Sequence of SHIP2_MOUSE
EC Number:2.7.10.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Other sequences found for EC No. 2.7.10.1
EC Number:3.1.3.36
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
Other sequences found for EC No. 3.1.3.36
EC Number:3.1.3.86
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
Q6P549
Mus musculus
1257
138973
Reaction
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
Other sequences found for EC No. 3.1.3.86
General information:
Sequence
0 MASVCGTPSP GGALGSPAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE SVAGAFALCV
60 LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG LYAQPNQGLV CALLLPVEGE
120 REPDPPDDRD ASDVEDEKPP LPPRSGSTSI SAPVGPSSPL PTPETPTTPA AESTPNGLST
180 VSHEYLKGSY GLDLEAVRGG ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS
240 SPMVTRLLQQ QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP
300 SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ RDSQEDWTTF
360 THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR KREAFCQLLQ LMKNRHSKQD
420 EPDMISVFIG TWNMGSVPPP KNVTSWFTSK GLGKALDEVT VTIPHDIYVF GTQENSVGDR
480 EWLDLLRGGL KELTDLDYRP IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG
540 NKGAVGVSFM FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF
600 THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR FSEEEISFPP
660 TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE THIICNSYGC TDDIVTSDHS
720 PVFGTFEVGV TSQFISKKGL SKTSDQAYIE FESIEAIVKT ASRTKFFIEF YSTCLEEYKK
780 SFENDAQSSD NINFLKVQWS SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV
840 ALKSMIGSTA QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK
900 SKVPSVSRGS QEHRSGSRKP ASTETSCPLS KLFEEPEKPP PTGRPPAPPR AVPREEPLNP
960 RLKSEGTSEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL EPPSLARAPL PPATKNKVAI
1020 TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG
1080 RSGGEARGPP PPKAHPRPPL PPGTSPASTF LGEVASGDDR SCSVLQMAKT LSEVDYAPGP
1140 GRSALLPNPL ELQPPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM
1200 GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL DTLQLSK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
736929
Schurmans S.,Carrio R.,Behrends J.,Pouillon V.,Merino J.,Clement S.
The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse.
Genomics
62
260-271
1999
736930
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
736931
Yamabhai M.,Kay B.K.
Examining the specificity of Src homology 3 domain -- ligand interactions with alkaline phosphatase fusion proteins.
Anal. Biochem.
247
143-151
1997
736932
Le Drean E.,Vely F.,Olcese L.,Cambiaggi A.,Guia S.,Krystal G.,Gervois N.,Moretta A.,Jotereau F.,Vivier E.
Inhibition of antigen-induced T cell response and antibody-induced NK cell cytotoxicity by NKG2A: association of NKG2A with SHP-1 and SHP-2 protein-tyrosine phosphatases.
Eur. J. Immunol.
28
264-276
1998
736933
Muraille E.,Bruhns P.,Pesesse X.,Daeeron M.,Erneux C.
The SH2 domain containing inositol 5-phosphatase SHIP2 associates to the immunoreceptor tyrosine-based inhibition motif of Fc gammaRIIB in B cells under negative signaling.
Immunol. Lett.
72
7-15
2000
736934
Taylor V.,Wong M.,Brandts C.,Reilly L.,Dean N.M.,Cowsert L.M.,Moodie S.,Stokoe D.
5' phospholipid phosphatase SHIP-2 causes protein kinase B inactivation and cell cycle arrest in glioblastoma cells.
Mol. Cell. Biol.
20
6860-6871
2000
736935
Clement S.,Krause U.,Desmedt F.,Tanti J.-F.,Behrends J.,Pesesse X.,Sasaki T.,Penninger J.,Doherty M.,Malaisse W.,Dumont J.E.,Le Marchand-Brustel Y.,Erneux C.,Hue L.,Schurmans S.
The lipid phosphatase SHIP2 controls insulin sensitivity.
Nature
409
92-97
2001
736937
Hori H.,Sasaoka T.,Ishihara H.,Wada T.,Murakami S.,Ishiki M.,Kobayashi M.
Association of SH2-containing inositol phosphatase 2 with the insulin resistance of diabetic db/db mice.
Diabetes
51
2387-2394
2002
736938
Sasaoka T.,Wada T.,Fukui K.,Murakami S.,Ishihara H.,Suzuki R.,Tobe K.,Kadowaki T.,Kobayashi M.
SH2-containing inositol phosphatase 2 predominantly regulates Akt2, and not Akt1, phosphorylation at the plasma membrane in response to insulin in 3T3-L1 adipocytes.
J. Biol. Chem.
279
14835-14843
2004
736939
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
736940
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
736941
Wang Y.,Keogh R.J.,Hunter M.G.,Mitchell C.A.,Frey R.S.,Javaid K.,Malik A.B.,Schurmans S.,Tridandapani S.,Marsh C.B.
SHIP2 is recruited to the cell membrane upon macrophage colony-stimulating factor (M-CSF) stimulation and regulates M-CSF-induced signaling.
J. Immunol.
173
6820-6830
2004
736942
Sleeman M.W.,Wortley K.E.,Lai K.-M.V.,Gowen L.C.,Kintner J.,Kline W.O.,Garcia K.,Stitt T.N.,Yancopoulos G.D.,Wiegand S.J.,Glass D.J.
Absence of the lipid phosphatase SHIP2 confers resistance to dietary obesity.
Nat. Med.
11
199-205
2005
736943
Ai J.,Maturu A.,Johnson W.,Wang Y.,Marsh C.B.,Tridandapani S.
The inositol phosphatase SHIP-2 down-regulates FcgammaR-mediated phagocytosis in murine macrophages independently of SHIP-1.
Blood
107
813-820
2006
736944
Villen J.,Beausoleil S.A.,Gerber S.A.,Gygi S.P.
Large-scale phosphorylation analysis of mouse liver.
Proc. Natl. Acad. Sci. U.S.A.
104
1488-1493
2007
736945
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
736946
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
736947
Wang Y.,Shang Y.,Li J.,Chen W.,Li G.,Wan J.,Liu W.,Zhang M.
Specific Eph receptor-cytoplasmic effector signaling mediated by SAM-SAM domain interactions.
Elife
7
0-0
2018
