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Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) (Protein-tyrosine phosphatase 1D) (PTP-1D) (Protein-tyrosine phosphatase SYP) (SH-PTP2) (SHP-2) (Shp2)

 PTN11_RAT               Reviewed;         597 AA.
P41499; Q62626;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 4.
25-OCT-2017, entry version 168.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 11;
EC=3.1.3.48 {ECO:0000250|UniProtKB:Q06124};
AltName: Full=Protein-tyrosine phosphatase 1D;
Short=PTP-1D;
AltName: Full=Protein-tyrosine phosphatase SYP;
AltName: Full=SH-PTP2;
Short=SHP-2;
Short=Shp2;
Name=Ptpn11;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley;
PubMed=8048963; DOI=10.1006/bbrc.1994.2015;
Ding W., Zhang W.R., Sullivan K., Hashimoto N., Goldstein B.J.;
"Identification of protein-tyrosine phosphatases prevalent in
adipocytes by molecular cloning.";
Biochem. Biophys. Res. Commun. 202:902-907(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=7512964;
Mei L., Dorherty C.A., Huganir R.L.;
"RNA splicing regulates the activity of a SH2 domain-containing
protein tyrosine phosphatase.";
J. Biol. Chem. 269:12254-12262(1994).
[3]
PARTIAL PROTEIN SEQUENCE.
PubMed=1382983; DOI=10.1111/j.1432-1033.1992.tb17277.x;
Hiraga A., Munakata H., Hata K., Suzuki Y., Tsuiki S.;
"Purification and characterization of a rat liver protein-tyrosine
phosphatase with sequence similarity to src-homology region 2.";
Eur. J. Biochem. 209:195-206(1992).
[4]
INTERACTION WITH PTPNS1.
PubMed=8810330; DOI=10.1074/jbc.271.41.25569;
Ohnishi H., Kubota M., Ohtake A., Sato K., Sano S.;
"Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-
based activation motif of a novel brain molecule.";
J. Biol. Chem. 271:25569-25574(1996).
[5]
INTERACTION WITH PTPNS1.
PubMed=9062191; DOI=10.1038/386181a0;
Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J.,
Ullrich A.;
"A family of proteins that inhibit signalling through tyrosine kinase
receptors.";
Nature 386:181-186(1997).
[6]
INTERACTION WITH ROS1.
PubMed=16885344; DOI=10.1158/0008-5472.CAN-06-1193;
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.;
"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.";
Cancer Res. 66:7473-7481(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Acts downstream of various receptor and cytoplasmic
protein tyrosine kinases to participate in the signal transduction
from the cell surface to the nucleus. Positively regulates MAPK
signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and
EGFR. Dephosphorylates ROCK2 at 'Tyr-722' resulting in
stimulatation of its RhoA binding activity. Dephosphorylates
CDC73. {ECO:0000250|UniProtKB:Q06124}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- ENZYME REGULATION: Inhibited by orthovanadate, molybdate and
spermidine. {ECO:0000269|PubMed:7512964}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15 mM for pNPP {ECO:0000269|PubMed:7512964};
KM=13 uM for nAChR {ECO:0000269|PubMed:7512964};
KM=67 nM for MBP {ECO:0000269|PubMed:7512964};
Vmax=16 umol/min/mg enzyme toward pNPP
{ECO:0000269|PubMed:7512964};
Vmax=98 nmol/min/mg enzyme toward nAChR
{ECO:0000269|PubMed:7512964};
Vmax=15 umol/min/mg enzyme toward MBP
{ECO:0000269|PubMed:7512964};
pH dependence:
Optimum pH is 8.5. {ECO:0000269|PubMed:7512964};
-!- SUBUNIT: Interacts with phosphorylated SIT1, LIME1, BCAR3 and
MZPL1. Interacts with FCRL4, FCRL6, ANKHD1, SHB, INPP5D/SHIP1 and
CD84 (By similarity). Interacts with MILR1 (tyrosine-
phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated),
FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated),
KIT and GRB2 (By similarity). Interacts with PTPNS1. Interacts
with KIR2DL1; the interaction is enhanced by ARRB2. Interacts (via
SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (By
similarity). Interacts with GAB2 (By similarity). 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.
Interacts with PDGFRA (tyrosine phosphorylated). Interacts with
PDGFRB (tyrosine phosphorylated); this interaction increases the
PTPN11 phosphatase activity (By similarity). Interacts with ROS1;
this mediates PTPN11 phosphorylation. Interacts with CEACAM1 (via
cytoplasmic domain); this interaction depends on the monomer/dimer
equilibrium and is phosphorylation-dependent (By similarity).
Interacts with MPIG6B (via ITIM motif) (By similarity). Interacts
with SIGLEC10 (By similarity). {ECO:0000250|UniProtKB:P35235,
ECO:0000250|UniProtKB:Q06124, ECO:0000269|PubMed:16885344,
ECO:0000269|PubMed:8810330, ECO:0000269|PubMed:9062191}.
-!- INTERACTION:
Q62689:Jak2; NbExp=3; IntAct=EBI-7180604, EBI-8656708;
P97710:Sirpa; NbExp=3; IntAct=EBI-7180604, EBI-7945080;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PTP1Di;
IsoId=P41499-1; Sequence=Displayed;
Name=2; Synonyms=PTP1D;
IsoId=P41499-2; Sequence=VSP_016676;
Note=Much higher phosphatase activity than isoform 1, optimum pH
is 7.;
-!- TISSUE SPECIFICITY: Expressed in brain, muscle and lung.
{ECO:0000269|PubMed:7512964}.
-!- 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.
-!- PTM: 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 upon activation
of the receptor-type kinase PDGFRA. Phosphorylated by activated
PDGFRB (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class 2 subfamily. {ECO:0000305}.
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EMBL; U09307; AAA20543.1; -; mRNA.
EMBL; U05963; AAA19133.1; -; mRNA.
PIR; A53593; A53593.
RefSeq; NP_001171064.1; NM_001177593.1. [P41499-1]
RefSeq; NP_037220.2; NM_013088.2. [P41499-2]
UniGene; Rn.98209; -.
ProteinModelPortal; P41499; -.
SMR; P41499; -.
BioGrid; 247651; 3.
CORUM; P41499; -.
DIP; DIP-47397N; -.
ELM; P41499; -.
IntAct; P41499; 11.
MINT; MINT-4591731; -.
STRING; 10116.ENSRNOP00000041842; -.
iPTMnet; P41499; -.
PhosphoSitePlus; P41499; -.
PaxDb; P41499; -.
PRIDE; P41499; -.
Ensembl; ENSRNOT00000046323; ENSRNOP00000041842; ENSRNOG00000030124. [P41499-1]
GeneID; 25622; -.
KEGG; rno:25622; -.
UCSC; RGD:3447; rat. [P41499-1]
CTD; 5781; -.
RGD; 3447; Ptpn11.
eggNOG; KOG0790; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00900000140780; -.
HOGENOM; HOG000273907; -.
HOVERGEN; HBG000223; -.
InParanoid; P41499; -.
KO; K07293; -.
OMA; KEYGAMR; -.
OrthoDB; EOG091G0VZ3; -.
PhylomeDB; P41499; -.
TreeFam; TF351632; -.
Reactome; R-RNO-109704; PI3K Cascade.
Reactome; R-RNO-110056; MAPK3 (ERK1) activation.
Reactome; R-RNO-112411; MAPK1 (ERK2) activation.
Reactome; R-RNO-114604; GPVI-mediated activation cascade.
Reactome; R-RNO-1170546; Prolactin receptor signaling.
Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
Reactome; R-RNO-1295596; Spry regulation of FGF signaling.
Reactome; R-RNO-1433557; Signaling by SCF-KIT.
Reactome; R-RNO-180292; GAB1 signalosome.
Reactome; R-RNO-186763; Downstream signal transduction.
Reactome; R-RNO-210993; Tie2 Signaling.
Reactome; R-RNO-388841; Costimulation by the CD28 family.
Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
Reactome; R-RNO-389948; PD-1 signaling.
Reactome; R-RNO-391160; Signal regulatory protein family interactions.
Reactome; R-RNO-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-RNO-5654689; PI-3K cascade:FGFR1.
Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-RNO-5654695; PI-3K cascade:FGFR2.
Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-RNO-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-RNO-5654710; PI-3K cascade:FGFR3.
Reactome; R-RNO-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-RNO-5654720; PI-3K cascade:FGFR4.
Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-RNO-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-RNO-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-RNO-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-RNO-6783589; Interleukin-6 family signaling.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-RNO-8853659; RET signaling.
Reactome; R-RNO-8865999; MET activates PTPN11.
Reactome; R-RNO-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-RNO-909733; Interferon alpha/beta signaling.
Reactome; R-RNO-912694; Regulation of IFNA signaling.
PRO; PR:P41499; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000030124; -.
Genevisible; P41499; RN.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
GO; GO:0005158; F:insulin receptor binding; IDA:RGD.
GO; GO:0043560; F:insulin receptor substrate binding; IPI:RGD.
GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0051428; F:peptide hormone receptor binding; IEA:Ensembl.
GO; GO:0043274; F:phospholipase binding; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:RGD.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IEA:Ensembl.
GO; GO:0033277; P:abortive mitotic cell cycle; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0036302; P:atrioventricular canal development; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IPI:RGD.
GO; GO:0021697; P:cerebellar cortex formation; IEA:Ensembl.
GO; GO:0000077; P:DNA damage checkpoint; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0048806; P:genitalia development; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:Ensembl.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0061582; P:intestinal epithelial cell migration; IEA:Ensembl.
GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
GO; GO:0032528; P:microvillus organization; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0048609; P:multicellular organismal reproductive process; IEA:Ensembl.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0051463; P:negative regulation of cortisol secretion; IEA:Ensembl.
GO; GO:0060125; P:negative regulation of growth hormone secretion; IEA:Ensembl.
GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
GO; GO:0035265; P:organ growth; IEA:Ensembl.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
GO; GO:0030220; P:platelet formation; IEA:Ensembl.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
GO; GO:0046887; P:positive regulation of hormone secretion; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0043254; P:regulation of protein complex assembly; IEA:Ensembl.
GO; GO:0046825; P:regulation of protein export from nucleus; IEA:Ensembl.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
Gene3D; 3.30.505.10; -; 2.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00017; SH2; 2.
Pfam; PF00102; Y_phosphatase; 1.
PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
PRINTS; PR00700; PRTYPHPHTASE.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SMART; SM00252; SH2; 2.
SUPFAM; SSF52799; SSF52799; 1.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50001; SH2; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Phosphoprotein;
Protein phosphatase; Reference proteome; Repeat; SH2 domain.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q06124}.
CHAIN 2 597 Tyrosine-protein phosphatase non-receptor
type 11.
/FTId=PRO_0000094769.
DOMAIN 6 102 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 112 216 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 247 521 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 463 469 Substrate binding. {ECO:0000250}.
ACT_SITE 463 463 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044}.
BINDING 429 429 Substrate. {ECO:0000250}.
BINDING 510 510 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:Q06124}.
MOD_RES 62 62 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 66 66 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35235}.
MOD_RES 546 546 Phosphotyrosine; by PDGFR.
{ECO:0000250|UniProtKB:P35235}.
MOD_RES 584 584 Phosphotyrosine; by PDGFR.
{ECO:0000250|UniProtKB:Q06124}.
VAR_SEQ 409 412 Missing (in isoform 2).
{ECO:0000303|PubMed:7512964,
ECO:0000303|PubMed:8048963}.
/FTId=VSP_016676.
CONFLICT 75 75 A -> P (in Ref. 1; AAA20543).
{ECO:0000305}.
CONFLICT 551 551 Y -> S (in Ref. 2; AAA19133).
{ECO:0000305}.
SEQUENCE 597 AA; 68458 MW; 7155D1E99161F5C2 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 LKLSKVGQAL LQGNTERTVW
QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ ESIVDAGPVV VHCSAGIGRT GTFIVIDILI
DIIREKGVDC DIDVPKTIQM VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK
RKGHEYTNIK YSLVDQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQRSFR


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10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.001 mg
PP-SHP1-020 SHP-1, Tyrosine-protein phosphatase non-receptor type 6, EC 3.1.3.48, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SH 20
EIAAB33048 Mouse,Mus musculus,Neural-specific protein-tyrosine phosphatase,Ptpn5,STEP,Striatum-enriched protein-tyrosine phosphatase,Tyrosine-protein phosphatase non-receptor type 5
EIAAB33049 Neural-specific protein-tyrosine phosphatase,Ptpn5,Rat,Rattus norvegicus,STEP,Striatum-enriched protein-tyrosine phosphatase,Tyrosine-protein phosphatase non-receptor type 5
EIAAB33094 Byp,HPTP beta-like tyrosine phosphatase,Mouse,Mus musculus,Protein-tyrosine phosphatase eta,Protein-tyrosine phosphatase receptor type J,Ptprj,Receptor-type tyrosine-protein phosphatase eta,R-PTP-eta,
EIAAB33117 FMI,Homo sapiens,hPTP-J,Human,Pancreatic carcinoma phosphatase 2,PCP2,PCP-2,Protein-tyrosine phosphatase J,Protein-tyrosine phosphatase pi,Protein-tyrosine phosphatase receptor omicron,PTP pi,PTP-J,PT
EIAAB33107 PC12-PTP1,Protein-tyrosine phosphatase PCPTP1,Ptp,Ptprr,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase R,R-PTP-R,Tyrosine phosphatase CBPTP
EIAAB33056 Hematopoietic protein-tyrosine phosphatase,HEPTP,Lcptp,Protein-tyrosine phosphatase LC-PTP,Ptpn7,Rat,Rattus norvegicus,Tyrosine-protein phosphatase non-receptor type 7
EIAAB33054 Hematopoietic protein-tyrosine phosphatase,HEPTP,Homo sapiens,Human,Protein-tyrosine phosphatase LC-PTP,PTPN7,Tyrosine-protein phosphatase non-receptor type 7


 

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