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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)DescriptionActionsGraphical viewLength
Binding sitei429SubstrateBy similarity1
Active sitei463Phosphocysteine intermediatePROSITE-ProRule annotation1
Binding sitei510SubstrateBy similarity1

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB
  • insulin receptor binding Source: MGI
  • non-membrane spanning protein tyrosine phosphatase activity Source: UniProtKB
  • peptide hormone receptor binding Source: MGI
  • phosphoprotein phosphatase activity Source: MGI
  • protein tyrosine phosphatase activity Source: MGI
  • receptor tyrosine kinase binding Source: UniProtKB
  • SH3/SH2 adaptor activity Source: MGI

GO - Biological processi

  • abortive mitotic cell cycle Source: MGI
  • activation of MAPK activity Source: MGI
  • atrioventricular canal development Source: MGI
  • axonogenesis Source: MGI
  • Bergmann glial cell differentiation Source: MGI
  • brain development Source: MGI
  • cerebellar cortex formation Source: MGI
  • DNA damage checkpoint Source: MGI
  • ephrin receptor signaling pathway Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: MGI
  • ERBB signaling pathway Source: MGI
  • face morphogenesis Source: MGI
  • genitalia development Source: MGI
  • glucose homeostasis Source: MGI
  • heart development Source: MGI
  • homeostasis of number of cells within a tissue Source: MGI
  • hormone-mediated signaling pathway Source: MGI
  • hormone metabolic process Source: MGI
  • inner ear development Source: MGI
  • integrin-mediated signaling pathway Source: MGI
  • intestinal epithelial cell migration Source: MGI
  • lipid metabolic process Source: MGI
  • megakaryocyte development Source: MGI
  • microvillus organization Source: MGI
  • multicellular organismal reproductive process Source: MGI
  • multicellular organism growth Source: MGI
  • negative regulation of cell adhesion mediated by integrin Source: MGI
  • negative regulation of cortisol secretion Source: MGI
  • negative regulation of growth hormone secretion Source: MGI
  • negative regulation of hormone secretion Source: MGI
  • negative regulation of insulin secretion Source: MGI
  • neurotrophin TRK receptor signaling pathway Source: MGI
  • organ growth Source: MGI
  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
  • platelet-derived growth factor receptor signaling pathway Source: MGI
  • platelet formation Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of glucose import in response to insulin stimulus Source: MGI
  • positive regulation of hormone secretion Source: MGI
  • positive regulation of mitotic cell cycle Source: MGI
  • positive regulation of signal transduction Source: MGI
  • regulation of cell adhesion mediated by integrin Source: UniProtKB
  • regulation of multicellular organism growth Source: MGI
  • regulation of protein complex assembly Source: MGI
  • regulation of protein export from nucleus Source: MGI
  • triglyceride metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiR-MMU-1059683. Interleukin-6 signaling.
R-MMU-109704. PI3K Cascade.
R-MMU-110056. MAPK3 (ERK1) activation.
R-MMU-112411. MAPK1 (ERK2) activation.
R-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1295596. Spry regulation of FGF signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-180292. GAB1 signalosome.
R-MMU-186763. Downstream signal transduction.
R-MMU-210993. Tie2 Signaling.
R-MMU-2586551. Signaling by Leptin.
R-MMU-2586552. Signaling by Leptin.
R-MMU-388841. Costimulation by the CD28 family.
R-MMU-389513. CTLA4 inhibitory signaling.
R-MMU-389948. PD-1 signaling.
R-MMU-418886. Netrin mediated repulsion signals.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654693. FRS-mediated FGFR1 signaling.
R-MMU-5654695. PI-3K cascade:FGFR2.
R-MMU-5654699. SHC-mediated cascade:FGFR2.
R-MMU-5654700. FRS-mediated FGFR2 signaling.
R-MMU-5654706. FRS-mediated FGFR3 signaling.
R-MMU-5654710. PI-3K cascade:FGFR3.
R-MMU-5654712. FRS-mediated FGFR4 signaling.
R-MMU-5654719. SHC-mediated cascade:FGFR4.
R-MMU-5654720. PI-3K cascade:FGFR4.
R-MMU-5654726. Negative regulation of FGFR1 signaling.
R-MMU-5654727. Negative regulation of FGFR2 signaling.
R-MMU-5654732. Negative regulation of FGFR3 signaling.
R-MMU-5654733. Negative regulation of FGFR4 signaling.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-8853659. RET signaling.
R-MMU-8865999. MET activates PTPN11.
R-MMU-909733. Interferon alpha/beta signaling.
R-MMU-912694. Regulation of IFNA 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
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:99511. Ptpn11.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000947682 – 597Tyrosine-protein phosphatase non-receptor type 11Add BLAST596

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Modified residuei62PhosphotyrosineCombined sources1
Modified residuei66PhosphotyrosineCombined sources1
Modified residuei546Phosphotyrosine; by PDGFR1 Publication1
Modified residuei584Phosphotyrosine; by PDGFR1 Publication1

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

EPDiP35235.
MaxQBiP35235.
PaxDbiP35235.
PeptideAtlasiP35235.
PRIDEiP35235.

PTM databases

iPTMnetiP35235.
PhosphoSitePlusiP35235.

Expressioni

Tissue specificityi

Highly expressed in brain, heart and kidney.1 Publication

Gene expression databases

BgeeiENSMUSG00000043733.
GenevisibleiP35235. MM.

Interactioni

Subunit structurei

Interacts with CD84 and with phosphorylated SIT1 and MZPL1. Interacts with FCRL3, FCRL4, FCRL6 and ANKHD1. Interacts with GAREM1 (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). Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (PubMed:19948503, PubMed:9867848).By similarity18 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

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB
  • insulin receptor binding Source: MGI
  • peptide hormone receptor binding Source: MGI
  • receptor tyrosine kinase binding Source: UniProtKB
  • SH3/SH2 adaptor activity Source: MGI

Protein-protein interaction databases

BioGridi202477. 25 interactors.
DIPiDIP-29669N.
IntActiP35235. 30 interactors.
MINTiMINT-4110032.
STRINGi10090.ENSMUSP00000058757.

Structurei

Secondary structure

1597
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 22Combined sources10
Beta strandi28 – 33Combined sources6
Beta strandi35 – 37Combined sources3
Beta strandi41 – 47Combined sources7
Beta strandi50 – 55Combined sources6
Beta strandi63 – 68Combined sources6
Beta strandi71 – 73Combined sources3
Helixi74 – 83Combined sources10
Helixi85 – 87Combined sources3
Turni91 – 93Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP35235.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 102SH2 1PROSITE-ProRule annotationAdd BLAST97
Domaini112 – 216SH2 2PROSITE-ProRule annotationAdd BLAST105
Domaini247 – 525Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST279

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni463 – 469Substrate bindingBy similarity7

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

eggNOGiKOG0790. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiP35235.
KOiK07293.
OMAiKEYGAMR.
OrthoDBiEOG091G0VZ3.
PhylomeDBiP35235.
TreeFamiTF351632.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR000980. SH2.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
IPR000387. TYR_PHOSPHATASE_dom.
[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.
SM00404. PTPc_motif. 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)DescriptionActionsGraphical viewLength
Sequence conflicti390E → G in BAE37500 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_016675408 – 411Missing in isoform 2. 2 Publications4

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYAX-ray2.05A/B4-103[»]
1AYBX-ray3.00A4-103[»]
1AYCX-ray2.30A4-103[»]
1AYDX-ray2.20A4-103[»]
ProteinModelPortaliP35235.
SMRiP35235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202477. 25 interactors.
DIPiDIP-29669N.
IntActiP35235. 30 interactors.
MINTiMINT-4110032.
STRINGi10090.ENSMUSP00000058757.

Chemistry databases

ChEMBLiCHEMBL2620.

PTM databases

iPTMnetiP35235.
PhosphoSitePlusiP35235.

Proteomic databases

EPDiP35235.
MaxQBiP35235.
PaxDbiP35235.
PeptideAtlasiP35235.
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

eggNOGiKOG0790. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiP35235.
KOiK07293.
OMAiKEYGAMR.
OrthoDBiEOG091G0VZ3.
PhylomeDBiP35235.
TreeFamiTF351632.

Enzyme and pathway databases

ReactomeiR-MMU-1059683. Interleukin-6 signaling.
R-MMU-109704. PI3K Cascade.
R-MMU-110056. MAPK3 (ERK1) activation.
R-MMU-112411. MAPK1 (ERK2) activation.
R-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1295596. Spry regulation of FGF signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-180292. GAB1 signalosome.
R-MMU-186763. Downstream signal transduction.
R-MMU-210993. Tie2 Signaling.
R-MMU-2586551. Signaling by Leptin.
R-MMU-2586552. Signaling by Leptin.
R-MMU-388841. Costimulation by the CD28 family.
R-MMU-389513. CTLA4 inhibitory signaling.
R-MMU-389948. PD-1 signaling.
R-MMU-418886. Netrin mediated repulsion signals.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654693. FRS-mediated FGFR1 signaling.
R-MMU-5654695. PI-3K cascade:FGFR2.
R-MMU-5654699. SHC-mediated cascade:FGFR2.
R-MMU-5654700. FRS-mediated FGFR2 signaling.
R-MMU-5654706. FRS-mediated FGFR3 signaling.
R-MMU-5654710. PI-3K cascade:FGFR3.
R-MMU-5654712. FRS-mediated FGFR4 signaling.
R-MMU-5654719. SHC-mediated cascade:FGFR4.
R-MMU-5654720. PI-3K cascade:FGFR4.
R-MMU-5654726. Negative regulation of FGFR1 signaling.
R-MMU-5654727. Negative regulation of FGFR2 signaling.
R-MMU-5654732. Negative regulation of FGFR3 signaling.
R-MMU-5654733. Negative regulation of FGFR4 signaling.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-8853659. RET signaling.
R-MMU-8865999. MET activates PTPN11.
R-MMU-909733. Interferon alpha/beta signaling.
R-MMU-912694. Regulation of IFNA signaling.
SABIO-RKP35235.

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000043733.
GenevisibleiP35235. MM.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR000980. SH2.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
IPR000387. TYR_PHOSPHATASE_dom.
[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.
SM00404. PTPc_motif. 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...

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: November 30, 2016
This is version 186 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

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 one 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.