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P35235 (PTN11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type 11

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase SYP
SH-PTP2
Short name=SHP-2
Short name=Shp2
Gene names
Name:Ptpn11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity. Ref.24

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

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). Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.23 Ref.25

Subcellular location

Cytoplasm.

Tissue specificity

Highly expressed in brain, heart and kidney. Ref.5

Domain

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

Post-translational modification

Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated by activated PDGFRB By similarity. Phosphorylated upon activation of the receptor-type kinase PDGFRA. Ref.6 Ref.14 Ref.20

Sequence similarities

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

Contains 2 SH2 domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

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

Inferred from mutant phenotype PubMed 12937170. Source: MGI

ERBB signaling pathway

Inferred from electronic annotation. Source: Ensembl

abortive mitotic cell cycle

Inferred from mutant phenotype PubMed 23509158. Source: MGI

activation of MAPK activity

Inferred from mutant phenotype PubMed 12937170PubMed 15273746. Source: MGI

atrioventricular canal development

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Inferred from mutant phenotype PubMed 12482708. Source: MGI

brain development

Inferred from electronic annotation. Source: Ensembl

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

genitalia development

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from mutant phenotype PubMed 15520383. Source: MGI

hormone metabolic process

Inferred from mutant phenotype PubMed 15520383. Source: MGI

hormone-mediated signaling pathway

Inferred from direct assay PubMed 15520383. Source: MGI

inner ear development

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Inferred from mutant phenotype PubMed 23509158. Source: MGI

lipid metabolic process

Inferred from mutant phenotype PubMed 15520383. Source: MGI

megakaryocyte development

Inferred from mutant phenotype PubMed 23509158. Source: MGI

multicellular organismal reproductive process

Inferred from mutant phenotype PubMed 15520383. Source: MGI

negative regulation of cell adhesion mediated by integrin

Inferred from mutant phenotype PubMed 23509158. Source: MGI

negative regulation of cortisol secretion

Inferred from mutant phenotype PubMed 15520383. Source: MGI

negative regulation of growth hormone secretion

Inferred from mutant phenotype PubMed 15520383. Source: MGI

negative regulation of hormone secretion

Inferred from mutant phenotype PubMed 15520383. Source: MGI

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 15520383. Source: MGI

neurotrophin TRK receptor signaling pathway

Inferred from mutant phenotype PubMed 12482708. Source: MGI

organ growth

Inferred from mutant phenotype PubMed 15520383. Source: MGI

peptidyl-tyrosine dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

platelet formation

Inferred from genetic interaction PubMed 23509158. Source: MGI

positive regulation of glucose import in response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

positive regulation of hormone secretion

Inferred from mutant phenotype PubMed 15520383. Source: MGI

positive regulation of signal transduction

Inferred from mutant phenotype PubMed 15520383. Source: MGI

regulation of cell adhesion mediated by integrin

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 15520383. Source: MGI

regulation of protein export from nucleus

Inferred from mutant phenotype PubMed 12937170. Source: MGI

triglyceride metabolic process

Inferred from mutant phenotype PubMed 15520383. Source: MGI

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionnon-membrane spanning protein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

peptide hormone receptor binding

Inferred from physical interaction PubMed 15520383. Source: MGI

phosphoprotein phosphatase activity

Inferred from mutant phenotype PubMed 15273746. Source: MGI

protein binding

Inferred from physical interaction Ref.23. Source: UniProtKB

receptor tyrosine kinase binding

Inferred from physical interaction Ref.20. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35235-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35235-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 597596Tyrosine-protein phosphatase non-receptor type 11
PRO_0000094768

Regions

Domain6 – 10297SH2 1
Domain112 – 216105SH2 2
Domain247 – 525279Tyrosine-protein phosphatase
Region463 – 4697Substrate binding By similarity

Sites

Active site4631Phosphocysteine intermediate By similarity
Binding site4291Substrate By similarity
Binding site5101Substrate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue621Phosphotyrosine Ref.21 Ref.22
Modified residue631Phosphotyrosine By similarity
Modified residue661Phosphotyrosine Ref.22
Modified residue5461Phosphotyrosine; by PDGFR Ref.20
Modified residue5621Phosphoserine By similarity
Modified residue5841Phosphotyrosine; by PDGFR Ref.20
Modified residue5951Phosphoserine By similarity

Natural variations

Alternative sequence408 – 4114Missing in isoform 2.
VSP_016675

Experimental info

Sequence conflict3901E → G in BAE37500. Ref.2

Secondary structure

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

Details...

Sequences

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

Last modified December 20, 2005. Version 2.
Checksum: C742BED37E39EA23

FASTA59768,460
        10         20         30         40         50         60 
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA VTHIKIQNTG 

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

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

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

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

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

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

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

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

       550        560        570        580        590 
RKGHEYTNIK YSLVDQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQRSFR 

« Hide

Isoform 2 [UniParc].

Checksum: 6C71EEEECCF7F159
Show »

FASTA59368,035

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS39247.1. [P35235-1]
CCDS51637.1. [P35235-2]
PIRA46209.
RefSeqNP_001103462.1. NM_001109992.1. [P35235-2]
NP_035332.1. NM_011202.3. [P35235-1]
UniGeneMm.8681.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYAX-ray2.05A/B4-103[»]
1AYBX-ray3.00A4-103[»]
1AYCX-ray2.30A4-103[»]
1AYDX-ray2.20A4-103[»]
ProteinModelPortalP35235.
SMRP35235. Positions 3-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202477. 22 interactions.
DIPDIP-29669N.
IntActP35235. 29 interactions.
MINTMINT-4110032.

Chemistry

ChEMBLCHEMBL2620.

PTM databases

PhosphoSiteP35235.

Proteomic databases

MaxQBP35235.
PaxDbP35235.
PRIDEP35235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054547; ENSMUSP00000058757; ENSMUSG00000043733. [P35235-1]
ENSMUST00000100770; ENSMUSP00000098333; ENSMUSG00000043733. [P35235-2]
GeneID19247.
KEGGmmu:19247.
UCSCuc008zio.2. mouse. [P35235-1]
uc008zip.2. mouse. [P35235-2]

Organism-specific databases

CTD5781.
MGIMGI:99511. Ptpn11.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00750000117233.
HOGENOMHOG000273907.
HOVERGENHBG000223.
InParanoidP35235.
KOK07293.
OMAKEYGAMR.
OrthoDBEOG7NPFST.
PhylomeDBP35235.
TreeFamTF351632.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_188576. Developmental Biology.
REACT_200794. Mus musculus biological processes.
SABIO-RKP35235.

Gene expression databases

ArrayExpressP35235.
BgeeP35235.
GenevestigatorP35235.

Family and domain databases

Gene3D3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProIPR029021. 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]
PfamPF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTSM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEPS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN11. mouse.
EvolutionaryTraceP35235.
NextBio296074.
PROP35235.
SOURCESearch...

Entry information

Entry namePTN11_MOUSE
AccessionPrimary (citable) accession number: P35235
Secondary accession number(s): Q3TQ84, Q64509, Q6PCL5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot