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Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)

 SHIP2_HUMAN             Reviewed;        1258 AA.
O15357; B2RTX5; Q13577; Q13578;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 2.
28-MAR-2018, entry version 143.
RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2;
EC=3.1.3.86;
AltName: Full=Inositol polyphosphate phosphatase-like protein 1;
Short=INPPL-1;
AltName: Full=Protein 51C;
AltName: Full=SH2 domain-containing inositol 5'-phosphatase 2;
Short=SH2 domain-containing inositol phosphatase 2;
Short=SHIP-2;
Name=INPPL1; Synonyms=SHIP2;
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), AND TISSUE SPECIFICITY.
PubMed=8530088; DOI=10.1006/geno.1995.1247;
Hejna J.A., Saito H., Merkens L.S., Tittle T.V., Jakobs P.M.,
Whitney M.A., Grompe M., Friedberg A.S., Moses R.E.;
"Cloning and characterization of a human cDNA (INPPL1) sharing
homology with inositol polyphosphate phosphatases.";
Genomics 29:285-287(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT GLY-1114.
TISSUE=Hippocampus;
PubMed=9367831; DOI=10.1006/bbrc.1997.7538;
Pesesse X., Deleu S., De Smedt F., Drayer L., Erneux C.;
"Identification of a second SH2-domain-containing protein closely
related to the phosphatidylinositol polyphosphate 5-phosphatase
SHIP.";
Biochem. Biophys. Res. Commun. 239:697-700(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-1114.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLY-1114.
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).
[6]
FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION, AND
INTERACTION WITH SHC1.
PubMed=9660833; DOI=10.1074/jbc.273.29.18605;
Habib T., Hejna J.A., Moses R.E., Decker S.J.;
"Growth factors and insulin stimulate tyrosine phosphorylation of the
51C/SHIP2 protein.";
J. Biol. Chem. 273:18605-18609(1998).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, ENZYME ACTIVITY, PHOSPHORYLATION,
AND INTERACTION WITH SHC1 AND ABL1.
PubMed=10194451;
Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H.,
Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B.;
"A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-
phosphatase (SHIP2) is constitutively tyrosine phosphorylated and
associated with src homologous and collagen gene (SHC) in chronic
myelogenous leukemia progenitor cells.";
Blood 93:2707-2720(1999).
[8]
INTERACTION WITH FCGR2B.
PubMed=11016922; DOI=10.1074/jbc.M003518200;
Bruhns P., Vely F., Malbec O., Fridman W.H., Vivier E., Daeeron M.;
"Molecular basis of the recruitment of the SH2 domain-containing
inositol 5-phosphatases SHIP1 and SHIP2 by fcgamma RIIB.";
J. Biol. Chem. 275:37357-37364(2000).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGFR AND SHC1, AND
PHOSPHORYLATION AT TYR-986.
PubMed=11349134; DOI=10.1074/jbc.M103537200;
Pesesse X., Dewaste V., De Smedt F., Laffargue M., Giuriato S.,
Moreau C., Payrastre B., Erneux C.;
"The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is
recruited to the epidermal growth factor (EGF) receptor and
dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-
stimulated COS-7 cells.";
J. Biol. Chem. 276:28348-28355(2001).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FLNA AND FLNB.
PubMed=11739414; DOI=10.1083/jcb.200104005;
Dyson J.M., O'Malley C.J., Becanovic J., Munday A.D., Berndt M.C.,
Coghill I.D., Nandurkar H.H., Ooms L.M., Mitchell C.A.;
"The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2,
binds filamin and regulates submembraneous actin.";
J. Cell Biol. 155:1065-1079(2001).
[11]
PHOSPHORYLATION, INTERACTION WITH BCAR1, AND MUTAGENESIS OF ARG-47.
PubMed=11158326; DOI=10.1128/MCB.21.4.1416-1428.2001;
Prasad N., Topping R.S., Decker S.J.;
"SH2-containing inositol 5'-phosphatase SHIP2 associates with the
p130(Cas) adapter protein and regulates cellular adhesion and
spreading.";
Mol. Cell. Biol. 21:1416-1428(2001).
[12]
PHOSPHORYLATION AT TYR-1162.
PubMed=11687594; DOI=10.1074/jbc.M109992200;
Steen H., Kuster B., Fernandez M., Pandey A., Mann M.;
"Tyrosine phosphorylation mapping of the epidermal growth factor
receptor signaling pathway.";
J. Biol. Chem. 277:1031-1039(2002).
[13]
FUNCTION, PHOSPHORYLATION AT TYR-986, AND MUTAGENESIS OF
986-TYR-TYR-987.
PubMed=12235291; DOI=10.1242/jcs.00070;
Prasad N., Topping R.S., Decker S.J.;
"Src family tyrosine kinases regulate adhesion-dependent tyrosine
phosphorylation of 5'-inositol phosphatase SHIP2 during cell
attachment and spreading on collagen I.";
J. Cell Sci. 115:3807-3815(2002).
[14]
INTERACTION WITH CBL AND SORBS1.
PubMed=12504111; DOI=10.1016/S0006-291X(02)02894-2;
Vandenbroere I., Paternotte N., Dumont J.E., Erneux C., Pirson I.;
"The c-Cbl-associated protein and c-Cbl are two new partners of the
SH2-containing inositol polyphosphate 5-phosphatase SHIP2.";
Biochem. Biophys. Res. Commun. 300:494-500(2003).
[15]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION
WITH ACTIN; FILAMIN AND GPIB.
PubMed=12676785; DOI=10.1182/blood-2002-09-2897;
Dyson J.M., Munday A.D., Kong A.M., Huysmans R.D., Matzaris M.,
Layton M.J., Nandurkar H.H., Berndt M.C., Mitchell C.A.;
"SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V:
localization of SHIP-2 to the activated platelet actin cytoskeleton.";
Blood 102:940-948(2003).
[16]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, PHOSPHORYLATION, INTERACTION
WITH FCGR2A, AND MUTAGENESIS OF ARG-47 AND ASP-607.
PubMed=12690104; DOI=10.1074/jbc.M302907200;
Pengal R.A., Ganesan L.P., Fang H., Marsh C.B., Anderson C.L.,
Tridandapani S.;
"SHIP-2 inositol phosphatase is inducibly expressed in human monocytes
and serves to regulate Fcgamma receptor-mediated signaling.";
J. Biol. Chem. 278:22657-22663(2003).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1135, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
ENZYME REGULATION.
PubMed=16824732; DOI=10.1016/j.cellsig.2006.05.010;
Vandeput F., Backers K., Villeret V., Pesesse X., Erneux C.;
"The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-
trisphosphate 5-phosphatase activity.";
Cell. Signal. 18:2193-2199(2006).
[20]
INTERACTION WITH SORBS3.
PubMed=16302969; DOI=10.1111/j.1742-4658.2005.04996.x;
Paternotte N., Zhang J., Vandenbroere I., Backers K., Blero D.,
Kioka N., Vanderwinden J.-M., Pirson I., Erneux C.;
"SHIP2 interaction with the cytoskeletal protein Vinexin.";
FEBS J. 272:6052-6066(2005).
[21]
FUNCTION.
PubMed=15668240; DOI=10.1074/jbc.M410289200;
Prasad N.K., Decker S.J.;
"SH2-containing 5'-inositol phosphatase, SHIP2, regulates cytoskeleton
organization and ligand-dependent down-regulation of the epidermal
growth factor receptor.";
J. Biol. Chem. 280:13129-13136(2005).
[22]
INTERACTION WITH MET.
PubMed=15735664; DOI=10.1038/sj.onc.1208558;
Koch A., Mancini A., El Bounkari O., Tamura T.;
"The SH2-domain-containing inositol 5-phosphatase (SHIP)-2 binds to c-
Met directly via tyrosine residue 1356 and involves hepatocyte growth
factor (HGF)-induced lamellipodium formation, cell scattering and cell
spreading.";
Oncogene 24:3436-3447(2005).
[23]
INTERACTION WITH CENTD3.
PubMed=17314030; DOI=10.1016/j.cellsig.2006.12.015;
Raaijmakers J.H., Deneubourg L., Rehmann H., de Koning J., Zhang Z.,
Krugmann S., Erneux C., Bos J.L.;
"The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase
SHIP2 in a SAM domain-dependent manner.";
Cell. Signal. 19:1249-1257(2007).
[24]
FUNCTION, AND INTERACTION WITH EPHA2.
PubMed=17135240; DOI=10.1074/jbc.M608509200;
Zhuang G., Hunter S., Hwang Y., Chen J.;
"Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase
via phosphatidylinositol 3-Kinase-dependent Rac1 activation.";
J. Biol. Chem. 282:2683-2694(2007).
[25]
PHOSPHORYLATION AT THR-958, AND MUTAGENESIS OF THR-958.
PubMed=17219406; DOI=10.1002/jcp.20965;
Artemenko Y., Gagnon A., Ibrahim S., Sorisky A.;
"Regulation of PDGF-stimulated SHIP2 tyrosine phosphorylation and
association with Shc in 3T3-L1 preadipocytes.";
J. Cell. Physiol. 211:598-607(2007).
[26]
INVOLVEMENT IN NIDDM.
PubMed=12086927; DOI=10.2337/diabetes.51.7.2012;
Marion E., Kaisaki P.J., Pouillon V., Gueydan C., Levy J.C.,
Bodson A., Krzentowski G., Daubresse J.-C., Mockel J., Behrends J.,
Servais G., Szpirer C., Kruys V., Gauguier D., Schurmans S.;
"The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate
for type 2 diabetes in rat and man.";
Diabetes 51:2012-2017(2002).
[27]
INVOLVEMENT IN METABOLIC SYNDROME.
PubMed=15220217; DOI=10.2337/diabetes.53.7.1900;
Kaisaki P.J., Delepine M., Woon P.Y., Sebag-Montefiore L.,
Wilder S.P., Menzel S., Vionnet N., Marion E., Riveline J.-P.,
Charpentier G., Schurmans S., Levy J.C., Lathrop M., Farrall M.,
Gauguier D.;
"Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase
(INPPL1, SHIP2) are associated with physiological abnormalities of the
metabolic syndrome.";
Diabetes 53:1900-1904(2004).
[28]
INVOLVEMENT IN NIDDM, AND VARIANTS ILE-632; MET-721; SER-982 AND
GLY-1083.
PubMed=15687335; DOI=10.1210/jc.2004-1724;
Kagawa S., Sasaoka T., Yaguchi S., Ishihara H., Tsuneki H.,
Murakami S., Fukui K., Wada T., Kobayashi S., Kimura I., Kobayashi M.;
"Impact of SRC homology 2-containing inositol 5'-phosphatase 2 gene
polymorphisms detected in a Japanese population on insulin
signaling.";
J. Clin. Endocrinol. Metab. 90:2911-2919(2005).
[29]
INVOLVEMENT IN METABOLIC SYNDROME.
PubMed=17557929; DOI=10.1136/jmg.2007.049718;
Braga Marcano A.C., Burke B., Gungadoo J., Wallace C., Kaisaki P.J.,
Woon P.Y., Farrall M., Clayton D., Brown M., Dominiczak A.,
Connell J.M., Webster J., Lathrop M., Caulfield M., Samani N.,
Gauguier D., Munroe P.B.;
"Genetic association analysis of inositol polyphosphate phosphatase-
like 1 (INPPL1, SHIP2) variants with essential hypertension.";
J. Med. Genet. 44:603-605(2007).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165 AND SER-241, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[33]
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).
[34]
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).
[35]
FUNCTION, INTERACTION WITH SH3YL1, AND MUTAGENESIS OF 140-PRO-LEU-141.
PubMed=21624956; DOI=10.1083/jcb.201012161;
Hasegawa J., Tokuda E., Tenno T., Tsujita K., Sawai H., Hiroaki H.,
Takenawa T., Itoh T.;
"SH3YL1 regulates dorsal ruffle formation by a novel phosphoinositide-
binding domain.";
J. Cell Biol. 193:901-916(2011).
[36]
FUNCTION, AND VARIANTS OPSMD TRP-401; SER-659; CYS-688 AND ILE-722.
PubMed=23273569; DOI=10.1016/j.ajhg.2012.11.015;
Huber C., Faqeih E.A., Bartholdi D., Bole-Feysot C., Borochowitz Z.,
Cavalcanti D.P., Frigo A., Nitschke P., Roume J., Santos H.G.,
Shalev S.A., Superti-Furga A., Delezoide A.L., Le Merrer M.,
Munnich A., Cormier-Daire V.;
"Exome sequencing identifies INPPL1 mutations as a cause of
opsismodysplasia.";
Am. J. Hum. Genet. 92:144-149(2013).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-352; TYR-886;
SER-890; THR-958; SER-1131; TYR-1135; TYR-1162 AND SER-1257, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- 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. Plays a central role in regulation of PI3K-dependent
insulin signaling, although the precise molecular mechanisms and
signaling pathways remain unclear. While overexpression reduces
both insulin-stimulated MAP kinase and Akt activation, its absence
does not affect insulin signaling or GLUT4 trafficking. Confers
resistance to dietary obesity. May act by regulating AKT2, but not
AKT1, phosphorylation at the plasma membrane. Part of a signaling
pathway that regulates actin cytoskeleton remodeling. Required for
the maintenance and dynamic remodeling of actin structures as well
as in endocytosis, having a major impact on ligand-induced EGFR
internalization and degradation. Participates in regulation of
cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3
thereby regulating membrane ruffling (PubMed:21624956). Regulates
cell adhesion and cell spreading. Required for HGF-mediated
lamellipodium formation, cell scattering and spreading. Acts as a
negative regulator of EPHA2 receptor endocytosis by inhibiting via
PI3K-dependent Rac1 activation. Acts as a regulator of
neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required
to form an initial protrusive pattern, and later, maintain proper
neurite outgrowth. Acts as a negative regulator of the FC-gamma-
RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB
receptor (FCGR2B), playing a central role in terminating signal
transduction from activating immune/hematopoietic cell receptor
systems. Involved in EGF signaling pathway. Upon stimulation by
EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3.
Plays a negative role in regulating the PI3K-PKB pathway, possibly
by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated
phagocytosis in macrophages independently of INPP5D/SHIP1. In
macrophages, down-regulates NF-kappa-B-dependent gene
transcription by regulating macrophage colony-stimulating factor
(M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4,
and could thus affect the levels of the higher inositol
polyphosphates like InsP6. Involved in endochondral ossification.
{ECO:0000269|PubMed:11349134, ECO:0000269|PubMed:11739414,
ECO:0000269|PubMed:12235291, ECO:0000269|PubMed:12676785,
ECO:0000269|PubMed:12690104, ECO:0000269|PubMed:15668240,
ECO:0000269|PubMed:17135240, ECO:0000269|PubMed:21624956,
ECO:0000269|PubMed:23273569, ECO:0000269|PubMed:9660833}.
-!- 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:10194451,
ECO:0000269|PubMed:21624956, ECO:0000269|PubMed:9660833}.
-!- ENZYME REGULATION: Activated upon translocation to the sites of
synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity
is enhanced in the presence of phosphatidylserine.
{ECO:0000269|PubMed:16824732}.
-!- SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1
(PubMed:9660833, PubMed:10194451, PubMed:11349134). Interacts with
EGFR (PubMed:11349134). Upon stimulation by the EGF signaling
pathway, it forms a complex with SHC1 and EGFR (PubMed:11349134).
Interacts with cytoskeletal protein SORBS3/vinexin, promoting its
localization to the periphery of cells (PubMed:16302969). Forms a
complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or GP1BB)
that regulates cortical and submembraneous actin (PubMed:11739414,
PubMed:12676785). Interacts with c-Met/MET, when c-Met/MET is
phosphorylated on 'Tyr-1356' (PubMed:15735664). Interacts with
p130Cas/BCAR1 (PubMed:11158326). Interacts with CENTD3/ARAP3 via
its SAM domain (PubMed:17314030). Interacts with c-Cbl/CBL and
CAP/SORBS1 (PubMed:12504111). Interacts with activated EPHA2
receptor (PubMed:17135240). Interacts with receptor FCGR2A
(PubMed:12690104). Interacts with receptor FCGR2B
(PubMed:11016922). Interacts with tyrosine kinase ABL1
(PubMed:10194451). Interacts with tyrosine kinase TEC (By
similarity). Interacts with CSF1R (By similarity). Interacts (via
N-terminus) with SH3YL1 (via SH3 domain) (PubMed:21624956).
Interacts with FCRL6 (tyrosine phosphorylated form)
(PubMed:20933011). {ECO:0000250|UniProtKB:Q6P549,
ECO:0000269|PubMed:10194451, ECO:0000269|PubMed:11016922,
ECO:0000269|PubMed:11158326, ECO:0000269|PubMed:11349134,
ECO:0000269|PubMed:11739414, ECO:0000269|PubMed:12504111,
ECO:0000269|PubMed:12676785, ECO:0000269|PubMed:12690104,
ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:16302969,
ECO:0000269|PubMed:17135240, ECO:0000269|PubMed:17314030,
ECO:0000269|PubMed:20933011, ECO:0000269|PubMed:9660833}.
-!- INTERACTION:
P10275:AR; NbExp=3; IntAct=EBI-1384248, EBI-608057;
P56945:BCAR1; NbExp=2; IntAct=EBI-1384248, EBI-702093;
P29317:EPHA2; NbExp=3; IntAct=EBI-15963021, EBI-702104;
Q13480:GAB1; NbExp=2; IntAct=EBI-1384248, EBI-517684;
Q9QYY0:Gab1 (xeno); NbExp=5; IntAct=EBI-1384248, EBI-644784;
A0A061I5T4:H671_4g13114 (xeno); NbExp=2; IntAct=EBI-1384248, EBI-2504267;
Q8IV36:HID1; NbExp=2; IntAct=EBI-1384248, EBI-743438;
Q15811-2:ITSN1; NbExp=9; IntAct=EBI-1384248, EBI-8052395;
P08581:MET; NbExp=2; IntAct=EBI-1384248, EBI-1039152;
Q9BX66:SORBS1; NbExp=5; IntAct=EBI-1384248, EBI-433642;
O60504-1:SORBS3; NbExp=2; IntAct=EBI-1384248, EBI-1222953;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton.
Membrane; Peripheral membrane protein. Cell projection,
filopodium. Cell projection, lamellipodium. Note=Translocates to
membrane ruffles when activated, translocation is probably due to
different mechanisms depending on the stimulus and cell type.
Partly translocated via its SH2 domain which mediates interaction
with tyrosine phosphorylated receptors such as the FC-gamma-RIIB
receptor (FCGR2B). Tyrosine phosphorylation may also participate
in membrane localization. Insulin specifically stimulates its
redistribution from the cytosol to the plasma membrane. Recruited
to the membrane following M-CSF stimulation. In activated
spreading platelets, localizes with actin at filopodia,
lamellipodia and the central actin ring.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O15357-1; Sequence=Displayed;
Name=2;
IsoId=O15357-2; Sequence=VSP_027985;
-!- TISSUE SPECIFICITY: Widely expressed, most prominently in skeletal
muscle, heart and brain. Present in platelets. Expressed in
transformed myeloid cells and in primary macrophages, but not in
peripheral blood monocytes. {ECO:0000269|PubMed:12676785,
ECO:0000269|PubMed:12690104, ECO:0000269|PubMed:8530088,
ECO:0000269|PubMed:9367831, ECO:0000269|PubMed:9660833}.
-!- INDUCTION: By bacterial lipopolysaccharides (LPS).
{ECO:0000269|PubMed:12690104}.
-!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated
forms of proteins such as SHC1 or FCGR2A. It also mediates the
interaction with p130Cas/BCAR1.
-!- 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
insulin, growth factors such as EGF or PDGF, chemokines, integrin
ligands and hypertonic and oxidative stress. May be phosphorylated
upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-986
following cell attachment and spreading. Phosphorylated at Tyr-
1162 following EGF signaling pathway stimulation. Phosphorylated
at Thr-958 in response to PDGF. {ECO:0000269|PubMed:10194451,
ECO:0000269|PubMed:11158326, ECO:0000269|PubMed:11349134,
ECO:0000269|PubMed:11687594, ECO:0000269|PubMed:12235291,
ECO:0000269|PubMed:12690104, ECO:0000269|PubMed:17219406,
ECO:0000269|PubMed:9660833}.
-!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM)
[MIM:125853]: A multifactorial disorder of glucose homeostasis
caused by a lack of sensitivity to the body's own insulin.
Affected individuals usually have an obese body habitus and
manifestations of a metabolic syndrome characterized by diabetes,
insulin resistance, hypertension and hypertriglyceridemia. The
disease results in long-term complications that affect the eyes,
kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:12086927,
ECO:0000269|PubMed:15687335}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Note=Genetic variations in INPPL1 may be a cause of
susceptibility to metabolic syndrome. Metabolic syndrome is
characterized by diabetes, insulin resistance, hypertension, and
hypertriglyceridemia is absent. {ECO:0000269|PubMed:15220217,
ECO:0000269|PubMed:17557929}.
-!- DISEASE: Opsismodysplasia (OPSMD) [MIM:258480]: A rare skeletal
dysplasia involving delayed bone maturation. Clinical signs
observed at birth include short limbs, small hands and feet,
relative macrocephaly with a large anterior fontanel, and
characteristic craniofacial abnormalities including a prominent
brow, depressed nasal bridge, a small anteverted nose, and a
relatively long philtrum. Death secondary to respiratory failure
during the first few years of life has been reported, but there
can be long-term survival. Typical radiographic findings include
shortened long bones with very delayed epiphyseal ossification,
severe platyspondyly, metaphyseal cupping, and characteristic
abnormalities of the metacarpals and phalanges.
{ECO:0000269|PubMed:23273569}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Its ability to confer resistance to dietary obesity
suggests that it may serve as a possible therapeutic target in
cases of type 2 diabetes and obesity.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA50503.1; Type=Frameshift; Positions=1153; Evidence={ECO:0000305};
Sequence=AAA96658.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/INPPL1ID40984ch11q13.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; L24444; AAA50503.1; ALT_FRAME; mRNA.
EMBL; L36818; AAA96658.1; ALT_FRAME; mRNA.
EMBL; Y14385; CAA74743.1; -; mRNA.
EMBL; AP000593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74855.1; -; Genomic_DNA.
EMBL; BC140853; AAI40854.1; -; mRNA.
CCDS; CCDS8213.1; -. [O15357-1]
PIR; JC5765; JC5765.
RefSeq; NP_001558.3; NM_001567.3. [O15357-1]
RefSeq; XP_011543301.1; XM_011544999.2. [O15357-1]
UniGene; Hs.523875; -.
PDB; 2K4P; NMR; -; A=1194-1258.
PDB; 2KSO; NMR; -; B=1200-1258.
PDB; 2MK2; NMR; -; A=20-117.
PDB; 3NR8; X-ray; 2.80 A; A/B=419-732.
PDB; 4A9C; X-ray; 2.10 A; A/B=419-732.
PDB; 5OKM; X-ray; 1.96 A; A/B/C/D/E/F/G/H=420-878.
PDB; 5OKN; X-ray; 2.65 A; A/B/C/D/E/F/G/H=420-878.
PDB; 5OKO; X-ray; 1.94 A; A/B=420-878.
PDB; 5OKP; X-ray; 1.85 A; A=420-878.
PDBsum; 2K4P; -.
PDBsum; 2KSO; -.
PDBsum; 2MK2; -.
PDBsum; 3NR8; -.
PDBsum; 4A9C; -.
PDBsum; 5OKM; -.
PDBsum; 5OKN; -.
PDBsum; 5OKO; -.
PDBsum; 5OKP; -.
ProteinModelPortal; O15357; -.
SMR; O15357; -.
BioGrid; 109848; 118.
DIP; DIP-39733N; -.
IntAct; O15357; 29.
MINT; O15357; -.
STRING; 9606.ENSP00000298229; -.
BindingDB; O15357; -.
ChEMBL; CHEMBL2331064; -.
GuidetoPHARMACOLOGY; 1459; -.
SwissLipids; SLP:000000953; -.
DEPOD; O15357; -.
iPTMnet; O15357; -.
PhosphoSitePlus; O15357; -.
BioMuta; INPPL1; -.
EPD; O15357; -.
MaxQB; O15357; -.
PaxDb; O15357; -.
PeptideAtlas; O15357; -.
PRIDE; O15357; -.
Ensembl; ENST00000298229; ENSP00000298229; ENSG00000165458. [O15357-1]
Ensembl; ENST00000538751; ENSP00000444619; ENSG00000165458. [O15357-2]
GeneID; 3636; -.
KEGG; hsa:3636; -.
UCSC; uc001osf.4; human. [O15357-1]
CTD; 3636; -.
DisGeNET; 3636; -.
EuPathDB; HostDB:ENSG00000165458.13; -.
GeneCards; INPPL1; -.
H-InvDB; HIX0201720; -.
HGNC; HGNC:6080; INPPL1.
HPA; HPA037601; -.
MalaCards; INPPL1; -.
MIM; 125853; phenotype.
MIM; 258480; phenotype.
MIM; 600829; gene.
neXtProt; NX_O15357; -.
OpenTargets; ENSG00000165458; -.
Orphanet; 2746; Opsismodysplasia.
PharmGKB; PA29888; -.
eggNOG; KOG0565; Eukaryota.
eggNOG; KOG4384; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00760000119075; -.
HOGENOM; HOG000004836; -.
HOVERGEN; HBG106726; -.
InParanoid; O15357; -.
KO; K15909; -.
OMA; VKSMDGY; -.
OrthoDB; EOG091G00P6; -.
PhylomeDB; O15357; -.
TreeFam; TF323475; -.
BioCyc; MetaCyc:HS09233-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-912526; Interleukin receptor SHC signaling.
SABIO-RK; O15357; -.
SignaLink; O15357; -.
SIGNOR; O15357; -.
ChiTaRS; INPPL1; human.
EvolutionaryTrace; O15357; -.
GeneWiki; INPPL1; -.
GenomeRNAi; 3636; -.
PRO; PR:O15357; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000165458; -.
CleanEx; HS_INPPL1; -.
ExpressionAtlas; O15357; baseline and differential.
Genevisible; O15357; HS.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0001958; P:endochondral ossification; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
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; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF03372; Exo_endo_phos; 1.
Pfam; PF00536; SAM_1; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00128; IPPc; 1.
SMART; SM00454; SAM; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56219; SSF56219; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Cell adhesion;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
Diabetes mellitus; Disease mutation; Hydrolase; Immunity; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; SH2 domain;
SH3-binding.
CHAIN 1 1258 Phosphatidylinositol 3,4,5-trisphosphate
5-phosphatase 2.
/FTId=PRO_0000302870.
DOMAIN 21 117 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 1196 1258 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
MOTIF 944 949 SH3-binding.
MOTIF 983 986 NPXY motif.
COMPBIAS 935 1105 Pro-rich.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 165 165 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 886 886 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 958 958 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17219406}.
MOD_RES 986 986 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:11349134,
ECO:0000269|PubMed:12235291}.
MOD_RES 1131 1131 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1135 1135 Phosphotyrosine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 1162 1162 Phosphotyrosine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11687594}.
MOD_RES 1257 1257 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 242 Missing (in isoform 2).
{ECO:0000303|PubMed:8530088}.
/FTId=VSP_027985.
VARIANT 401 401 R -> W (in OPSMD; dbSNP:rs397514511).
{ECO:0000269|PubMed:23273569}.
/FTId=VAR_069586.
VARIANT 632 632 L -> I (associated with susceptibility to
NIDDM; dbSNP:rs61749195).
{ECO:0000269|PubMed:15687335}.
/FTId=VAR_034980.
VARIANT 659 659 P -> S (in OPSMD; dbSNP:rs397514510).
{ECO:0000269|PubMed:23273569}.
/FTId=VAR_069587.
VARIANT 688 688 W -> C (in OPSMD).
{ECO:0000269|PubMed:23273569}.
/FTId=VAR_069588.
VARIANT 721 721 V -> M (in dbSNP:rs116848359).
{ECO:0000269|PubMed:15687335}.
/FTId=VAR_034981.
VARIANT 722 722 F -> I (in OPSMD; dbSNP:rs397514512).
{ECO:0000269|PubMed:23273569}.
/FTId=VAR_069589.
VARIANT 982 982 N -> S (associated with susceptibility to
NIDDM; dbSNP:rs70940821).
{ECO:0000269|PubMed:15687335}.
/FTId=VAR_034982.
VARIANT 1083 1083 A -> G (in dbSNP:rs11548491).
{ECO:0000269|PubMed:15687335}.
/FTId=VAR_034983.
VARIANT 1114 1114 A -> G (in dbSNP:rs1049472).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9367831,
ECO:0000269|Ref.4}.
/FTId=VAR_034984.
MUTAGEN 47 47 R->G: Abolishes interaction with
p130Cas/BCAR1 and its ability to induce
increased adhesion. Abolishes
phosphorylation upon FCGR2A clustering.
{ECO:0000269|PubMed:11158326,
ECO:0000269|PubMed:12690104}.
MUTAGEN 140 141 PL->AA: Abolishes interaction with
SH3YL1. {ECO:0000269|PubMed:21624956}.
MUTAGEN 607 607 D->A: Abolishes enzyme activity but not
phosphorylation upon FCGR2A clustering.
{ECO:0000269|PubMed:12690104}.
MUTAGEN 958 958 T->A: Reduces PDGF-stimulated tyrosine
phosphorylation and association with
SHC1. {ECO:0000269|PubMed:17219406}.
MUTAGEN 986 987 YY->FF: Inducer a strong reduction of
phosphorylation upon re-plating on
collagen I.
{ECO:0000269|PubMed:12235291}.
CONFLICT 307 307 I -> M (in Ref. 1; AAA96658).
{ECO:0000305}.
CONFLICT 1142 1142 R -> A (in Ref. 1; AAA50503/AAA96658).
{ECO:0000305}.
STRAND 21 23 {ECO:0000244|PDB:2MK2}.
HELIX 28 38 {ECO:0000244|PDB:2MK2}.
STRAND 41 48 {ECO:0000244|PDB:2MK2}.
STRAND 56 61 {ECO:0000244|PDB:2MK2}.
STRAND 66 72 {ECO:0000244|PDB:2MK2}.
STRAND 75 77 {ECO:0000244|PDB:2MK2}.
STRAND 79 81 {ECO:0000244|PDB:2MK2}.
STRAND 85 87 {ECO:0000244|PDB:2MK2}.
STRAND 91 94 {ECO:0000244|PDB:2MK2}.
HELIX 95 102 {ECO:0000244|PDB:2MK2}.
STRAND 422 432 {ECO:0000244|PDB:5OKP}.
HELIX 443 446 {ECO:0000244|PDB:5OKP}.
STRAND 450 453 {ECO:0000244|PDB:5OKP}.
TURN 458 460 {ECO:0000244|PDB:5OKP}.
STRAND 465 473 {ECO:0000244|PDB:5OKP}.
HELIX 478 493 {ECO:0000244|PDB:5OKP}.
STRAND 498 505 {ECO:0000244|PDB:5OKP}.
STRAND 508 514 {ECO:0000244|PDB:5OKP}.
HELIX 516 521 {ECO:0000244|PDB:5OKP}.
STRAND 522 531 {ECO:0000244|PDB:5OKP}.
STRAND 538 550 {ECO:0000244|PDB:5OKP}.
STRAND 553 561 {ECO:0000244|PDB:5OKP}.
HELIX 569 582 {ECO:0000244|PDB:5OKP}.
HELIX 588 592 {ECO:0000244|PDB:5OKM}.
HELIX 595 597 {ECO:0000244|PDB:5OKP}.
STRAND 599 607 {ECO:0000244|PDB:5OKP}.
STRAND 612 614 {ECO:0000244|PDB:5OKP}.
HELIX 616 624 {ECO:0000244|PDB:5OKP}.
HELIX 629 632 {ECO:0000244|PDB:5OKP}.
HELIX 636 642 {ECO:0000244|PDB:5OKP}.
STRAND 645 647 {ECO:0000244|PDB:5OKP}.
STRAND 675 677 {ECO:0000244|PDB:4A9C}.
STRAND 680 682 {ECO:0000244|PDB:4A9C}.
STRAND 690 696 {ECO:0000244|PDB:5OKP}.
STRAND 702 709 {ECO:0000244|PDB:5OKP}.
STRAND 715 718 {ECO:0000244|PDB:5OKP}.
STRAND 721 728 {ECO:0000244|PDB:5OKP}.
TURN 732 734 {ECO:0000244|PDB:5OKO}.
STRAND 747 758 {ECO:0000244|PDB:5OKP}.
STRAND 765 770 {ECO:0000244|PDB:5OKP}.
STRAND 774 776 {ECO:0000244|PDB:5OKO}.
STRAND 784 787 {ECO:0000244|PDB:5OKP}.
STRAND 793 799 {ECO:0000244|PDB:5OKP}.
HELIX 800 802 {ECO:0000244|PDB:5OKP}.
HELIX 813 816 {ECO:0000244|PDB:5OKP}.
STRAND 820 827 {ECO:0000244|PDB:5OKP}.
TURN 828 830 {ECO:0000244|PDB:5OKP}.
STRAND 833 841 {ECO:0000244|PDB:5OKP}.
TURN 842 844 {ECO:0000244|PDB:5OKP}.
STRAND 845 848 {ECO:0000244|PDB:5OKO}.
STRAND 850 858 {ECO:0000244|PDB:5OKP}.
STRAND 861 873 {ECO:0000244|PDB:5OKP}.
HELIX 1202 1206 {ECO:0000244|PDB:2K4P}.
TURN 1207 1209 {ECO:0000244|PDB:2K4P}.
HELIX 1211 1213 {ECO:0000244|PDB:2K4P}.
HELIX 1214 1218 {ECO:0000244|PDB:2K4P}.
TURN 1219 1221 {ECO:0000244|PDB:2K4P}.
HELIX 1225 1228 {ECO:0000244|PDB:2K4P}.
HELIX 1233 1238 {ECO:0000244|PDB:2K4P}.
HELIX 1244 1256 {ECO:0000244|PDB:2K4P}.
SEQUENCE 1258 AA; 138599 MW; D76B5AA8ACDE8CBA CRC64;
MASACGAPGP GGALGSQAPS WYHRDLSRAA AEELLARAGR DGSFLVRDSE SVAGAFALCV
LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG LYAQPNQGLV CALLLPVEGE
REPDPPDDRD ASDGEDEKPP LPPRSGSTSI SAPTGPSSPL PAPETPTAPA AESAPNGLST
VSHDYLKGSY GLDLEAVRGG ASHLPHLTRT LATSCRRLHS EVDKVLSGLE ILSKVFDQQS
SPMVTRLLQQ QNLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPQPS
TRKAKTIPVQ AFEVKLDVTL GDLTKIGKSQ KFTLSVDVEG GRLVLLRRQR DSQEDWTTFT
HDRIRQLIKS QRVQNKLGVV FEKEKDRTQR KDFIFVSARK REAFCQLLQL MKNKHSKQDE
PDMISVFIGT WNMGSVPPPK NVTSWFTSKG LGKTLDEVTV TIPHDIYVFG TQENSVGDRE
WLDLLRGGLK ELTDLDYRPI AMQSLWNIKV AVLVKPEHEN RISHVSTSSV KTGIANTLGN
KGAVGVSFMF NGTSFGFVNC HLTSGNEKTA RRNQNYLDIL RLLSLGDRQL NAFDISLRFT
HLFWFGDLNY RLDMDIQEIL NYISRKEFEP LLRVDQLNLE REKHKVFLRF SEEEISFPPT
YRYERGSRDT YAWHKQKPTG VRTNVPSWCD RILWKSYPET HIICNSYGCT DDIVTSDHSP
VFGTFEVGVT SQFISKKGLS KTSDQAYIEF ESIEAIVKTA SRTKFFIEFY STCLEEYKKS
FENDAQSSDN INFLKVQWSS RQLPTLKPIL ADIEYLQDQH LLLTVKSMDG YESYGECVVA
LKSMIGSTAQ QFLTFLSHRG EETGNIRGSM KVRVPTERLG TRERLYEWIS IDKDEAGAKS
KAPSVSRGSQ EPRSGSRKPA FTEASCPLSR LFEEPEKPPP TGRPPAPPRA APREEPLTPR
LKPEGAPEPE GVAAPPPKNS FNNPAYYVLE GVPHQLLPPE PPSPARAPVP SATKNKVAIT
VPAPQLGHHR HPRVGEGSSS DEESGGTLPP PDFPPPPLPD SAIFLPPSLD PLPGPVVRGR
GGAEARGPPP PKAHPRPPLP PGPSPASTFL GEVASGDDRS CSVLQMAKTL SEVDYAPAGP
ARSALLPGPL ELQPPRGLPS DYGRPLSFPP PRIRESIQED LAEEAPCLQG GRASGLGEAG
MSAWLRAIGL ERYEEGLVHN GWDDLEFLSD ITEEDLEEAG VQDPAHKRLL LDTLQLSK


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EIAAB38291 Inositol polyphosphate phosphatase-like protein 1,Inppl1,INPPL-1,Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2,Rat,Rattus norvegicus,SH2 domain-containing inositol phosphatase 2,SH2 domain-
EIAAB38289 Homo sapiens,Human,Inositol polyphosphate phosphatase-like protein 1,INPPL1,INPPL-1,Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2,Protein 51C,SH2 domain-containing inositol phosphatase 2,SH
EIAAB38290 AblSH3-binding protein,Inositol polyphosphate phosphatase-like protein 1,Inppl1,INPPL-1,Mouse,Mus musculus,Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2,SH2 domain-containing inositol phosp
EIAAB38287 Inpp5d,Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1,Rat,Rattus norvegicus,SH2 domain-containing inositol phosphatase 1,SH2 domain-containing inositol-5'-phosphatase 1,Ship,Ship1,SHIP-1
EIAAB38286 7a33,Inositol polyphosphate-5-phosphatase of 145 kDa,Inpp5d,Mouse,Mus musculus,p150Ship,Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1,SH2 domain-containing inositol phosphatase 1,SH2 domain
EIAAB38288 Homo sapiens,hp51CN,Human,Inositol polyphosphate-5-phosphatase of 145 kDa,INPP5D,p150Ship,Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1,SH2 domain-containing inositol phosphatase 1,SH2 doma
EIAAB37179 Homo sapiens,hSAC2,Human,Inositol polyphosphate 5-phosphatase F,INPP5F,KIAA0966,MSTP007,MSTP047,Phosphatidylinositide phosphatase SAC2,Sac domain-containing inositol phosphatase 2,Sac domain-containin
EIAAB37180 Inositol polyphosphate 5-phosphatase F,Inpp5f,Kiaa0966,Mouse,Mus musculus,Phosphatidylinositide phosphatase SAC2,Sac domain-containing inositol phosphatase 2,Sac domain-containing phosphoinositide 5-p
EIAAB31027 Inositol polyphosphate 5-phosphatase J,Inpp5j,Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A,Pib5pa,Pipp,Proline-rich inositol polyphosphate 5-phosphatase,Rat,Rattus norvegicus
EIAAB24785 Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase,Ins(1,3,4,5)P(4) 3-phosphatase,Minpp1,Mipp,MNCb-1572,Mouse,Multiple inositol polyphosphate phosphatase 1,Mus musculus
EIAAB24786 Homo sapiens,Human,Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase,Ins(1,3,4,5)P(4) 3-phosphatase,MINPP1,MIPP,Multiple inositol polyphosphate phosphatase 1,UNQ900_PRO1917
EIAAB24787 Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase,Ins(1,3,4,5)P(4) 3-phosphatase,Minpp1,Mipp1,Multiple inositol polyphosphate phosphatase 1,Rat,Rattus norvegicus
FP-0084 Signaling inositol polyphosphate phosphatase SHIP II.; SH2-Domain: SHIP2 10ug
EIAAB31028 Inositol polyphosphate 5-phosphatase J,Inpp5j,Mouse,Mus musculus,Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A,Pib5pa
EIAAB31026 Homo sapiens,Human,Inositol polyphosphate 5-phosphatase J,INPP5J,Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A,PIB5PA,PIPP
FP-0083 SH2 containing inositol-5-phosphatase.; SH2-Domain: SHIP 10ug
FP-0084 Signaling inositol polyphosphate phosphatase SHIP II. 10ug
FP-0084 Signaling inositol polyphosphate phosphatase SHIP II. 10 ug
EIAAB43668 Homo sapiens,Human,Lipid phosphatase TPIP,Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase TPTE2,TPIP,TPTE and PTEN homologous inositol lipid phosphatase,TPTE2
FP-0084 Fusion proteins: Signaling inositol polyphosphate phosphatase SHIP II., SHIP2 10ug
FP-0037 Signaling inositol polyphosphate 5 phosphatase SIP-145; SH2-Domain: INPP5D 10ug
FP-0083 Fusion proteins: SH2 containing inositol-5-phosphatase., SHIP 10ug
EIAAB37945 27 kDa inositol polyphosphate phosphatase interacting protein B,Bos taurus,Bovine,FAM109B,IPIP27B,Ses2,Sesquipedalian-2
EIAAB37942 27 kDa inositol polyphosphate phosphatase interacting protein A,Fam109a,IPIP27A,Mouse,Mus musculus,Ses1,Sesquipedalian-1
EIAAB37944 27 kDa inositol polyphosphate phosphatase interacting protein A,Fam109a,IPIP27A,Rat,Rattus norvegicus,Ses1,Sesquipedalian-1


 

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