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Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (70Z-SHP) (Hematopoietic cell protein-tyrosine phosphatase) (PTPTY-42) (Protein-tyrosine phosphatase 1C) (PTP-1C) (SH-PTP1) (SHP-1)

 PTN6_MOUSE              Reviewed;         595 AA.
P29351; O35128; Q63872; Q63873; Q63874; Q921G3; Q9QVA6; Q9QVA7;
Q9QVA8; Q9R0V6;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
11-JUL-2002, sequence version 2.
28-MAR-2018, entry version 192.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 6;
EC=3.1.3.48;
AltName: Full=70Z-SHP;
AltName: Full=Hematopoietic cell protein-tyrosine phosphatase;
AltName: Full=PTPTY-42;
AltName: Full=Protein-tyrosine phosphatase 1C;
Short=PTP-1C;
AltName: Full=SH-PTP1;
Short=SHP-1;
Name=Ptpn6; Synonyms=Hcp, Hcph, Ptp1C;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=DBA/2J;
PubMed=1732748; DOI=10.1128/MCB.12.2.836;
Yi T., Cleveland J.L., Ihle J.N.;
"Protein tyrosine phosphatase containing SH2 domains:
characterization, preferential expression in hematopoietic cells, and
localization to human chromosome 12p12-p13.";
Mol. Cell. Biol. 12:836-846(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1373816; DOI=10.1128/MCB.12.5.2396;
Matthews R.J., Bowne D.B., Flores E., Thomas M.L.;
"Characterization of hematopoietic intracellular protein tyrosine
phosphatases: description of a phosphatase containing an SH2 domain
and another enriched in proline-, glutamic acid-, serine-, and
threonine-rich sequences.";
Mol. Cell. Biol. 12:2396-2405(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MOTHEATEN AND VIABLE
MOTHEATEN.
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=8324828; DOI=10.1016/0092-8674(93)90369-2;
Schultz L.D., Schweitzer P.A., Rajan T.V., Yi T., Ihle J.N.,
Matthews R.J., Thomas M.L., Beier D.R.;
"Mutations at the murine motheaten locus are within the hematopoietic
cell protein-tyrosine phosphatase (Hcph) gene.";
Cell 73:1445-1454(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
PubMed=9445485;
Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
Gibbs R.A.;
"Comparative sequence analysis of a gene-rich cluster at human
chromosome 12p13 and its syntenic region in mouse chromosome 6.";
Genome Res. 8:29-40(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND SUBUNIT.
STRAIN=C3H/HeJ; TISSUE=Adrenal gland;
PubMed=10419485; DOI=10.1074/jbc.274.31.21725;
Martin A., Tsui H.W., Shulman M.J., Isenman D., Tsui F.W.;
"Murine SHP-1 splice variants with altered Src homology 2 (SH2)
domains. Implications for the SH2-mediated intramolecular regulation
of SHP-1.";
J. Biol. Chem. 274:21725-21734(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 54-68; 128-135; 137-151; 242-252; 278-285; 293-308
AND 373-382, AND PHOSPHORYLATION.
PubMed=1385421;
Yeung Y.-G., Berg K.L., Pixley F.J., Angeletti R.H., Stanley E.R.;
"Protein tyrosine phosphatase-1C is rapidly phosphorylated in tyrosine
in macrophages in response to colony stimulating factor-1.";
J. Biol. Chem. 267:23447-23450(1992).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 342-451, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Myeloid leukemia cell;
PubMed=1932742;
Yi T., Cleveland J.L., Ihle J.N.;
"Identification of novel protein tyrosine phosphatases of
hematopoietic cells by polymerase chain reaction amplification.";
Blood 78:2222-2228(1991).
[9]
INTERACTION WITH SIRPA.
PubMed=9712903; DOI=10.1074/jbc.273.35.22719;
Veillette A., Thibaudeau E., Latour S.;
"High expression of inhibitory receptor SHPS-1 and its association
with protein tyrosine phosphatase SHP-1 in macrophages.";
J. Biol. Chem. 273:22719-22728(1998).
[10]
INTERACTION WITH KIT, FUNCTION IN MODULATING KIT SIGNALING, AND
PHOSPHORYLATION.
PubMed=9528781; DOI=10.1128/MCB.18.4.2089;
Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R.,
Siminovitch K.A.;
"SHP-1 binds and negatively modulates the c-Kit receptor by
interaction with tyrosine 569 in the c-Kit juxtamembrane domain.";
Mol. Cell. Biol. 18:2089-2099(1998).
[11]
INTERACTION WITH CEACAM1.
PubMed=9867848; DOI=10.1074/jbc.274.1.335;
Huber M., Izzi L., Grondin P., Houde C., Kunath T., Veillette A.,
Beauchemin N.;
"The carboxyl-terminal region of biliary glycoprotein controls its
tyrosine phosphorylation and association with protein-tyrosine
phosphatases SHP-1 and SHP-2 in epithelial cells.";
J. Biol. Chem. 274:335-344(1999).
[12]
INTERACTION WITH CD300LF.
STRAIN=C57BL/6J;
PubMed=14662855; DOI=10.4049/jimmunol.171.12.6541;
Chung D.-H., Humphrey M.B., Nakamura M.C., Ginzinger D.G.,
Seaman W.E., Daws M.R.;
"CMRF-35-like molecule-1, a novel mouse myeloid receptor, can inhibit
osteoclast formation.";
J. Immunol. 171:6541-6548(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377 AND TYR-536, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[15]
INTERACTION WITH CEACAM1.
PubMed=19948503; DOI=10.1083/jcb.200904150;
Mueller M.M., Klaile E., Vorontsova O., Singer B.B., Obrink B.;
"Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L
and recruitment of SHP-2 and c-Src.";
J. Cell Biol. 187:569-581(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[17]
INTERACTION WITH MILR1.
PubMed=20526344; DOI=10.1038/ni.1886;
Hitomi K., Tahara-Hanaoka S., Someya S., Fujiki A., Tada H.,
Sugiyama T., Shibayama S., Shibuya K., Shibuya A.;
"An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin
E-mediated immediate hypersensitivity reactions.";
Nat. Immunol. 11:601-607(2010).
[18]
INTERACTION WITH MPIG6B.
PubMed=23112346; DOI=10.1126/scisignal.2002936;
Mazharian A., Wang Y.J., Mori J., Bem D., Finney B., Heising S.,
Gissen P., White J.G., Berndt M.C., Gardiner E.E., Nieswandt B.,
Douglas M.R., Campbell R.D., Watson S.P., Senis Y.A.;
"Mice lacking the ITIM-containing receptor G6b-B exhibit
macrothrombocytopenia and aberrant platelet function.";
Sci. Signal. 5:RA78-RA78(2012).
-!- FUNCTION: Modulates signaling by tyrosine phosphorylated cell
surface receptors such as KIT and the EGF receptor/EGFR. The SH2
regions may interact with other cellular components to modulate
its own phosphatase activity against interacting substrates.
Together with MTUS1, induces UBE2V2 expression upon angiotensin II
stimulation. Plays a key role in hematopoiesis.
{ECO:0000269|PubMed:9528781}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Monomer. Interacts with MTUS1 (By similarity). Interacts
with MILR1 (tyrosine-phosphorylated) (PubMed:20526344). Interacts
with KIT (PubMed:9528781). Interacts with SIRPA/PTPNS1
(PubMed:9712903). Interacts with FCRL2 and FCRL4 (By similarity).
Interacts with CD84 (By similarity). Interacts with CD300LF
(PubMed:14662855). Interacts with CDK2 (By similarity). Interacts
with KIR2DL1; the interaction is enhanced by ARRB2 (By
similarity). Interacts (via SH2 1 domain) with ROS1; the
interaction is direct and promotes ROS1 dephosphorylation (By
similarity). Interacts with EGFR; inhibits EGFR-dependent
activation of MAPK/ERK (By similarity). Interacts with LYN (By
similarity). Interacts with the tyrosine phosphorylated form of
PDPK1 (By similarity). Interacts with CEACAM1 (via cytoplasmic
domain); this interaction depends on the monomer/dimer equilibrium
and is phosphorylation-dependent (PubMed:19948503,
PubMed:9867848). Interacts with MPIG6B (via ITIM motif)
(PubMed:23112346). Interacts with KLRI1 and KLRI2 (By similarity).
{ECO:0000250|UniProtKB:P29350, ECO:0000250|UniProtKB:P81718,
ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:20526344,
ECO:0000269|PubMed:23112346, ECO:0000269|PubMed:9528781,
ECO:0000269|PubMed:9712903, ECO:0000269|PubMed:9867848}.
-!- INTERACTION:
Q91YS8:Camk1; NbExp=3; IntAct=EBI-2620699, EBI-911352;
P35329:Cd22; NbExp=5; IntAct=EBI-2620699, EBI-300059;
Q9Z1S8:Gab2; NbExp=2; IntAct=EBI-2620699, EBI-641738;
P51432:Plcb3; NbExp=4; IntAct=EBI-2620699, EBI-2606131;
Q78DX7:Ros1; NbExp=3; IntAct=EBI-2620699, EBI-7800362;
P42225:Stat1; NbExp=2; IntAct=EBI-2620699, EBI-647118;
B7UM99:tir (xeno); NbExp=2; IntAct=EBI-2620699, EBI-2504426;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=In
neurons, translocates into the nucleus after treatment with
angiotensin II. Shuttles between the cytoplasm and nucleus via its
association with PDPK1 (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P29351-1; Sequence=Displayed;
Name=2;
IsoId=P29351-2; Sequence=VSP_005131;
Name=3;
IsoId=P29351-3; Sequence=VSP_005132, VSP_005133;
-!- TISSUE SPECIFICITY: Expressed predominantly in hematopoietic
cells. {ECO:0000269|PubMed:1932742}.
-!- DOMAIN: The N-terminal SH2 domain functions as an auto-inhibitory
domain, blocking the catalytic domain in the ligand-free close
conformation. {ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residues. Phosphorylation at Tyr-
564 enhances phosphatase activity (By similarity). Binding of
KITLG/SCF to KIT increases tyrosine phosphorylation. {ECO:0000250,
ECO:0000269|PubMed:1385421, ECO:0000269|PubMed:9528781}.
-!- DISEASE: Note=Defects in Ptpn6 are the cause of the motheaten (me)
or viable motheaten (mev) phenotypes. Mice homozygous for the
recessive allelic mutations develop severe defects in
hematopoiesis.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class 2 subfamily. {ECO:0000305}.
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EMBL; M68902; AAA37796.1; -; mRNA.
EMBL; M90389; AAA40007.1; -; mRNA.
EMBL; S63763; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S63764; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S63803; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC002397; AAC36009.1; -; Genomic_DNA.
EMBL; AC002397; AAC36008.1; -; Genomic_DNA.
EMBL; U65955; AAD00152.1; -; Genomic_DNA.
EMBL; U65952; AAD00152.1; JOINED; Genomic_DNA.
EMBL; U65953; AAD00152.1; JOINED; Genomic_DNA.
EMBL; U65954; AAD00152.1; JOINED; Genomic_DNA.
EMBL; U65955; AAD00151.1; -; Genomic_DNA.
EMBL; U65951; AAD00151.1; JOINED; Genomic_DNA.
EMBL; U65952; AAD00151.1; JOINED; Genomic_DNA.
EMBL; U65953; AAD00151.1; JOINED; Genomic_DNA.
EMBL; U65954; AAD00151.1; JOINED; Genomic_DNA.
EMBL; BC012660; AAH12660.1; -; mRNA.
CCDS; CCDS39628.1; -. [P29351-1]
CCDS; CCDS51908.1; -. [P29351-2]
PIR; A44390; A44390.
RefSeq; NP_001071173.1; NM_001077705.2. [P29351-2]
RefSeq; NP_038573.2; NM_013545.3. [P29351-1]
UniGene; Mm.271799; -.
ProteinModelPortal; P29351; -.
SMR; P29351; -.
BioGrid; 200256; 10.
DIP; DIP-41455N; -.
ELM; P29351; -.
IntAct; P29351; 18.
MINT; P29351; -.
STRING; 10090.ENSMUSP00000004377; -.
CarbonylDB; P29351; -.
iPTMnet; P29351; -.
PhosphoSitePlus; P29351; -.
EPD; P29351; -.
MaxQB; P29351; -.
PaxDb; P29351; -.
PeptideAtlas; P29351; -.
PRIDE; P29351; -.
Ensembl; ENSMUST00000004377; ENSMUSP00000004377; ENSMUSG00000004266. [P29351-2]
Ensembl; ENSMUST00000112484; ENSMUSP00000108103; ENSMUSG00000004266. [P29351-1]
Ensembl; ENSMUST00000171549; ENSMUSP00000129124; ENSMUSG00000004266. [P29351-2]
Ensembl; ENSMUST00000174265; ENSMUSP00000133991; ENSMUSG00000004266. [P29351-3]
GeneID; 15170; -.
KEGG; mmu:15170; -.
UCSC; uc009drk.2; mouse. [P29351-1]
CTD; 5777; -.
MGI; MGI:96055; Ptpn6.
eggNOG; KOG0790; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00910000144001; -.
HOVERGEN; HBG000223; -.
InParanoid; P29351; -.
KO; K05697; -.
OMA; QAKGEPW; -.
PhylomeDB; P29351; -.
TreeFam; TF351632; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1433559; Regulation of KIT signaling.
Reactome; R-MMU-388841; Costimulation by the CD28 family.
Reactome; R-MMU-389948; PD-1 signaling.
Reactome; R-MMU-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-MMU-5690714; CD22 mediated BCR regulation.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-877300; Interferon gamma signaling.
Reactome; R-MMU-909733; Interferon alpha/beta signaling.
Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
Reactome; R-MMU-912694; Regulation of IFNA signaling.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
ChiTaRS; Ptpn6; mouse.
PRO; PR:P29351; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000004266; -.
CleanEx; MM_PTPN6; -.
ExpressionAtlas; P29351; baseline and differential.
Genevisible; P29351; MM.
GO; GO:0042105; C:alpha-beta T cell receptor complex; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:UniProtKB.
GO; GO:0140031; F:phosphorylation-dependent protein binding; ISO:MGI.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0033277; P:abortive mitotic cell cycle; IMP:MGI.
GO; GO:0050853; P:B cell receptor signaling pathway; IMP:MGI.
GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:MGI.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:MGI.
GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IGI:MGI.
GO; GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:MGI.
GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:MGI.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0070527; P:platelet aggregation; IMP:MGI.
GO; GO:0030220; P:platelet formation; IGI:MGI.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
GO; GO:0045577; P:regulation of B cell differentiation; IMP:MGI.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IGI:MGI.
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;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Hydrolase; Nucleus;
Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
SH2 domain.
CHAIN 1 595 Tyrosine-protein phosphatase non-receptor
type 6.
/FTId=PRO_0000094759.
DOMAIN 4 100 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 110 213 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 244 515 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 453 459 Substrate binding. {ECO:0000250}.
ACT_SITE 453 453 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044}.
BINDING 419 419 Substrate. {ECO:0000250}.
BINDING 500 500 Substrate. {ECO:0000250}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P81718}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 64 64 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29350}.
MOD_RES 377 377 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 536 536 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 564 564 Phosphotyrosine; by LYN.
{ECO:0000250|UniProtKB:P29350}.
VAR_SEQ 1 39 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_005132.
VAR_SEQ 1 3 MVR -> MLSRG (in isoform 2).
{ECO:0000305}.
/FTId=VSP_005131.
VAR_SEQ 40 44 SLSVR -> MLSRG (in isoform 3).
{ECO:0000305}.
/FTId=VSP_005133.
VARIANT 77 99 EYYTQQQGILQDRDGTIIHLKYP -> VPRPHIWRAGGVTA
AGQGRALD (in motheaten (me)).
VARIANT 100 595 Missing (in motheaten (me)).
CONFLICT 240 240 A -> R (in Ref. 1; AAA37796).
{ECO:0000305}.
CONFLICT 572 572 K -> Q (in Ref. 1; AAA37796).
{ECO:0000305}.
CONFLICT 586 586 E -> D (in Ref. 6; AAH12660).
{ECO:0000305}.
SEQUENCE 595 AA; 67559 MW; CF17300D032638D2 CRC64;
MVRWFHRDLS GPDAETLLKG RGVPGSFLAR PSRKNQGDFS LSVRVDDQVT HIRIQNSGDF
YDLYGGEKFA TLTELVEYYT QQQGILQDRD GTIIHLKYPL NCSDPTSERW YHGHISGGQA
ESLLQAKGEP WTFLVRESLS QPGDFVLSVL NDQPKAGPGS PLRVTHIKVM CEGGRYTVGG
SETFDSLTDL VEHFKKTGIE EASGAFVYLR QPYYATRVNA ADIENRVLEL NKKQESEDTA
KAGFWEEFES LQKQEVKNLH QRLEGQRPEN KSKNRYKNIL PFDHSRVILQ GRDSNIPGSD
YINANYVKNQ LLGPDENSKT YIASQGCLDA TVNDFWQMAW QENTRVIVMT TREVEKGRNK
CVPYWPEVGT QRVYGLYSVT NSREHDTAEY KLRTLQISPL DNGDLVREIW HYQYLSWPDH
GVPSEPGGVL SFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ESISTKGLDC
DIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEIIQSQK GQESEYGNIT
YPPAVRSAHA KASRTSSKHK EEVYENVHSK SKKEEKVKKQ RSADKEKNKG SLKRK


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