Sequence of SHIP1_MOUSE

phosphoinositide 5-phosphatase

Q9ES52

1191

133542

736834

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

736835

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

736836

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

736837

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

736838

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

736839

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

736840

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

736841

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

Genome Res.

14

2121-2127

2004

736842

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

736843

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

736844

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

736845

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

736846

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

736847

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

736848

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

736849

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

736850

Rameh L.E.,Tolias K.F.,Duckworth B.C.,Cantley L.C.

A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate.

Nature

390

192-196

1997

736851

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

736852

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

736853

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

736854

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

736855

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

736856

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

736857

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

736858

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

736859

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

736860

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

736861

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

736862

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

736863

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

736864

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

736865

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

736866

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

736867

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

736868

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

736869

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

736870

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

736871

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

736872

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

736873

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

736874

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

736875

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

736876

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

736877

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

736878

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

736879

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

736880

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

736881

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

736882

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

736883

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

736884

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