P35235 (PTN11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Ptpn11

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	597 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. Ref.22
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.18 Ref.19 Ref.20 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.19
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 component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat SH2 domain
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from mutant phenotype PubMed 12937170. Source: MGI activation of MAPK activity Inferred from mutant phenotype PubMed 12937170PubMed 15273746. Source: MGI axonogenesis Inferred from mutant phenotype PubMed 12482708. Source: MGI ephrin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB 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 multicellular organismal reproductive process Inferred from mutant phenotype PubMed 15520383. 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 insulin secretion Inferred from mutant phenotype PubMed 15520383. Source: MGI nerve growth factor receptor signaling pathway Inferred from mutant phenotype PubMed 12482708. Source: MGI organ growth Inferred from mutant phenotype PubMed 15520383. Source: MGI positive regulation of glucose import in response to insulin stimulus Inferred from electronic annotation. Source: Compara positive regulation of hormone secretion 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_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	non-membrane spanning protein tyrosine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fes	P16879	2	EBI-397236,EBI-771815
Ido1	P28776	5	EBI-397236,EBI-4410822
KIT	P10721	2	EBI-397236,EBI-1379503	From a different organism.
Traf6	P70196	2	EBI-397236,EBI-448028

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 597

597

Tyrosine-protein phosphatase non-receptor type 11

PRO_0000094768

Regions

Domain

6 – 102

97

SH2 1

Domain

112 – 216

105

SH2 2

Domain

247 – 525

279

Tyrosine-protein phosphatase

Region

463 – 469

7

Substrate binding By similarity

Sites

Active site

463

1

Phosphocysteine intermediate By similarity

Binding site

429

1

Substrate By similarity

Binding site

510

1

Substrate By similarity

Amino acid modifications

Modified residue

62

1

Phosphotyrosine Ref.23 Ref.24

Modified residue

63

1

Phosphotyrosine By similarity

Modified residue

66

1

Phosphotyrosine Ref.24

Modified residue

280

1

N6-acetyllysine By similarity

Modified residue

546

1

Phosphotyrosine; by PDGFR Ref.19

Modified residue

562

1

Phosphoserine By similarity

Modified residue

584

1

Phosphotyrosine; by PDGFR Ref.19 Ref.21

Modified residue

595

1

Phosphoserine By similarity

Natural variations

Alternative sequence

408 – 411

4

Missing in isoform 2.

VSP_016675

Experimental info

Sequence conflict

390

1

E → G in BAE37500. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

597

Helix Strand Turn

Details...

Helix

13 – 22

10

Beta strand

28 – 33

6

Beta strand

35 – 37

3

Beta strand

41 – 47

7

Beta strand

50 – 55

6

Beta strand

63 – 68

6

Beta strand

71 – 73

3

Helix

74 – 83

10

Helix

85 – 87

3

Turn

91 – 93

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: C742BED37E39EA23	FASTA	597	68,460
	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
	Isoform 2 [UniParc]. Checksum: 6C71EEEECCF7F159	FASTA	593	68,035
	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 LKLSKVGQGN TERTVWQYHF 430 440 450 460 470 480 RTWPDHGVPS DPGGVLDFLE EVHHKQESIV DAGPVVVHCS AGIGRTGTFI VIDILIDIIR 490 500 510 520 530 540 EKGVDCDIDV PKTIQMVRSQ RSGMVQTEAQ YRFIYMAVQH YIETLQRRIE EEQKSKRKGH 550 560 570 580 590 EYTNIKYSLV DQTSGDQSPL PPCTPTPPCA EMREDSARVY ENVGLMQQQR SFR

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[19]	"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.
[20]	"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.
[21]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-584, MASS SPECTROMETRY.
[22]	"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.
[23]	"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, MASS SPECTROMETRY. Tissue: Mast cell.
[24]	"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, MASS SPECTROMETRY. Tissue: Brain.
[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.

IPI

IPI00116554.
IPI00316479.

PIR

A46209.

RefSeq

NP_001103462.1. NM_001109992.1.
NP_035332.1. NM_011202.3.

UniGene

Mm.474046.
Mm.8681.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P35235.

SMR

P35235. Positions 3-595.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29669N.

IntAct

P35235. 13 interactions.

MINT

MINT-4110032.

PTM databases

PhosphoSite

P35235.

Proteomic databases

PaxDb

P35235.

PRIDE

P35235.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000054547; ENSMUSP00000058757; ENSMUSG00000043733.
ENSMUST00000100770; ENSMUSP00000098333; ENSMUSG00000043733.

GeneID

19247.

KEGG

mmu:19247.

UCSC

uc008zio.2. mouse.
uc008zip.2. mouse.

Organism-specific databases

CTD

5781.

MGI

MGI:99511. Ptpn11.

Phylogenomic databases

eggNOG

COG5599.

GeneTree

ENSGT00700000104166.

HOGENOM

HOG000273907.

HOVERGEN

HBG000223.

InParanoid

P35235.

KO

K07293.

OMA

KEYGAMR.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.
REACT_127416. Developmental Biology.

Gene expression databases

ArrayExpress

P35235.

Bgee

P35235.

Genevestigator

P35235.

GermOnline

ENSMUSG00000043733. Mus musculus.

Family and domain databases

Gene3D

3.30.505.10. 2 hits.

InterPro

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]

Pfam

PF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PIRSF

PIRSF000929. Tyr-Ptase_nr_6. 1 hit.

PRINTS

PR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.

SMART

SM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]

PROSITE

PS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

ProtoNet

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Other

ChEMBL

CHEMBL2620.

ChiTaRS

PTPN11. mouse.

EvolutionaryTrace

P35235.

NextBio

296074.

SOURCE

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Entry information

Entry name

PTN11_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 148 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program