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P35235

- PTN11_MOUSE

UniProt

P35235 - PTN11_MOUSE

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Protein
Tyrosine-protein phosphatase non-receptor type 11
Gene
Ptpn11
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. DNA damage checkpoint Source: MGI
  2. ERBB signaling pathway Source: Ensembl
  3. abortive mitotic cell cycle Source: MGI
  4. activation of MAPK activity Source: MGI
  5. atrioventricular canal development Source: Ensembl
  6. axonogenesis Source: MGI
  7. brain development Source: Ensembl
  8. ephrin receptor signaling pathway Source: UniProtKB
  9. face morphogenesis Source: Ensembl
  10. genitalia development Source: Ensembl
  11. glucose homeostasis Source: MGI
  12. hormone metabolic process Source: MGI
  13. hormone-mediated signaling pathway Source: MGI
  14. inner ear development Source: Ensembl
  15. integrin-mediated signaling pathway Source: MGI
  16. lipid metabolic process Source: MGI
  17. megakaryocyte development Source: MGI
  18. multicellular organismal reproductive process Source: MGI
  19. negative regulation of cell adhesion mediated by integrin Source: MGI
  20. negative regulation of cortisol secretion Source: MGI
  21. negative regulation of growth hormone secretion Source: MGI
  22. negative regulation of hormone secretion Source: MGI
  23. negative regulation of insulin secretion Source: MGI
  24. neurotrophin TRK receptor signaling pathway Source: MGI
  25. organ growth Source: MGI
  26. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  27. platelet formation Source: MGI
  28. positive regulation of glucose import in response to insulin stimulus Source: Ensembl
  29. positive regulation of hormone secretion Source: MGI
  30. positive regulation of signal transduction Source: MGI
  31. regulation of cell adhesion mediated by integrin Source: UniProtKB
  32. regulation of multicellular organism growth Source: MGI
  33. regulation of protein export from nucleus Source: MGI
  34. triglyceride metabolic process Source: MGI
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_225477. Costimulation by the CD28 family.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226341. PIP3 activates AKT signaling.
SABIO-RKP35235.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:99511. Ptpn11.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine By similarity
Modified residuei62 – 621Phosphotyrosine2 Publications
Modified residuei63 – 631Phosphotyrosine By similarity
Modified residuei66 – 661Phosphotyrosine1 Publication
Modified residuei546 – 5461Phosphotyrosine; by PDGFR1 Publication
Modified residuei562 – 5621Phosphoserine By similarity
Modified residuei584 – 5841Phosphotyrosine; by PDGFR1 Publication
Modified residuei595 – 5951Phosphoserine By 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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35235.
PaxDbiP35235.
PRIDEiP35235.

PTM databases

PhosphoSiteiP35235.

Expressioni

Tissue specificityi

Highly expressed in brain, heart and kidney.1 Publication

Gene expression databases

ArrayExpressiP35235.
BgeeiP35235.
GenevestigatoriP35235.

Interactioni

Subunit structurei

Interacts with CD84 and with phosphorylated SIT1 and MZPL1. Interacts with FCRL3, FCRL4, FCRL6 and ANKHD1. Interacts with GAREM (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation By similarity. Interacts with PTPNS1 and BCAR3. Interacts with phosphorylated LIME1. Interacts with SHB and INPP5D/SHIP1. Interacts with KIR2DL1; the interaction is enhanced by ARRB2 By similarity. Interacts with GAB2. Interacts with TERT; the interaction retains TERT in the nucleus. Interacts with PECAM1 and FER. Interacts with EPHA2 (activated); participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream signaling By similarity. Interacts with MILR1 (tyrosine phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2. Interacts with ROS1; mediates PTPN11 phosphorylation. Interacts with PDGFRA (tyrosine phosphorylated). Interacts with PDGFRB (tyrosine phosphorylated); this interaction increases the PTPN11 phosphatase activity. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated).16 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

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP35235.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 10297SH2 1
Add
BLAST
Domaini112 – 216105SH2 2
Add
BLAST
Domaini247 – 525279Tyrosine-protein phosphatase
Add
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.
GeneTreeiENSGT00750000117233.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiP35235.
KOiK07293.
OMAiKEYGAMR.
OrthoDBiEOG7NPFST.
PhylomeDBiP35235.
TreeFamiTF351632.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

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

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

« Hide

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

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

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei408 – 4114Missing in isoform 2.
VSP_016675

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti390 – 3901E → G in BAE37500. 1 Publication

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLi CHEMBL2620.

PTM databases

PhosphoSitei P35235.

Proteomic databases

MaxQBi P35235.
PaxDbi P35235.
PRIDEi P35235.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 5781.
MGIi MGI:99511. Ptpn11.

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

ArrayExpressi P35235.
Bgeei P35235.
Genevestigatori P35235.

Family and domain databases

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

Publicationsi

« 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: September 3, 2014
This is version 162 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

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