PTN11_RAT
ID PTN11_RAT Reviewed; 593 AA.
AC P41499; Q62626;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 5.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 11;
DE EC=3.1.3.48 {ECO:0000269|PubMed:7512964};
DE AltName: Full=Protein-tyrosine phosphatase 1D;
DE Short=PTP-1D;
DE AltName: Full=Protein-tyrosine phosphatase SYP;
DE AltName: Full=SH-PTP2;
DE Short=SHP-2;
DE Short=Shp2;
GN Name=Ptpn11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RX PubMed=8048963; DOI=10.1006/bbrc.1994.2015;
RA Ding W., Zhang W.R., Sullivan K., Hashimoto N., Goldstein B.J.;
RT "Identification of protein-tyrosine phosphatases prevalent in adipocytes by
RT molecular cloning.";
RL Biochem. Biophys. Res. Commun. 202:902-907(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7512964; DOI=10.1016/s0021-9258(17)32709-6;
RA Mei L., Dorherty C.A., Huganir R.L.;
RT "RNA splicing regulates the activity of a SH2 domain-containing protein
RT tyrosine phosphatase.";
RL J. Biol. Chem. 269:12254-12262(1994).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1382983; DOI=10.1111/j.1432-1033.1992.tb17277.x;
RA Hiraga A., Munakata H., Hata K., Suzuki Y., Tsuiki S.;
RT "Purification and characterization of a rat liver protein-tyrosine
RT phosphatase with sequence similarity to src-homology region 2.";
RL Eur. J. Biochem. 209:195-206(1992).
RN [4]
RP INTERACTION WITH PTPNS1.
RX PubMed=8810330; DOI=10.1074/jbc.271.41.25569;
RA Ohnishi H., Kubota M., Ohtake A., Sato K., Sano S.;
RT "Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based
RT activation motif of a novel brain molecule.";
RL J. Biol. Chem. 271:25569-25574(1996).
RN [5]
RP INTERACTION WITH PTPNS1.
RX PubMed=9062191; DOI=10.1038/386181a0;
RA Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A.;
RT "A family of proteins that inhibit signalling through tyrosine kinase
RT receptors.";
RL Nature 386:181-186(1997).
RN [6]
RP INTERACTION WITH ROS1.
RX PubMed=16885344; DOI=10.1158/0008-5472.can-06-1193;
RA Charest A., Wilker E.W., McLaughlin M.E., Lane K., Gowda R., Coven S.,
RA McMahon K., Kovach S., Feng Y., Yaffe M.B., Jacks T., Housman D.;
RT "ROS fusion tyrosine kinase activates a SH2 domain-containing phosphatase-
RT 2/phosphatidylinositol 3-kinase/mammalian target of rapamycin signaling
RT axis to form glioblastoma in mice.";
RL Cancer Res. 66:7473-7481(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts downstream of various receptor and cytoplasmic protein
CC tyrosine kinases to participate in the signal transduction from the
CC cell surface to the nucleus (By similarity). Positively regulates MAPK
CC signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR.
CC Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its
CC RhoA binding activity. Dephosphorylates CDC73 (By similarity).
CC Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9
CC and promote ossification (By similarity).
CC {ECO:0000250|UniProtKB:P35235, ECO:0000250|UniProtKB:Q06124}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:7512964};
CC -!- ACTIVITY REGULATION: Inhibited by orthovanadate, molybdate and
CC spermidine. {ECO:0000269|PubMed:7512964}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 mM for pNPP (isoform 1) {ECO:0000269|PubMed:7512964};
CC KM=48 uM for nAChR (isoform 1) {ECO:0000269|PubMed:7512964};
CC KM=1.3 uM for MBP (isoform 1) {ECO:0000269|PubMed:7512964};
CC KM=15 mM for pNPP (isoform 2) {ECO:0000269|PubMed:7512964};
CC KM=13 uM for nAChR (isoform 2) {ECO:0000269|PubMed:7512964};
CC KM=0.067 uM for MBP (isoform 2) {ECO:0000269|PubMed:7512964};
CC Vmax=120 umol/min/mg enzyme toward pNPP (isoform 1)
CC {ECO:0000269|PubMed:7512964};
CC Vmax=220 nmol/min/mg enzyme toward nAChR (isoform 1)
CC {ECO:0000269|PubMed:7512964};
CC Vmax=210 nmol/min/mg enzyme toward MBP (isoform 1)
CC {ECO:0000269|PubMed:7512964};
CC Vmax=16 umol/min/mg enzyme toward pNPP (isoform 2)
CC {ECO:0000269|PubMed:7512964};
CC Vmax=98 nmol/min/mg enzyme toward nAChR (isoform 2)
CC {ECO:0000269|PubMed:7512964};
CC Vmax=15 nmol/min/mg enzyme toward MBP (isoform 2)
CC {ECO:0000269|PubMed:7512964};
CC pH dependence:
CC Optimum pH is 7.0-7.5 (isoform 1). Optimum pH is 8.5 (isoform 2).
CC {ECO:0000269|PubMed:7512964};
CC -!- SUBUNIT: Interacts with phosphorylated SIT1, LIME1, BCAR3 and MZPL1.
CC Interacts with FCRL4, FCRL6, ANKHD1, SHB, INPP5D/SHIP1 and CD84 (By
CC similarity). Interacts with MILR1 (tyrosine-phosphorylated). Interacts
CC with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated),
CC FLT4 (tyrosine-phosphorylated), KIT and GRB2 (By similarity). Interacts
CC with PTPNS1. Interacts with KIR2DL1; the interaction is enhanced by
CC ARRB2. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine
CC phosphorylated) (By similarity). Interacts with GAB2 (By similarity).
CC Interacts with TERT; the interaction retains TERT in the nucleus.
CC Interacts with PECAM1 and FER. Interacts with EPHA2 (activated);
CC participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream
CC signaling. Interacts with PDGFRA (tyrosine phosphorylated). Interacts
CC with PDGFRB (tyrosine phosphorylated); this interaction increases the
CC PTPN11 phosphatase activity (By similarity). Interacts with ROS1; this
CC mediates PTPN11 phosphorylation. Interacts with CEACAM1 (via
CC cytoplasmic domain); this interaction depends on the monomer/dimer
CC equilibrium and is phosphorylation-dependent (By similarity). Interacts
CC with MPIG6B (via ITIM motif) (By similarity). Interacts with SIGLEC10
CC (By similarity). Interacts with CLEC12B (via ITIM motif); this
CC interaction triggers dephosphorylation and activation of PTPN11.
CC {ECO:0000250|UniProtKB:P35235, ECO:0000250|UniProtKB:Q06124,
CC ECO:0000269|PubMed:16885344, ECO:0000269|PubMed:8810330,
CC ECO:0000269|PubMed:9062191}.
CC -!- INTERACTION:
CC P41499; Q62689: Jak2; NbExp=3; IntAct=EBI-7180604, EBI-8656708;
CC P41499; P97710: Sirpa; NbExp=3; IntAct=EBI-7180604, EBI-7945080;
CC P41499; P09619: PDGFRB; Xeno; NbExp=4; IntAct=EBI-7180604, EBI-641237;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PTP1D;
CC IsoId=P41499-2; Sequence=Displayed;
CC Name=2; Synonyms=PTP1Di;
CC IsoId=P41499-1; Sequence=VSP_060441;
CC -!- TISSUE SPECIFICITY: Expressed in brain, muscle and lung.
CC {ECO:0000269|PubMed:7512964}.
CC -!- DOMAIN: The SH2 domains repress phosphatase activity. Binding of these
CC domains to phosphotyrosine-containing proteins relieves this auto-
CC inhibition, possibly by inducing a conformational change in the enzyme.
CC -!- PTM: Phosphorylated on Tyr-542 and Tyr-580 upon receptor protein
CC tyrosine kinase activation; which creates a binding site for GRB2 and
CC other SH2-containing proteins. Phosphorylated upon activation of the
CC receptor-type kinase FLT3. Phosphorylated upon activation of the
CC receptor-type kinase PDGFRA. Phosphorylated by activated PDGFRB (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 2 subfamily. {ECO:0000305}.
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DR EMBL; U09307; AAA20543.1; -; mRNA.
DR EMBL; U05963; AAA19133.1; -; mRNA.
DR PIR; A53593; A53593.
DR RefSeq; NP_001171064.1; NM_001177593.1. [P41499-1]
DR RefSeq; NP_037220.2; NM_013088.2. [P41499-2]
DR AlphaFoldDB; P41499; -.
DR SMR; P41499; -.
DR BioGRID; 247651; 6.
DR CORUM; P41499; -.
DR DIP; DIP-47397N; -.
DR ELM; P41499; -.
DR IntAct; P41499; 31.
DR MINT; P41499; -.
DR STRING; 10116.ENSRNOP00000041842; -.
DR iPTMnet; P41499; -.
DR PhosphoSitePlus; P41499; -.
DR jPOST; P41499; -.
DR PaxDb; P41499; -.
DR PRIDE; P41499; -.
DR GeneID; 25622; -.
DR KEGG; rno:25622; -.
DR UCSC; RGD:3447; rat. [P41499-2]
DR CTD; 5781; -.
DR RGD; 3447; Ptpn11.
DR VEuPathDB; HostDB:ENSRNOG00000030124; -.
DR eggNOG; KOG0790; Eukaryota.
DR HOGENOM; CLU_001645_9_10_1; -.
DR InParanoid; P41499; -.
DR OMA; KYYIATQ; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P41499; -.
DR TreeFam; TF351632; -.
DR Reactome; R-RNO-1059683; Interleukin-6 signaling.
DR Reactome; R-RNO-109704; PI3K Cascade.
DR Reactome; R-RNO-110056; MAPK3 (ERK1) activation.
DR Reactome; R-RNO-112411; MAPK1 (ERK2) activation.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-1295596; Spry regulation of FGF signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-180292; GAB1 signalosome.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-210990; PECAM1 interactions.
DR Reactome; R-RNO-210993; Tie2 Signaling.
DR Reactome; R-RNO-388841; Costimulation by the CD28 family.
DR Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
DR Reactome; R-RNO-389948; PD-1 signaling.
DR Reactome; R-RNO-432142; Platelet sensitization by LDL.
DR Reactome; R-RNO-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-RNO-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-RNO-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-RNO-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-RNO-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-RNO-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-RNO-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-RNO-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-RNO-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-RNO-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-8853659; RET signaling.
DR Reactome; R-RNO-8854691; Interleukin-20 family signaling.
DR Reactome; R-RNO-8865999; MET activates PTPN11.
DR Reactome; R-RNO-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-RNO-912694; Regulation of IFNA/IFNB signaling.
DR Reactome; R-RNO-9674555; Signaling by CSF3 (G-CSF).
DR PRO; PR:P41499; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000030124; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; P41499; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0044853; C:plasma membrane raft; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0005158; F:insulin receptor binding; IDA:RGD.
DR GO; GO:0043560; F:insulin receptor substrate binding; IPI:RGD.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0051428; F:peptide hormone receptor binding; ISO:RGD.
DR GO; GO:0043274; F:phospholipase binding; IDA:RGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISO:RGD.
DR GO; GO:0033277; P:abortive mitotic cell cycle; ISO:RGD.
DR GO; GO:0036302; P:atrioventricular canal development; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IPI:RGD.
DR GO; GO:0021697; P:cerebellar cortex formation; ISO:RGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:RGD.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0038127; P:ERBB signaling pathway; ISO:RGD.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0048806; P:genitalia development; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0042445; P:hormone metabolic process; ISO:RGD.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0061582; P:intestinal epithelial cell migration; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0035855; P:megakaryocyte development; ISO:RGD.
DR GO; GO:0032528; P:microvillus organization; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0048609; P:multicellular organismal reproductive process; ISO:RGD.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0051463; P:negative regulation of cortisol secretion; ISO:RGD.
DR GO; GO:0060125; P:negative regulation of growth hormone secretion; ISO:RGD.
DR GO; GO:0046888; P:negative regulation of hormone secretion; ISO:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:RGD.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISO:RGD.
DR GO; GO:0035265; P:organ growth; ISO:RGD.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030220; P:platelet formation; ISO:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:RGD.
DR GO; GO:0046887; P:positive regulation of hormone secretion; ISO:RGD.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0045778; P:positive regulation of ossification; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0009967; P:positive regulation of signal transduction; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISO:RGD.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0048659; P:smooth muscle cell proliferation; IEP:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR Gene3D; 3.30.505.10; -; 2.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
KW SH2 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q06124"
FT CHAIN 2..593
FT /note="Tyrosine-protein phosphatase non-receptor type 11"
FT /id="PRO_0000094769"
FT DOMAIN 6..102
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 112..216
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 247..517
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 459
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 459..465
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06124"
FT MOD_RES 62
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 66
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35235"
FT MOD_RES 542
FT /note="Phosphotyrosine; by PDGFR"
FT /evidence="ECO:0000250|UniProtKB:P35235"
FT MOD_RES 580
FT /note="Phosphotyrosine; by PDGFR"
FT /evidence="ECO:0000250|UniProtKB:Q06124"
FT VAR_SEQ 407
FT /note="G -> GQALL (in isoform 2)"
FT /id="VSP_060441"
FT CONFLICT 75
FT /note="A -> P (in Ref. 1; AAA20543)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="Y -> S (in Ref. 2; AAA19133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 68033 MW; 3329F10F0F60AF48 CRC64;
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA VTHIKIQNTG
DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY PLNCADPTSE RWFHGHLSGK
EAEKLLTEKG KHGSFLVRES QSHPGDFVLS VRTGDDKGES NDSKSKVTHV MIRCQELKYD
VGGGERFDSL TDLVEHYKKN PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT
DKVKQGFWEE FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS RVIVMTTKEV
ERGKSKCVKY WPDECALKEY GVMRVRNVRE SAAHDYTLRE LKLSKVGQGN TERTVWQYHF
RTWPDHGVPS DPGGVLDFLE EVHHKQESIV DAGPVVVHCS AGIGRTGTFI VIDILIDIIR
EKGVDCDIDV PKTIQMVRSQ RSGMVQTEAQ YRFIYMAVQH YIETLQRRIE EEQKSKRKGH
EYTNIKYSLV DQTSGDQSPL PPCTPTPPCA EMREDSARVY ENVGLMQQQR SFR
