 signalosome.
REACT_211860. Tie2 Signaling.
REACT_223993. PI-3K cascade.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_225477. Costimulation by the CD28 family.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_230639. Downstream signal transduction.
REACT_234357. FRS2-mediated cascade.
REACT_240139. PI3K Cascade.
REACT_247448. ERK1 activation.
REACT_253341. Netrin mediated repulsion signals.
REACT_261568. CTLA4 inhibitory signaling.
REACT_263321. ERK2 activation.
REACT_263643. PD-1 signaling.
SABIO-RKP35235.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:99511. Ptpn11.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. mitochondrion Source: Ensembl
  4. nucleus Source: MGI
  5. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated by activated PDGFRB (By similarity). Phosphorylated upon activation of the receptor-type kinase PDGFRA.By similarity3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35235.
PaxDbiP35235.
PRIDEiP35235.

PTM databases

PhosphoSiteiP35235.

Expressioni

Tissue specificityi

Highly expressed in brain, heart and kidney.1 Publication

Gene expression databases

BgeeiP35235.
ExpressionAtlasiP35235. baseline and differential.
GenevestigatoriP35235.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP35235.

Family & Domainsi

Domains and Repeats

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

Region

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

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiP35235.
KOiK07293.
OMAiKEYGAMR.
OrthoDBiEOG7NPFST.
PhylomeDBiP35235.
TreeFamiTF351632.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000980. SH2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTiSM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA
60 70 80 90 100
VTHIKIQNTG DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY
110 120 130 140 150
PLNCADPTSE RWFHGHLSGK EAEKLLTEKG KHGSFLVRES QSHPGDFVLS
160 170 180 190 200
VRTGDDKGES NDGKSKVTHV MIRCQELKYD VGGGERFDSL TDLVEHYKKN
210 220 230 240 250
PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT DKVKQGFWEE
260 270 280 290 300
FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP
310 320 330 340 350
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS
360 370 380 390 400
RVIVMTTKEV ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE
410 420 430 440 450
LKLSKVGQAL LQGNTERTVW QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ
460 470 480 490 500
ESIVDAGPVV VHCSAGIGRT GTFIVIDILI DIIREKGVDC DIDVPKTIQM
510 520 530 540 550
VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK RKGHEYTNIK
560 570 580 590
YSLVDQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQRSFR
Length:597
Mass (Da):68,460
Last modified:December 20, 2005 - v2
Checksum:iC742BED37E39EA23
GO
Isoform 2 (identifier: P35235-2) [UniParc]FASTAAdd to basket

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

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

Experimental Info

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

Alternative sequence

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

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2620.

PTM databases

PhosphoSiteiP35235.

Proteomic databases

MaxQBiP35235.
PaxDbiP35235.
PRIDEiP35235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5781.
MGIiMGI:99511. Ptpn11.

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiP35235.
KOiK07293.
OMAiKEYGAMR.
OrthoDBiEOG7NPFST.
PhylomeDBiP35235.
TreeFamiTF351632.

Enzyme and pathway databases

ReactomeiREACT_169390. Signaling by Leptin.
REACT_188529. Signaling by Leptin.
REACT_188578. Signaling by SCF-KIT.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198525. Negative regulation of FGFR signaling.
REACT_198526. Spry regulation of FGF signaling.
REACT_198561. Prolactin receptor signaling.
REACT_198622. Interferon alpha/beta signaling.
REACT_198627. Regulation of IFNA signaling.
REACT_199118. Interleukin-6 signaling.
REACT_206286. GAB1 signalosome.
REACT_211860. Tie2 Signaling.
REACT_223993. PI-3K cascade.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_225477. Costimulation by the CD28 family.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_230639. Downstream signal transduction.
REACT_234357. FRS2-mediated cascade.
REACT_240139. PI3K Cascade.
REACT_247448. ERK1 activation.
REACT_253341. Netrin mediated repulsion signals.
REACT_261568. CTLA4 inhibitory signaling.
REACT_263321. ERK2 activation.
REACT_263643. PD-1 signaling.
SABIO-RKP35235.

Miscellaneous databases

ChiTaRSiPtpn11. mouse.
EvolutionaryTraceiP35235.
NextBioi296074.
PROiP35235.
SOURCEiSearch...

Gene expression databases

BgeeiP35235.
ExpressionAtlasiP35235. baseline and differential.
GenevestigatoriP35235.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule."
    Ohnishi H., Kubota M., Ohtake A., Sato K., Sano S.
    J. Biol. Chem. 271:25569-25574(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Head.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6.
    Tissue: Brain and Mammary tumor.
  4. "SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases."
    Feng G.-S., Hui C.-C., Pawson T.
    Science 259:1607-1611(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-552 (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. "Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation."
    Vogel W., Lammers R., Huang J., Ullrich A.
    Science 259:1611-1614(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation."
    Bazenet C.E., Gelderloos J.A., Kazlauskas A.
    Mol. Cell. Biol. 16:6926-6936(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRA AND GRB2, PHOSPHORYLATION.
  7. "Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2."
    Liu L., Damen J.E., Ware M.D., Krystal G.
    J. Biol. Chem. 272:10998-11001(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPP5D.
  8. "A family of proteins that inhibit signalling through tyrosine kinase receptors."
    Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A.
    Nature 386:181-186(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPNS1.
  9. "The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the protein tyrosine phosphatase SHP-2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors."
    Sattler M., Salgia R., Shrikhande G., Verma S., Choi J.-L., Rohrschneider L.R., Griffin J.D.
    Oncogene 15:2379-2384(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPP5D.
  10. "Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
    Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
    J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT1.
  11. "SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain."
    Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., Siminovitch K.A.
    Mol. Cell. Biol. 18:2089-2099(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIT.
  12. "Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors."
    Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T., Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.
    Blood 93:1809-1816(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAB2.
  13. "Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration."
    Jones N., Master Z., Jones J., Bouchard D., Gunji Y., Sasaki H., Daly R., Alitalo K., Dumont D.J.
    J. Biol. Chem. 274:30896-30905(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TEK/TIE2.
  14. "Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells."
    Zhang S., Mantel C., Broxmeyer H.E.
    J. Leukoc. Biol. 65:372-380(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH GRB2.
  15. "p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras guanine nucleotide exchange factor."
    Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.
    J. Biol. Chem. 275:30118-30123(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCAR3.
  16. "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells."
    Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M., Claesson-Welsh L.
    Mol. Biol. Cell 13:2881-2893(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHB.
  17. "LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation."
    Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.
    J. Exp. Med. 198:1463-1473(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIME1.
  18. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
    Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
    Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT3.
  20. "ROS fusion tyrosine kinase activates a SH2 domain-containing phosphatase-2/phosphatidylinositol 3-kinase/mammalian target of rapamycin signaling axis to form glioblastoma in mice."
    Charest A., Wilker E.W., McLaughlin M.E., Lane K., Gowda R., Coven S., McMahon K., Kovach S., Feng Y., Yaffe M.B., Jacks T., Housman D.
    Cancer Res. 66:7473-7481(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROS1, PHOSPHORYLATION AT TYR-546 AND TYR-584.
  21. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  22. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62 AND TYR-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  23. "An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E-mediated immediate hypersensitivity reactions."
    Hitomi K., Tahara-Hanaoka S., Someya S., Fujiki A., Tada H., Sugiyama T., Shibayama S., Shibuya K., Shibuya A.
    Nat. Immunol. 11:601-607(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MILR1.
  24. "Shp2 regulates SRC family kinase activity and Ras/Erk activation by controlling Csk recruitment."
    Zhang S.Q., Yang W., Kontaridis M.I., Bivona T.G., Wen G., Araki T., Luo J., Thompson J.A., Schraven B.L., Philips M.R., Neel B.G.
    Mol. Cell 13:341-355(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase."
    Lee C.-H., Kominos D., Jacques S., Margolis B., Schlessinger J., Shoelson S.E., Kuriyan J.
    Structure 2:423-438(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 4-103 IN COMPLEX WITH PDGFRB, INTERACTION WITH PDGFRB.

Entry informationi

Entry nameiPTN11_MOUSE
AccessioniPrimary (citable) accession number: P35235
Secondary accession number(s): Q3TQ84, Q64509, Q6PCL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: December 20, 2005
Last modified: March 4, 2015
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.