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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)

 SHIP1_MOUSE             Reviewed;        1191 AA.
Q9ES52; Q3UPF9; Q4U212; Q61034; Q61173; Q61181; Q9JKR7; Q9JLF9;
Q9JLG0; Q9QVN8; Q9WUC2;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
10-MAY-2017, entry version 139.
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;
Name=Inpp5d; Synonyms=7a33, Ship, Ship1;
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] (ISOFORM 2), PROTEIN SEQUENCE OF 2-9 AND
1163-1173, FUNCTION, ENZYME ACTIVITY, PHOSPHORYLATION, TISSUE
SPECIFICITY, AND INTERACTION WITH SHC1.
STRAIN=DBA/2J;
PubMed=8654924; DOI=10.1101/gad.10.9.1084;
Lioubin M.N., Algate P.A., Tsai S., Carlberg K., Aebersold A.,
Rohrschneider L.R.;
"p150Ship, a signal transduction molecule with inositol polyphosphate-
5-phosphatase activity.";
Genes Dev. 10:1084-1095(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 902-916,
ENZYME ACTIVITY, TISSUE SPECIFICITY, AND INTERACTION WITH GRB2 AND
SHC1.
PubMed=8643691; DOI=10.1073/pnas.93.4.1689;
Damen J.E., Liu L., Rosten P., Humphries R.K., Jefferson A.B.,
Majerus P.W., Krystal G.;
"The 145-kDa protein induced to associate with Shc by multiple
cytokines is an inositol tetraphosphate and phosphatidylinositol
3,4,5-triphosphate 5-phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 93:1689-1693(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9027494; DOI=10.1006/geno.1996.4374;
Liu Q., Dumont D.J.;
"Molecular cloning and chromosomal localization in human and mouse of
the SH2-containing inositol phosphatase, INPP5D (SHIP).";
Genomics 39:109-112(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PHOSPHORYLATION, INTERACTION
WITH SHC1 AND GRB2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=BALB/cJ;
PubMed=10068665;
Lucas D.M., Rohrschneider L.R.;
"A novel spliced form of SH2-containing inositol phosphatase is
expressed during myeloid development.";
Blood 93:1922-1933(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 4).
STRAIN=129/Sv;
PubMed=11013080; DOI=10.1006/geno.2000.6324;
Wolf I., Lucas D.M., Algate P.A., Rohrschneider L.R.;
"Cloning of the genomic locus of mouse SH2 containing inositol 5-
phosphatase (SHIP) and a novel 110-kDa splice isoform, SHIPdelta.";
Genomics 69:104-112(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND SUBCELLULAR LOCATION
(ISOFORM 5).
PubMed=11567986; DOI=10.1182/blood.V98.7.2028;
Tu Z., Ninos J.M., Ma Z., Wang J.-W., Lemos M.P., Desponts C.,
Ghansah T., Howson J.M., Kerr W.G.;
"Embryonic and hematopoietic stem cells express a novel SH2-containing
inositol 5'-phosphatase isoform that partners with the Grb2 adapter
protein.";
Blood 98:2028-2038(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thyroid;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-106.
PubMed=8632995; DOI=10.1073/pnas.93.9.3947;
Kerr W.G., Heller M., Herzenberg L.A.;
"Analysis of lipopolysaccharide-response genes in B-lineage cells
demonstrates that they can have differentiation stage-restricted
expression and contain SH2 domains.";
Proc. Natl. Acad. Sci. U.S.A. 93:3947-3952(1996).
[10]
PARTIAL PROTEIN SEQUENCE.
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).
[11]
FUNCTION.
PubMed=8805703; DOI=10.1038/383263a0;
Ono M., Bolland S., Tempst P., Ravetch J.V.;
"Role of the inositol phosphatase SHIP in negative regulation of the
immune system by the receptor Fc(gamma)RIIB.";
Nature 383:263-266(1996).
[12]
PHOSPHORYLATION.
PubMed=8805618;
Chacko G.W., Tridandapani S., Damen J.E., Liu L., Krystal G.,
Coggeshall K.M.;
"Negative signaling in B lymphocytes induces tyrosine phosphorylation
of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP.";
J. Immunol. 157:2234-2238(1996).
[13]
FUNCTION.
PubMed=9244303; DOI=10.1016/S0092-8674(00)80337-2;
Ono M., Okada H., Bolland S., Yanagi S., Kurosaki T., Ravetch J.V.;
"Deletion of SHIP or SHP-1 reveals two distinct pathways for
inhibitory signaling.";
Cell 90:293-301(1997).
[14]
DOMAIN SH2, AND INTERACTION WITH SHC1.
PubMed=9083021; DOI=10.1074/jbc.272.14.8983;
Liu L., Damen J.E., Hughes M.R., Babic I., Jirik F.R., Krystal G.;
"The Src homology 2 (SH2) domain of SH2-containing inositol
phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP,
its association with Shc, and its induction of apoptosis.";
J. Biol. Chem. 272:8983-8988(1997).
[15]
PHOSPHORYLATION AT TYR-918 AND TYR-1021, INTERACTION WITH SHC1, AND
MUTAGENESIS OF TYR-918 AND TYR-1021.
PubMed=9099679; DOI=10.1074/jbc.272.16.10396;
Lamkin T.D., Walk S.F., Liu L., Damen J.E., Krystal G.,
Ravichandran K.S.;
"Shc interaction with Src homology 2 domain containing inositol
phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding
domain and two specific phosphotyrosines on SHIP.";
J. Biol. Chem. 272:10396-10401(1997).
[16]
INTERACTION WITH PTPN11.
PubMed=9110989; DOI=10.1074/jbc.272.17.10998;
Liu L., Damen J.E., Ware M.D., Krystal G.;
"Interleukin-3 induces the association of the inositol 5-phosphatase
SHIP with SHP2.";
J. Biol. Chem. 272:10998-11001(1997).
[17]
INTERACTION WITH DAB2.
PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
Morris S.M., Cooper J.A.;
"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and
interacts with AP-2.";
Traffic 2:111-123(2001).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-935 AND TYR-945, 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).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-935; THR-964;
SER-967 AND SER-972, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
Testis;
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).
[21]
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).
[22]
ENZYME ACTIVITY.
PubMed=9341117; DOI=10.1074/jbc.272.43.26857;
Giuriato S., Payrastre B., Drayer A.L., Plantavid M., Woscholski R.,
Parker P., Erneux C., Chap H.;
"Tyrosine phosphorylation and relocation of SHIP are integrin-mediated
in thrombin-stimulated human blood platelets.";
J. Biol. Chem. 272:26857-26863(1997).
[23]
INTERACTION WITH PTPN11.
PubMed=9393882; DOI=10.1038/sj.onc.1201422;
Sattler M., Salgia R., Shrikhande G., Verma S., Choi J.-L.,
Rohrschneider L.R., Griffin J.D.;
"The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the
protein tyrosine phosphatase SHP-2 form a complex in hematopoietic
cells which can be regulated by BCR/ABL and growth factors.";
Oncogene 15:2379-2384(1997).
[24]
SUBCELLULAR LOCATION.
PubMed=9694708;
Damen J.E., Liu L., Ware M.D., Ermolaeva M., Majerus P.W., Krystal G.;
"Multiple forms of the SH2-containing inositol phosphatase, SHIP, are
generated by C-terminal truncation.";
Blood 92:1199-1205(1998).
[25]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9531585;
Liu Q., Shalaby F., Jones J., Bouchard D., Dumont D.J.;
"The SH2-containing inositol polyphosphate 5-phosphatase, ship, is
expressed during hematopoiesis and spermatogenesis.";
Blood 91:2753-2759(1998).
[26]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9857188; DOI=10.1093/emboj/17.24.7311;
Huber M., Helgason C.D., Scheid M.P., Duronio V., Humphries R.K.,
Krystal G.;
"Targeted disruption of SHIP leads to Steel factor-induced
degranulation of mast cells.";
EMBO J. 17:7311-7319(1998).
[27]
FUNCTION.
PubMed=9763612; DOI=10.1084/jem.188.7.1333;
Liu Q., Oliveira-Dos-Santos A.J., Mariathasan S., Bouchard D.,
Jones J., Sarao R., Kozieradzki I., Ohashi P.S., Penninger J.M.,
Dumont D.J.;
"The inositol polyphosphate 5-phosphatase ship is a crucial negative
regulator of B cell antigen receptor signaling.";
J. Exp. Med. 188:1333-1342(1998).
[28]
FUNCTION.
PubMed=9736736; DOI=10.1073/pnas.95.19.11330;
Huber M., Helgason C.D., Damen J.E., Liu L., Humphries R.K.,
Krystal G.;
"The src homology 2-containing inositol phosphatase (SHIP) is the
gatekeeper of mast cell degranulation.";
Proc. Natl. Acad. Sci. U.S.A. 95:11330-11335(1998).
[29]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9620849; DOI=10.1101/gad.12.11.1610;
Helgason C.D., Damen J.E., Rosten P., Grewal R., Sorensen P.,
Chappel S.M., Borowski A., Jirik F., Krystal G., Humphries R.K.;
"Targeted disruption of SHIP leads to hemopoietic perturbations, lung
pathology, and a shortened life span.";
Genes Dev. 12:1610-1620(1998).
[30]
INTERACTION WITH SHC1 AND FCGR2B, AND PHOSPHORYLATION.
PubMed=10395202; DOI=10.1016/S0161-5890(98)00097-2;
Tridandapani S., Phee H., Shivakumar L., Kelley T.W., Coggeshall K.M.;
"Role of SHIP in FcgammaRIIb-mediated inhibition of Ras activation in
B cells.";
Mol. Immunol. 35:1135-1146(1998).
[31]
INTERACTION WITH SRC.
PubMed=10794720; DOI=10.1042/bj3480107;
Giuriato S., Bodin S., Erneux C., Woscholski R., Plantavid M.,
Chap H., Payrastre B.;
"pp60c-src associates with the SH2-containing inositol-5-phosphatase
SHIP1 and is involved in its tyrosine phosphorylation downstream of
alphaIIbbeta3 integrin in human platelets.";
Biochem. J. 348:107-112(2000).
[32]
INTERACTION WITH EPOR, AND PHOSPHORYLATION.
PubMed=10660611; DOI=10.1074/jbc.275.6.4398;
Mason J.M., Beattie B.K., Liu Q., Dumont D.J., Barber D.L.;
"The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent
manner to the erythropoietin receptor.";
J. Biol. Chem. 275:4398-4406(2000).
[33]
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).
[34]
INTERACTION WITH FCGR2B.
PubMed=10779347; DOI=10.1128/MCB.20.10.3576-3589.2000;
Aman M.J., Walk S.F., March M.E., Su H.-P., Carver D.J.,
Ravichandran K.S.;
"Essential role for the C-terminal noncatalytic region of SHIP in
FcgammaRIIB1-mediated inhibitory signaling.";
Mol. Cell. Biol. 20:3576-3589(2000).
[35]
FUNCTION, AND MUTAGENESIS OF ASP-676; TYR-918 AND TYR-1021.
PubMed=11222379; DOI=10.1182/blood.V97.5.1343;
Damen J.E., Ware M.D., Kalesnikoff J., Hughes M.R., Krystal G.;
"SHIP's C-terminus is essential for its hydrolysis of PIP3 and
inhibition of mast cell degranulation.";
Blood 97:1343-1351(2001).
[36]
INTERACTION WITH DOK1 AND CRKL, AND MUTAGENESIS OF TYR-918 AND
TYR-1021.
PubMed=11031258; DOI=10.1074/jbc.M006250200;
Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R.,
Griffin J.D.;
"SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates
migration through two critical tyrosine residues and forms a novel
signaling complex with DOK1 and CRKL.";
J. Biol. Chem. 276:2451-2458(2001).
[37]
FUNCTION.
PubMed=11359765; DOI=10.1074/jbc.M011094200;
Malbec O., Schmitt C., Bruhns P., Krystal G., Fridman W.H.,
Daeeron M.;
"Src homology 2 domain-containing inositol 5-phosphatase 1 mediates
cell cycle arrest by FcgammaRIIB.";
J. Biol. Chem. 276:30381-30391(2001).
[38]
FUNCTION.
PubMed=11136821; DOI=10.1084/jem.193.1.61;
Cox D., Dale B.M., Kashiwada M., Helgason C.D., Greenberg S.;
"A regulatory role for Src homology 2 domain-containing inositol 5'-
phosphatase (SHIP) in phagocytosis mediated by Fc gamma receptors and
complement receptor 3 (alpha(M)beta(2); CD11b/CD18).";
J. Exp. Med. 193:61-71(2001).
[39]
SUBCELLULAR LOCATION, AND INTERACTION WITH FCGR3.
PubMed=12393695; DOI=10.1182/blood-2002-04-1058;
Galandrini R., Tassi I., Mattia G., Lenti L., Piccoli M., Frati L.,
Santoni A.;
"SH2-containing inositol phosphatase (SHIP-1) transiently translocates
to raft domains and modulates CD16-mediated cytotoxicity in human NK
cells.";
Blood 100:4581-4589(2002).
[40]
FUNCTION, INTERACTION WITH FCGR2A, AND PHOSPHORYLATION.
PubMed=12370370; DOI=10.4049/jimmunol.169.8.4370;
Tridandapani S., Wang Y., Marsh C.B., Anderson C.L.;
"Src homology 2 domain-containing inositol polyphosphate phosphatase
regulates NF-kappa B-mediated gene transcription by phagocytic Fc
gamma Rs in human myeloid cells.";
J. Immunol. 169:4370-4378(2002).
[41]
FUNCTION, AND INDUCTION.
PubMed=12447389; DOI=10.1038/ncb885;
Valderrama-Carvajal H., Cocolakis E., Lacerte A., Lee E.-H.,
Krystal G., Ali S., Lebrun J.-J.;
"Activin/TGF-beta induce apoptosis through Smad-dependent expression
of the lipid phosphatase SHIP.";
Nat. Cell Biol. 4:963-969(2002).
[42]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12161749; DOI=10.1038/nm752;
Takeshita S., Namba N., Zhao J.J., Jiang Y., Genant H.K., Silva M.J.,
Brodt M.D., Helgason C.D., Kalesnikoff J., Rauh M.J., Humphries R.K.,
Krystal G., Teitelbaum S.L., Ross F.P.;
"SHIP-deficient mice are severely osteoporotic due to increased
numbers of hyper-resorptive osteoclasts.";
Nat. Med. 8:943-949(2002).
[43]
FUNCTION, AND INTERACTION WITH MET.
PubMed=11896575; DOI=10.1038/sj.onc.1205224;
Mancini A., Koch A., Wilms R., Tamura T.;
"The SH2-containing inositol 5-phosphatase (SHIP)-1 is implicated in
the control of cell-cell junction and induces dissociation and
dispersion of MDCK cells.";
Oncogene 21:1477-1484(2002).
[44]
FUNCTION.
PubMed=12882960; DOI=10.1074/jbc.M305021200;
Baran C.P., Tridandapani S., Helgason C.D., Humphries R.K.,
Krystal G., Marsh C.B.;
"The inositol 5'-phosphatase SHIP-1 and the Src kinase Lyn negatively
regulate macrophage colony-stimulating factor-induced Akt activity.";
J. Biol. Chem. 278:38628-38636(2003).
[45]
FUNCTION.
PubMed=15166241; DOI=10.1074/jbc.M400746200;
Maxwell M.J., Yuan Y., Anderson K.E., Hibbs M.L., Salem H.H.,
Jackson S.P.;
"SHIP1 and Lyn kinase negatively regulate integrin alpha IIb beta 3
signaling in platelets.";
J. Biol. Chem. 279:32196-32204(2004).
[46]
INTERACTION WITH FCGR2B.
PubMed=15456754; DOI=10.1074/jbc.M410261200;
Isnardi I., Lesourne R., Bruhns P., Fridman W.H., Cambier J.C.,
Daeeron M.;
"Two distinct tyrosine-based motifs enable the inhibitory receptor
FcgammaRIIB to cooperatively recruit the inositol phosphatases SHIP1/2
and the adapters Grb2/Grap.";
J. Biol. Chem. 279:51931-51938(2004).
[47]
INTERACTION WITH TEC.
PubMed=15492005; DOI=10.1074/jbc.M408141200;
Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.;
"SHIP family inositol phosphatases interact with and negatively
regulate the Tec tyrosine kinase.";
J. Biol. Chem. 279:55089-55096(2004).
[48]
FUNCTION, AND INTERACTION WITH DOK3.
PubMed=14993273; DOI=10.1128/MCB.24.6.2332-2343.2004;
Robson J.D., Davidson D., Veillette A.;
"Inhibition of the Jun N-terminal protein kinase pathway by SHIP-1, a
lipid phosphatase that interacts with the adaptor molecule Dok-3.";
Mol. Cell. Biol. 24:2332-2343(2004).
[49]
INTERACTION WITH PLCG1.
PubMed=16000869; DOI=10.1038/emm.2005.22;
Song M., Kim M.J., Ha S., Park J.B., Ryu S.H., Suh P.-G.;
"Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1
and modulates EGF-induced PLC activity.";
Exp. Mol. Med. 37:161-168(2005).
[50]
SUBCELLULAR LOCATION.
PubMed=16406061; DOI=10.1016/j.imlet.2005.11.027;
Isnardi I., Bruhns P., Bismuth G., Fridman W.H., Daeeron M.;
"The SH2 domain-containing inositol 5-phosphatase SHIP1 is recruited
to the intracytoplasmic domain of human FcgammaRIIB and is mandatory
for negative regulation of B cell activation.";
Immunol. Lett. 104:156-165(2006).
[51]
FUNCTION.
PubMed=17142780; DOI=10.4049/jimmunol.177.12.8777;
Zhou P., Kitaura H., Teitelbaum S.L., Krystal G., Ross F.P.,
Takeshita S.;
"SHIP1 negatively regulates proliferation of osteoclast precursors via
Akt-dependent alterations in D-type cyclins and p27.";
J. Immunol. 177:8777-8784(2006).
[52]
INTERACTION WITH IL6ST.
PubMed=17105399; DOI=10.1089/scd.2006.15.641;
Desponts C., Ninos J.M., Kerr W.G.;
"s-SHIP associates with receptor complexes essential for pluripotent
stem cell growth and survival.";
Stem Cells Dev. 15:641-646(2006).
[53]
FUNCTION.
PubMed=17173042; DOI=10.1038/ncb1515;
Nishio M., Watanabe K., Sasaki J., Taya C., Takasuga S., Iizuka R.,
Balla T., Yamazaki M., Watanabe H., Itoh R., Kuroda S., Horie Y.,
Foerster I., Mak T.W., Yonekawa H., Penninger J.M., Kanaho Y.,
Suzuki A., Sasaki T.;
"Control of cell polarity and motility by the PtdIns(3,4,5)P3
phosphatase SHIP1.";
Nat. Cell Biol. 9:36-44(2007).
-!- 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:11136821, ECO:0000269|PubMed:11222379,
ECO:0000269|PubMed:11359765, ECO:0000269|PubMed:11896575,
ECO:0000269|PubMed:12161749, ECO:0000269|PubMed:12370370,
ECO:0000269|PubMed:12447389, ECO:0000269|PubMed:12882960,
ECO:0000269|PubMed:14993273, ECO:0000269|PubMed:15166241,
ECO:0000269|PubMed:17142780, ECO:0000269|PubMed:17173042,
ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:8805703,
ECO:0000269|PubMed:9244303, ECO:0000269|PubMed:9620849,
ECO:0000269|PubMed:9736736, ECO:0000269|PubMed:9763612,
ECO:0000269|PubMed:9857188}.
-!- 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:8643691,
ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:9341117}.
-!- ENZYME REGULATION: Activated upon translocation to the sites of
synthesis of PtdIns(3,4,5)P3 in the membrane.
-!- SUBUNIT: Interacts with tyrosine phosphorylated forms of SHC1,
DOK1, DOK3, PTPN11/SHP-2, SLAMF1/CD150. Interacts with PTPN11 in
response to IL-3. Interacts with receptors EPOR, MS4A2/FCER1B and
FCER1G, FCGR2A, FCGR2B and FCGR3. Interacts with GRB2 and PLCG1.
Interacts with tyrosine kinases SRC and TEC. Interacts with
FCGR2A, leading to regulate gene expression during the phagocytic
process. Interacts with c-Met/MET. Interacts with MILR1 (tyrosine-
phosphorylated). Isoform 5 interacts with IL6ST/gp130. Can weakly
interact (via NPXY motif 2) with DAB2 (via PID domain); the
interaction is impaired by tyrosine phosphorylation of the NPXY
motif. {ECO:0000269|PubMed:10068665, ECO:0000269|PubMed:10395202,
ECO:0000269|PubMed:10660611, ECO:0000269|PubMed:10779347,
ECO:0000269|PubMed:10794720, ECO:0000269|PubMed:11016922,
ECO:0000269|PubMed:11031258, ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11896575, ECO:0000269|PubMed:12370370,
ECO:0000269|PubMed:12393695, ECO:0000269|PubMed:14993273,
ECO:0000269|PubMed:15456754, ECO:0000269|PubMed:15492005,
ECO:0000269|PubMed:16000869, ECO:0000269|PubMed:17105399,
ECO:0000269|PubMed:20526344, ECO:0000269|PubMed:8643691,
ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:9083021,
ECO:0000269|PubMed:9099679, ECO:0000269|PubMed:9110989,
ECO:0000269|PubMed:9393882}.
-!- INTERACTION:
P23727:PIK3R1 (xeno); NbExp=2; IntAct=EBI-1452545, EBI-520244;
Q8CIH5:Plcg2; NbExp=3; IntAct=EBI-300210, EBI-617954;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16406061}.
Cell membrane {ECO:0000269|PubMed:12393695}; Peripheral membrane
protein {ECO:0000305|PubMed:12393695}. Membrane raft
{ECO:0000269|PubMed:12393695}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:9694708}. Note=Translocates to the plasma
membrane when activated, translocation is probably due to
different mechanisms depending on the stimulus and cell type
(PubMed:12393695). Translocates from the cytoplasm to membrane
ruffles in a FCGR3/CD16-dependent manner (PubMed:12393695).
Colocalizes with FC-gamma-RIIB receptor (FCGR2B) or FCGR3/CD16 at
membrane ruffles (PubMed:12393695). Tyrosine phosphorylation may
also participate in membrane localization (PubMed:12393695).
{ECO:0000269|PubMed:12393695}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane
{ECO:0000269|PubMed:11567986}; Peripheral membrane protein
{ECO:0000305|PubMed:11567986}. Note=Constitutively present at the
cell membrane (PubMed:11567986). {ECO:0000269|PubMed:11567986}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q9ES52-1; Sequence=Displayed;
Name=2;
IsoId=Q9ES52-2; Sequence=VSP_027981;
Name=3; Synonyms=135 kDa SHIP;
IsoId=Q9ES52-3; Sequence=VSP_027982;
Name=4; Synonyms=SHIPdelta;
IsoId=Q9ES52-4; Sequence=VSP_027981, VSP_027983, VSP_027984;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=5; Synonyms=s-SHIP;
IsoId=Q9ES52-5; Sequence=VSP_027980;
Name=6; Synonyms=s-SHIPD183;
IsoId=Q9ES52-6; Sequence=VSP_027980, VSP_027982;
-!- TISSUE SPECIFICITY: Specifically expressed in immune and
hematopoietic cells. Levels vary considerably within this
compartment. Lost during erythropoiesis when erythroid cells
become Ter119+. Increases substantially with T-cell maturation and
when resting B-cells are activated. Also present in mature
granulocytes, monocyte/macrophages, mast cells and platelets.
Isoform 5 is the only form expressed in embryonic stem (ES) cells
and is coexpressed with other isoforms in hematopoietic stem
cells, and disappears with differentiation.
{ECO:0000269|PubMed:10068665, ECO:0000269|PubMed:8643691,
ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:9531585}.
-!- DEVELOPMENTAL STAGE: Expressed in late primitive-streak stage
embryos (7.5 dpc), when hematopoiesis is thought to begin, and the
expression is restricted to the hematopoietic lineage in embryo.
In adults expression continues to be in the majority of cells from
hematopoietic origin, including granulocytes, monocytes and
lymphocytes, and is also found in the spermatids of the testis.
{ECO:0000269|PubMed:10068665, ECO:0000269|PubMed:9531585}.
-!- INDUCTION: By activin/TGF-beta (at protein level). Regulated by
the Smad pathway. Isoform 3 is expressed during myeloid
development. {ECO:0000269|PubMed:12447389}.
-!- 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.
{ECO:0000269|PubMed:9083021}.
-!- DOMAIN: The NPXY sequence motif found in many tyrosine-
phosphorylated proteins is required for the specific binding of
the PID domain. {ECO:0000269|PubMed:9083021}.
-!- 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:10068665,
ECO:0000269|PubMed:10395202, ECO:0000269|PubMed:10660611,
ECO:0000269|PubMed:12370370, ECO:0000269|PubMed:8654924,
ECO:0000269|PubMed:8805618, ECO:0000269|PubMed:9099679}.
-!- DISRUPTION PHENOTYPE: Mice are viable and fertile. They however
fail to thrive and only 40% survive by 14 weeks of age. Mortality
is associated with extensive consolidation of the lungs resulting
from infiltration by myeloid cells. Increased numbers of
granulocyte-macrophage progenitors are observed in both the bone
marrow and spleen. Absence of Inpp5d leads to steel factor-induced
degranulation of mast cells. They also display increased numbers
of osteoclast precursors leading to a severe osteoporosis.
{ECO:0000269|PubMed:12161749, ECO:0000269|PubMed:9620849,
ECO:0000269|PubMed:9857188}.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U51742; AAC52606.1; -; mRNA.
EMBL; U39203; AAB18937.1; -; mRNA.
EMBL; U52044; AAC53023.1; -; mRNA.
EMBL; AF125996; AAD37118.1; -; mRNA.
EMBL; AF235502; AAG23922.1; -; Genomic_DNA.
EMBL; AF235496; AAG23922.1; JOINED; Genomic_DNA.
EMBL; AF235498; AAG23922.1; JOINED; Genomic_DNA.
EMBL; AF235499; AAG23922.1; JOINED; Genomic_DNA.
EMBL; AF235500; AAG23922.1; JOINED; Genomic_DNA.
EMBL; AF235501; AAG23922.1; JOINED; Genomic_DNA.
EMBL; AF228679; AAF69143.1; -; mRNA.
EMBL; AF184912; AAF25823.1; -; mRNA.
EMBL; AF184913; AAF25824.1; -; mRNA.
EMBL; AK143560; BAE25436.1; -; mRNA.
EMBL; BC108328; AAI08329.1; -; mRNA.
CCDS; CCDS35655.1; -. [Q9ES52-1]
CCDS; CCDS48310.1; -. [Q9ES52-3]
CCDS; CCDS48311.1; -. [Q9ES52-2]
PIR; JC6118; JC6118.
RefSeq; NP_001103662.1; NM_001110192.2. [Q9ES52-2]
RefSeq; NP_001103663.1; NM_001110193.2. [Q9ES52-3]
RefSeq; NP_034696.2; NM_010566.3. [Q9ES52-1]
UniGene; Mm.15105; -.
ProteinModelPortal; Q9ES52; -.
SMR; Q9ES52; -.
BioGrid; 200769; 24.
IntAct; Q9ES52; 15.
MINT; MINT-205819; -.
STRING; 10090.ENSMUSP00000127941; -.
SwissLipids; SLP:000000873; -.
iPTMnet; Q9ES52; -.
PhosphoSitePlus; Q9ES52; -.
PaxDb; Q9ES52; -.
PeptideAtlas; Q9ES52; -.
PRIDE; Q9ES52; -.
Ensembl; ENSMUST00000042275; ENSMUSP00000044647; ENSMUSG00000026288. [Q9ES52-2]
Ensembl; ENSMUST00000072999; ENSMUSP00000072763; ENSMUSG00000026288. [Q9ES52-4]
Ensembl; ENSMUST00000167032; ENSMUSP00000126569; ENSMUSG00000026288. [Q9ES52-5]
Ensembl; ENSMUST00000168783; ENSMUSP00000131244; ENSMUSG00000026288. [Q9ES52-3]
Ensembl; ENSMUST00000169754; ENSMUSP00000127941; ENSMUSG00000026288. [Q9ES52-1]
Ensembl; ENSMUST00000170300; ENSMUSP00000132384; ENSMUSG00000026288. [Q9ES52-6]
GeneID; 16331; -.
KEGG; mmu:16331; -.
UCSC; uc007bxc.3; mouse. [Q9ES52-1]
UCSC; uc007bxd.3; mouse. [Q9ES52-3]
UCSC; uc007bxf.3; mouse. [Q9ES52-2]
UCSC; uc007bxg.3; mouse. [Q9ES52-6]
CTD; 3635; -.
MGI; MGI:107357; Inpp5d.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00760000119075; -.
HOVERGEN; HBG106726; -.
InParanoid; Q9ES52; -.
KO; K03084; -.
OMA; LTKPEMF; -.
OrthoDB; EOG091G00P6; -.
PhylomeDB; Q9ES52; -.
TreeFam; TF323475; -.
Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
PRO; PR:Q9ES52; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026288; -.
CleanEx; MM_INPP5D; -.
ExpressionAtlas; Q9ES52; baseline and differential.
Genevisible; Q9ES52; MM.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IDA:MGI.
GO; GO:0034594; F:phosphatidylinositol trisphosphate phosphatase activity; IDA:MGI.
GO; GO:0051425; F:PTB domain binding; IDA:MGI.
GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; IMP:MGI.
GO; GO:0050869; P:negative regulation of B cell activation; IMP:MGI.
GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:MGI.
GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; IMP:MGI.
GO; GO:0050777; P:negative regulation of immune response; IMP:MGI.
GO; GO:0045409; P:negative regulation of interleukin-6 biosynthetic process; IMP:MGI.
GO; GO:0045656; P:negative regulation of monocyte differentiation; IMP:MGI.
GO; GO:0045659; P:negative regulation of neutrophil differentiation; IMP:MGI.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
GO; GO:0009968; P:negative regulation of signal transduction; IMP:MGI.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:MGI.
GO; GO:0045621; P:positive regulation of lymphocyte differentiation; IMP:MGI.
Gene3D; 3.30.505.10; -; 1.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR000300; IPPc.
InterPro; IPR000980; SH2.
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;
Alternative splicing; Apoptosis; Cell membrane; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Hydrolase;
Immunity; Membrane; Phosphoprotein; Reference proteome; Repeat;
SH2 domain; SH3-binding.
CHAIN 1 1191 Phosphatidylinositol 3,4,5-trisphosphate
5-phosphatase 1.
/FTId=PRO_0000302867.
DOMAIN 8 104 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 1015 1029 Interaction with DAB2.
{ECO:0000269|PubMed:11247302}.
MOTIF 127 132 SH3-binding 1.
MOTIF 915 918 NPXY motif 1.
MOTIF 970 975 SH3-binding 2.
MOTIF 1018 1021 NPXY motif 2.
MOTIF 1039 1050 SH3-binding 3.
COMPBIAS 962 1153 Pro-rich.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 918 918 Phosphotyrosine.
{ECO:0000269|PubMed:9099679}.
MOD_RES 935 935 Phosphoserine.
{ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:21183079}.
MOD_RES 945 945 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 964 964 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 967 967 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 972 972 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1021 1021 Phosphotyrosine.
{ECO:0000269|PubMed:9099679}.
VAR_SEQ 1 263 Missing (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:11567986}.
/FTId=VSP_027980.
VAR_SEQ 120 120 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11013080,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8643691,
ECO:0000303|PubMed:8654924}.
/FTId=VSP_027981.
VAR_SEQ 920 980 Missing (in isoform 3 and isoform 6).
{ECO:0000303|PubMed:10068665}.
/FTId=VSP_027982.
VAR_SEQ 920 960 GMGPFGQPLHGKSTLSPDQQLTAWSYDQLPKDSSLGPGRGE
-> VFIFHSQPRSLPQGARGKTWGSGKGGSSAPGGPAADEA
RDV (in isoform 4).
{ECO:0000303|PubMed:11013080}.
/FTId=VSP_027983.
VAR_SEQ 961 1191 Missing (in isoform 4).
{ECO:0000303|PubMed:11013080}.
/FTId=VSP_027984.
MUTAGEN 676 676 D->G: Loss of function.
{ECO:0000269|PubMed:11222379}.
MUTAGEN 918 918 Y->F: Strongly impairs function, tyrosine
phosphorylation, subcellular location and
interaction with DOK1; when associated
with F-1021.
{ECO:0000269|PubMed:11031258,
ECO:0000269|PubMed:11222379,
ECO:0000269|PubMed:9099679}.
MUTAGEN 1021 1021 Y->F: Strongly impairs function, tyrosine
phosphorylation, subcellular location and
interaction with DOK1; when associated
with F-918. {ECO:0000269|PubMed:11031258,
ECO:0000269|PubMed:11222379,
ECO:0000269|PubMed:9099679}.
CONFLICT 43 43 Y -> C (in Ref. 2; AAB18937).
{ECO:0000305}.
CONFLICT 527 527 V -> A (in Ref. 3; AAC53023).
{ECO:0000305}.
CONFLICT 534 534 N -> I (in Ref. 3; AAC53023).
{ECO:0000305}.
CONFLICT 905 905 C -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 981 981 A -> T (in Ref. 2; AAB18937).
{ECO:0000305}.
SEQUENCE 1191 AA; 133542 MW; AF9F21326A59EC7A CRC64;
MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR NCVYTYRILP
NEDDKFTVQA SEGVPMRFFT KLDQLIDFYK KENMGLVTHL QYPVPLEEED AIDEAEEDTV
ESVMSPPELP PRNIPMSAGP SEAKDLPLAT ENPRAPEVTR LSLSETLFQR LQSMDTSGLP
EEHLKAIQDY LSTQLLLDSD FLKTGSSNLP HLKKLMSLLC KELHGEVIRT LPSLESLQRL
FDQQLSPGLR PRPQVPGEAS PITMVAKLSQ LTSLLSSIED KVKSLLHEGS ESTNRRSLIP
PVTFEVKSES LGIPQKMHLK VDVESGKLIV KKSKDGSEDK FYSHKKILQL IKSQKFLNKL
VILVETEKEK ILRKEYVFAD SKKREGFCQL LQQMKNKHSE QPEPDMITIF IGTWNMGNAP
PPKKITSWFL SKGQGKTRDD SADYIPHDIY VIGTQEDPLG EKEWLELLRH SLQEVTSMTF
KTVAIHTLWN IRIVVLAKPE HENRISHICT DNVKTGIANT LGNKGAVGVS FMFNGTSLGF
VNSHLTSGSE KKLRRNQNYM NILRFLALGD KKLSPFNITH RFTHLFWLGD LNYRVELPTW
EAEAIIQKIK QQQYSDLLAH DQLLLERKDQ KVFLHFEEEE ITFAPTYRFE RLTRDKYAYT
KQKATGMKYN LPSWCDRVLW KSYPLVHVVC QSYGSTSDIM TSDHSPVFAT FEAGVTSQFV
SKNGPGTVDS QGQIEFLACY ATLKTKSQTK FYLEFHSSCL ESFVKSQEGE NEEGSEGELV
VRFGETLPKL KPIISDPEYL LDQHILISIK SSDSDESYGE GCIALRLETT EAQHPIYTPL
THHGEMTGHF RGEIKLQTSQ GKMREKLYDF VKTERDESSG MKCLKNLTSH DPMRQWEPSG
RVPACGVSSL NEMINPNYIG MGPFGQPLHG KSTLSPDQQL TAWSYDQLPK DSSLGPGRGE
GPPTPPSQPP LSPKKFSSST ANRGPCPRVQ EARPGDLGKV EALLQEDLLL TKPEMFENPL
YGSVSSFPKL VPRKEQESPK MLRKEPPPCP DPGISSPSIV LPKAQEVESV KGTSKQAPVP
VLGPTPRIRS FTCSSSAEGR MTSGDKSQGK PKASASSQAP VPVKRPVKPS RSEMSQQTTP
IPAPRPPLPV KSPAVLQLQH SKGRDYRDNT ELPHHGKHRQ EEGLLGRTAM Q


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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
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. 10 ug
FP-0084 Signaling inositol polyphosphate phosphatase SHIP II. 10ug
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
INS INPP5K Gene inositol polyphosphate-5-phosphatase K
FP-0037 Signaling inositol polyphosphate 5 phosphatase SIP-145 10ug
I5P1_CANFA Dog ELISA Kit FOR Type I inositol-1,4,5-trisphosphate 5-phosphatase 96T


 

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