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Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship) (hp51CN)

 SHIP1_HUMAN             Reviewed;        1189 AA.
Q92835; O00145; Q13544; Q13545; Q6P5A4; Q92656; Q9UE80;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
25-OCT-2017, entry version 144.
RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1;
EC=3.1.3.86;
AltName: Full=Inositol polyphosphate-5-phosphatase of 145 kDa;
Short=SIP-145;
AltName: Full=SH2 domain-containing inositol 5'-phosphatase 1;
Short=SH2 domain-containing inositol phosphatase 1;
Short=SHIP-1;
AltName: Full=p150Ship;
Short=hp51CN;
Name=INPP5D; Synonyms=SHIP, SHIP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ENZYME ACTIVITY, TISSUE
SPECIFICITY, AND VARIANT TYR-1169.
PubMed=8769125; DOI=10.1006/bbrc.1996.1161;
Drayer A.L., Pesesse X., De Smedt F., Woscholski R., Parker P.,
Erneux C.;
"Cloning and expression of a human placenta inositol 1,3,4,5-
tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-
phosphatase.";
Biochem. Biophys. Res. Commun. 225:243-249(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
INTERACTION WITH SHC1.
PubMed=8874179;
Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., Krystal G.;
"Cloning and characterization of human SHIP, the 145-kD inositol 5-
phosphatase that associates with SHC after cytokine stimulation.";
Blood 88:2833-2840(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
1-1139 (ISOFORM 1), ENZYME ACTIVITY, AND INTERACTION WITH GRB2.
TISSUE=Lung;
PubMed=8723348; DOI=10.1016/S0960-9822(02)00511-0;
Kavanaugh W.M., Pot D.A., Chin S.M., Deuter-Reinhard M.,
Jefferson A.B., Norris F.A., Masiarz F.R., Cousens L.S., Majerus P.W.,
Williams L.T.;
"Multiple forms of an inositol polyphosphate 5-phosphatase form
signaling complexes with Shc and Grb2.";
Curr. Biol. 6:438-445(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=9058707;
Geier S.J., Algate P.A., Carlberg K., Flowers D., Friedman C.,
Trask B., Rohrschneider L.R.;
"The human SHIP gene is differentially expressed in cell lineages of
the bone marrow and blood.";
Blood 89:1876-1885(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
PHOSPHORYLATION, AND INTERACTION WITH GRB2.
PubMed=9108392;
Odai H., Sasaki K., Iwamatsu A., Nakamoto T., Ueno H., Yamagata T.,
Mitani K., Yazaki Y., Hirai H.;
"Purification and molecular cloning of SH2- and SH3-containing
inositol polyphosphate-5-phosphatase, which is involved in the
signaling pathway of granulocyte-macrophage colony-stimulating factor,
erythropoietin, and Bcr-Abl.";
Blood 89:2745-2756(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
TYR-1169.
TISSUE=B-cell, and Lymph;
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]
INTERACTION WITH SLAMF1.
PubMed=10229804;
Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A.,
Sidorenko S.P.;
"CDw150 associates with src-homology 2-containing inositol phosphatase
and modulates CD95-mediated apoptosis.";
J. Immunol. 162:5719-5727(1999).
[8]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH DOK1.
PubMed=10822173; DOI=10.1016/S0898-6568(00)00073-5;
Dunant N.M., Wisniewski D., Strife A., Clarkson B., Resh M.D.;
"The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates
with the dok1 phosphoprotein in bcr-Abl transformed cells.";
Cell. Signal. 12:317-326(2000).
[9]
FUNCTION.
PubMed=12421919; DOI=10.4049/jimmunol.169.10.5441;
Freeburn R.W., Wright K.L., Burgess S.J., Astoul E., Cantrell D.A.,
Ward S.G.;
"Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-
trisphosphate metabolism in T lymphocytes and can regulate novel
phosphoinositide 3-kinase effectors.";
J. Immunol. 169:5441-5450(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-915, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
FUNCTION.
PubMed=16682172; DOI=10.1016/j.cellsig.2006.03.012;
Vaillancourt M., Levasseur S., Tremblay M.-L., Marois L.,
Rollet-Labelle E., Naccache P.H.;
"The Src homology 2-containing inositol 5-phosphatase 1 (SHIP1) is
involved in CD32a signaling in human neutrophils.";
Cell. Signal. 18:2022-2032(2006).
[12]
INTERACTION WITH FCRL3.
PubMed=19843936; DOI=10.4049/jimmunol.0901982;
Kochi Y., Myouzen K., Yamada R., Suzuki A., Kurosaki T., Nakamura Y.,
Yamamoto K.;
"FCRL3, an autoimmune susceptibility gene, has inhibitory potential on
B-cell receptor-mediated signaling.";
J. Immunol. 183:5502-5510(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INTERACTION WITH FCRL6.
PubMed=20933011; DOI=10.1016/j.imlet.2010.09.023;
Kulemzin S.V., Zamoshnikova A.Y., Yurchenko M.Y., Vitak N.Y.,
Najakshin A.M., Fayngerts S.A., Chikaev N.A., Reshetnikova E.S.,
Kashirina N.M., Peclo M.M., Rutkevich P.N., Shevelev A.Y.,
Yanushevskaya E.V., Baranov K.O., Mamonkin M., Vlasik T.N.,
Sidorenko S.P., Taranin A.V., Mechetina L.V.;
"FCRL6 receptor: expression and associated proteins.";
Immunol. Lett. 134:174-182(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-960; THR-963 AND
SER-971, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
STRUCTURE BY NMR OF 1-112.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the human SHIP SH2 domain.";
Submitted (APR-2008) to the PDB data bank.
[17]
VARIANT GLU-685.
PubMed=12529653; DOI=10.1038/sj.leu.2402725;
Luo J.-M., Yoshida H., Komura S., Ohishi N., Pan L., Shigeno K.,
Hanamura I., Miura K., Iida S., Ueda R., Naoe T., Akao Y., Ohno R.,
Ohnishi K.;
"Possible dominant-negative mutation of the SHIP gene in acute myeloid
leukemia.";
Leukemia 17:1-8(2003).
-!- FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that
specifically hydrolyzes the 5-phosphate of phosphatidylinositol-
3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2,
thereby negatively regulating the PI3K (phosphoinositide 3-kinase)
pathways. Acts as a negative regulator of B-cell antigen receptor
signaling. Mediates signaling from the FC-gamma-RIIB receptor
(FCGR2B), playing a central role in terminating signal
transduction from activating immune/hematopoietic cell receptor
systems. Acts as a negative regulator of myeloid cell
proliferation/survival and chemotaxis, mast cell degranulation,
immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in
platelets and JNK signaling in B-cells. Regulates proliferation of
osteoclast precursors, macrophage programming, phagocytosis and
activation and is required for endotoxin tolerance. Involved in
the control of cell-cell junctions, CD32a signaling in neutrophils
and modulation of EGF-induced phospholipase C activity. Key
regulator of neutrophil migration, by governing the formation of
the leading edge and polarization required for chemotaxis.
Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates
the activin/TGF-beta-induced apoptosis through its Smad-dependent
expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus
affect the levels of the higher inositol polyphosphates like
InsP6. {ECO:0000269|PubMed:12421919, ECO:0000269|PubMed:16682172}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3,4,5-
triphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3,4-
diphosphate + phosphate. {ECO:0000269|PubMed:8723348,
ECO:0000269|PubMed:8769125}.
-!- ENZYME REGULATION: Activated upon translocation to the sites of
synthesis of PtdIns(3,4,5)P3 in the membrane. {ECO:0000250}.
-!- SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1
(PubMed:8874179). Interacts with tyrosine phosphorylated form of
DOK1 (PubMed:10822173). Interacts with tyrosine phosphorylated
form of DOK3 (By similarity). Interacts with tyrosine
phosphorylated form of SLAMF1/CD150 (PubMed:10229804). Interacts
with PTPN11 in response to IL-3 (By similarity). Interacts with
receptor EPOR (By similarity). Interacts with receptors
MS4A2/FCER1B and FCER1G (By similarity). Interacts with receptors
FCGR2B and FCGR3 (By similarity). Interacts with receptor FCGR2A,
leading to regulate gene expression during the phagocytic process
(By similarity). Interacts with GRB2 (PubMed:8723348,
PubMed:9108392). Interacts with PLCG1 (By similarity). Interacts
with tyrosine kinases SRC and TEC (By similarity). Interacts with
c-Met/MET (By similarity). Interacts with MILR1 (tyrosine-
phosphorylated) (By similarity). Can weakly interact (via NPXY
motif 2) with DAB2 (via PID domain); the interaction is impaired
by tyrosine phosphorylation of the NPXY motif (By similarity).
Interacts with FCRL3 and FCRL6 (tyrosine phosphorylated form)
(PubMed:20933011, PubMed:19843936). {ECO:0000250|UniProtKB:P97573,
ECO:0000250|UniProtKB:Q9ES52, ECO:0000269|PubMed:19843936,
ECO:0000269|PubMed:20933011}.
-!- INTERACTION:
Q9BZW8:CD244; NbExp=6; IntAct=EBI-1380477, EBI-1580565;
A8MQ03:CYSRT1; NbExp=4; IntAct=EBI-9092209, EBI-3867333;
P31994:FCGR2B; NbExp=3; IntAct=EBI-1380477, EBI-724784;
O75525:KHDRBS3; NbExp=3; IntAct=EBI-1380477, EBI-722504;
Q15323:KRT31; NbExp=3; IntAct=EBI-1380477, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-1380477, EBI-10171697;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-1380477, EBI-10172290;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-1380477, EBI-10172052;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-1380477, EBI-945833;
Q96B97:SH3KBP1; NbExp=6; IntAct=EBI-1380477, EBI-346595;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10822173}.
Cell membrane {ECO:0000250|UniProtKB:Q9ES52}; Peripheral membrane
protein {ECO:0000250|UniProtKB:Q9ES52}. Membrane raft
{ECO:0000250|UniProtKB:Q9ES52}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9ES52}. Membrane
{ECO:0000269|PubMed:10822173}; Peripheral membrane protein
{ECO:0000269|PubMed:10822173}. Note=Translocates to the plasma
membrane when activated, translocation is probably due to
different mechanisms depending on the stimulus and cell type.
Translocates from the cytoplasm to membrane ruffles in a
FCGR3/CD16-dependent manner. Colocalizes with FC-gamma-RIIB
receptor (FCGR2B) or FCGR3/CD16 at membrane ruffles. Tyrosine
phosphorylation may also participate in membrane localization.
{ECO:0000250|UniProtKB:Q9ES52}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q92835-1; Sequence=Displayed;
Name=2;
IsoId=Q92835-2; Sequence=VSP_027978;
Name=3; Synonyms=SIP-110;
IsoId=Q92835-3; Sequence=VSP_027977, VSP_027979;
-!- TISSUE SPECIFICITY: Specifically expressed in immune and
hematopoietic cells. Expressed in bone marrow and blood cells.
Levels vary considerably within this compartment. Present in at
least 74% of immature CD34+ cells, whereas within the more mature
population of CD33+ cells, it is present in only 10% of cells.
Present in the majority of T-cells, while it is present in a
minority of B-cells (at protein level).
{ECO:0000269|PubMed:8769125, ECO:0000269|PubMed:8874179,
ECO:0000269|PubMed:9058707, ECO:0000269|PubMed:9108392}.
-!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated
forms of proteins such as SHC1 or PTPN11/SHP-2. It competes with
that of GRB2 for binding to phosphorylated SHC1 to inhibit the Ras
pathway. It is also required for tyrosine phosphorylation (By
similarity). {ECO:0000250}.
-!- DOMAIN: The NPXY sequence motif found in many tyrosine-
phosphorylated proteins is required for the specific binding of
the PID domain. {ECO:0000250}.
-!- PTM: Tyrosine phosphorylated by the members of the SRC family
after exposure to a diverse array of extracellular stimuli such as
cytokines, growth factors, antibodies, chemokines, integrin
ligands and hypertonic and oxidative stress. Phosphorylated upon
IgG receptor FCGR2B-binding. {ECO:0000269|PubMed:10822173,
ECO:0000269|PubMed:9108392}.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC50454.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X98429; CAA67071.1; -; mRNA.
EMBL; U57650; AAB53573.1; -; mRNA.
EMBL; U50040; AAC50453.1; -; mRNA.
EMBL; U50041; AAC50454.1; ALT_INIT; mRNA.
EMBL; U84400; AAB49680.1; -; mRNA.
EMBL; U53470; AAD00081.1; -; mRNA.
EMBL; BC062985; AAH62985.1; -; mRNA.
EMBL; BC099920; AAH99920.1; -; mRNA.
EMBL; BC113580; AAI13581.1; -; mRNA.
EMBL; BC113582; AAI13583.1; -; mRNA.
CCDS; CCDS74672.1; -. [Q92835-1]
CCDS; CCDS77543.1; -. [Q92835-2]
PIR; JC4889; JC4889.
RefSeq; NP_001017915.1; NM_001017915.2. [Q92835-1]
RefSeq; NP_005532.2; NM_005541.4. [Q92835-2]
UniGene; Hs.262886; -.
UniGene; Hs.601911; -.
PDB; 2YSX; NMR; -; A=1-112.
PDBsum; 2YSX; -.
ProteinModelPortal; Q92835; -.
SMR; Q92835; -.
BioGrid; 109847; 40.
ELM; Q92835; -.
IntAct; Q92835; 27.
MINT; MINT-123561; -.
STRING; 9606.ENSP00000352575; -.
ChEMBL; CHEMBL1781870; -.
SwissLipids; SLP:000000951; -.
DEPOD; Q92835; -.
iPTMnet; Q92835; -.
PhosphoSitePlus; Q92835; -.
BioMuta; INPP5D; -.
DMDM; 158564077; -.
EPD; Q92835; -.
MaxQB; Q92835; -.
PaxDb; Q92835; -.
PeptideAtlas; Q92835; -.
PRIDE; Q92835; -.
Ensembl; ENST00000359570; ENSP00000352575; ENSG00000168918. [Q92835-2]
Ensembl; ENST00000445964; ENSP00000405338; ENSG00000168918. [Q92835-1]
Ensembl; ENST00000629761; ENSP00000486669; ENSG00000281614. [Q92835-2]
Ensembl; ENST00000630854; ENSP00000487191; ENSG00000281614. [Q92835-1]
GeneID; 3635; -.
KEGG; hsa:3635; -.
UCSC; uc032ovq.2; human. [Q92835-1]
CTD; 3635; -.
DisGeNET; 3635; -.
EuPathDB; HostDB:ENSG00000168918.13; -.
GeneCards; INPP5D; -.
H-InvDB; HIX0057065; -.
HGNC; HGNC:6079; INPP5D.
HPA; CAB016300; -.
HPA; HPA070455; -.
MIM; 601582; gene.
neXtProt; NX_Q92835; -.
OpenTargets; ENSG00000168918; -.
PharmGKB; PA29887; -.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00760000119075; -.
HOVERGEN; HBG106726; -.
InParanoid; Q92835; -.
KO; K03084; -.
OMA; LTKPEMF; -.
OrthoDB; EOG091G00P6; -.
PhylomeDB; Q92835; -.
TreeFam; TF323475; -.
BioCyc; MetaCyc:HS09849-MONOMER; -.
BRENDA; 3.1.3.86; 2681.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; Q92835; -.
SIGNOR; Q92835; -.
ChiTaRS; INPP5D; human.
EvolutionaryTrace; Q92835; -.
GeneWiki; INPP5D; -.
GenomeRNAi; 3635; -.
PRO; PR:Q92835; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000168918; -.
CleanEx; HS_INPP5D; -.
ExpressionAtlas; Q92835; baseline and differential.
Genevisible; Q92835; HS.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; TAS:ProtInc.
GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; TAS:Reactome.
GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0051425; F:PTB domain binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
GO; GO:0050777; P:negative regulation of immune response; IEA:Ensembl.
GO; GO:0045409; P:negative regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
GO; GO:0045656; P:negative regulation of monocyte differentiation; IEA:Ensembl.
GO; GO:0045659; P:negative regulation of neutrophil differentiation; IEA:Ensembl.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0009968; P:negative regulation of signal transduction; IEA:Ensembl.
GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
Gene3D; 3.30.505.10; -; 1.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR000300; IPPc.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF03372; Exo_endo_phos; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00128; IPPc; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56219; SSF56219; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell membrane;
Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Immunity;
Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
SH2 domain; SH3-binding.
CHAIN 1 1189 Phosphatidylinositol 3,4,5-trisphosphate
5-phosphatase 1.
/FTId=PRO_0000302866.
DOMAIN 5 101 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 1016 1030 Interaction with DAB2. {ECO:0000250}.
MOTIF 124 129 SH3-binding 1.
MOTIF 912 915 NPXY motif 1.
MOTIF 969 974 SH3-binding 2.
MOTIF 1019 1022 NPXY motif 2.
MOTIF 1040 1051 SH3-binding 3.
COMPBIAS 920 1148 Pro-rich.
MOD_RES 243 243 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES52}.
MOD_RES 915 915 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES52}.
MOD_RES 944 944 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9ES52}.
MOD_RES 960 960 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 963 963 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 971 971 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1022 1022 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9ES52}.
VAR_SEQ 1 212 Missing (in isoform 3).
{ECO:0000303|PubMed:8723348}.
/FTId=VSP_027977.
VAR_SEQ 117 117 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8769125,
ECO:0000303|PubMed:8874179}.
/FTId=VSP_027978.
VAR_SEQ 213 222 TTLLCKELYG -> MFTLSPAPR (in isoform 3).
{ECO:0000303|PubMed:8723348}.
/FTId=VSP_027979.
VARIANT 685 685 V -> E (in one patient with acute myeloid
leukemya; somatic mutation).
{ECO:0000269|PubMed:12529653}.
/FTId=VAR_034979.
VARIANT 1169 1169 H -> Y (in dbSNP:rs9247).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8769125}.
/FTId=VAR_059358.
CONFLICT 25 26 DG -> GT (in Ref. 4; AAB49680).
{ECO:0000305}.
CONFLICT 1029 1029 P -> H (in Ref. 4; AAB49680).
{ECO:0000305}.
STRAND 4 9 {ECO:0000244|PDB:2YSX}.
HELIX 12 22 {ECO:0000244|PDB:2YSX}.
STRAND 27 32 {ECO:0000244|PDB:2YSX}.
STRAND 39 45 {ECO:0000244|PDB:2YSX}.
STRAND 50 57 {ECO:0000244|PDB:2YSX}.
STRAND 63 65 {ECO:0000244|PDB:2YSX}.
STRAND 70 72 {ECO:0000244|PDB:2YSX}.
STRAND 76 78 {ECO:0000244|PDB:2YSX}.
HELIX 79 85 {ECO:0000244|PDB:2YSX}.
STRAND 88 95 {ECO:0000244|PDB:2YSX}.
SEQUENCE 1189 AA; 133292 MW; 7958E91A64A4B68B CRC64;
MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV YTYRILPNED
DKFTVQASEG VSMRFFTKLD QLIEFYKKEN MGLVTHLQYP VPLEEEDTGD DPEEDTVESV
VSPPELPPRN IPLTASSCEA KEVPFSNENP RATETSRPSL SETLFQRLQS MDTSGLPEEH
LKAIQDYLST QLAQDSEFVK TGSSSLPHLK KLTTLLCKEL YGEVIRTLPS LESLQRLFDQ
QLSPGLRPRP QVPGEANPIN MVSKLSQLTS LLSSIEDKVK ALLHEGPESP HRPSLIPPVT
FEVKAESLGI PQKMQLKVDV ESGKLIIKKS KDGSEDKFYS HKKILQLIKS QKFLNKLVIL
VETEKEKILR KEYVFADSKK REGFCQLLQQ MKNKHSEQPE PDMITIFIGT WNMGNAPPPK
KITSWFLSKG QGKTRDDSAD YIPHDIYVIG TQEDPLSEKE WLEILKHSLQ EITSVTFKTV
AIHTLWNIRI VVLAKPEHEN RISHICTDNV KTGIANTLGN KGAVGVSFMF NGTSLGFVNS
HLTSGSEKKL RRNQNYMNIL RFLALGDKKL SPFNITHRFT HLFWFGDLNY RVDLPTWEAE
TIIQKIKQQQ YADLLSHDQL LTERREQKVF LHFEEEEITF APTYRFERLT RDKYAYTKQK
ATGMKYNLPS WCDRVLWKSY PLVHVVCQSY GSTSDIMTSD HSPVFATFEA GVTSQFVSKN
GPGTVDSQGQ IEFLRCYATL KTKSQTKFYL EFHSSCLESF VKSQEGENEE GSEGELVVKF
GETLPKLKPI ISDPEYLLDQ HILISIKSSD SDESYGEGCI ALRLEATETQ LPIYTPLTHH
GELTGHFQGE IKLQTSQGKT REKLYDFVKT ERDESSGPKT LKSLTSHDPM KQWEVTSRAP
PCSGSSITEI INPNYMGVGP FGPPMPLHVK QTLSPDQQPT AWSYDQPPKD SPLGPCRGES
PPTPPGQPPI SPKKFLPSTA NRGLPPRTQE SRPSDLGKNA GDTLPQEDLP LTKPEMFENP
LYGSLSSFPK PAPRKDQESP KMPRKEPPPC PEPGILSPSI VLTKAQEADR GEGPGKQVPA
PRLRSFTCSS SAEGRAAGGD KSQGKPKTPV SSQAPVPAKR PIKPSRSEIN QQTPPTPTPR
PPLPVKSPAV LHLQHSKGRD YRDNTELPHH GKHRPEEGPP GPLGRTAMQ


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