Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1

Preferred order of sections

Names and origin

Protein names

Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
EC=3.1.3.86

Alternative name(s):
Inositol polyphosphate-5-phosphatase of 145 kDa
Short name=SIP-145
SH2 domain-containing inositol 5'-phosphatase 1
Short name=SH2 domain-containing inositol phosphatase 1
Short name=SHIP-1
p150Ship

Gene names

Name:	Inpp5d
Synonyms:	7a33, Ship, Ship1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1191 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.11 Ref.13 Ref.23 Ref.24 Ref.25 Ref.26 Ref.32 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.45 Ref.48 Ref.51
Catalytic activity	1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate. Ref.1 Ref.2 Ref.19
Enzyme regulation	Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane.
Subunit structure	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. Ref.1 Ref.2 Ref.4 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33 Ref.36 Ref.37 Ref.40 Ref.43 Ref.44 Ref.45 Ref.46 Ref.49
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein. Note: Translocates to the plasma membrane 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) or CD16/FCGR3. Tyrosine phosphorylation may also participate in membrane localization. Ref.21 Ref.36 Ref.47 Isoform 5: Cell membrane; Peripheral membrane protein. Note: Constitutively present at the cell membrane. Ref.21 Ref.36 Ref.47
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. Ref.1 Ref.2 Ref.4 Ref.22
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. Ref.4 Ref.22
Induction	By activin/TGF-beta (at protein level). Regulated by the Smad pathway. Isoform 3 is expressed during myeloid development. Ref.38
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. Ref.14 The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. Ref.14
Post-translational modification	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. Ref.1 Ref.4 Ref.12 Ref.15 Ref.27 Ref.29 Ref.37
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. Ref.23 Ref.26 Ref.39
Sequence similarities	Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family. Contains 1 SH2 domain.

Ontologies

Keywords
Biological process	Apoptosis Immunity
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat SH2 domain SH3-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW determination of adult lifespan Inferred from mutant phenotype Ref.26. Source: MGI immunoglobulin mediated immune response Inferred from mutant phenotype PubMed 10704460. Source: MGI intracellular signal transduction Inferred from mutant phenotype PubMed 10704460. Source: MGI negative regulation of B cell proliferation Inferred from mutant phenotype PubMed 10704460. Source: MGI negative regulation of bone resorption Inferred from mutant phenotype Ref.39. Source: MGI negative regulation of immune response Inferred from mutant phenotype PubMed 10704460. Source: MGI negative regulation of interleukin-6 biosynthetic process Inferred from mutant phenotype Ref.39. Source: MGI negative regulation of monocyte differentiation Inferred from mutant phenotype Ref.26. Source: MGI negative regulation of neutrophil differentiation Inferred from mutant phenotype Ref.26. Source: MGI negative regulation of osteoclast differentiation Inferred from mutant phenotype Ref.39. Source: MGI negative regulation of signal transduction Inferred from mutant phenotype PubMed 10704460 Ref.39 Ref.26. Source: MGI phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro positive regulation of B cell differentiation Inferred from mutant phenotype PubMed 10704460 Ref.26. Source: MGI positive regulation of apoptotic process Inferred from mutant phenotype Ref.39. Source: MGI positive regulation of erythrocyte differentiation Inferred from mutant phenotype Ref.26. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	PTB domain binding Inferred from direct assay Ref.1. Source: MGI SH3 domain binding Inferred from direct assay Ref.2. Source: MGI hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW inositol-polyphosphate 5-phosphatase activity Inferred from direct assay Ref.2. Source: MGI phosphatidylinositol trisphosphate phosphatase activity Inferred from direct assay PubMed 8890215. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PIK3R1	P23727	2	EBI-1452545,EBI-520244	From a different organism.
Plcg2	Q8CIH5	3	EBI-300210,EBI-617954

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9ES52-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9ES52-2) The sequence of this isoform differs from the canonical sequence as follows: 120-120: Missing.

Isoform 3 (identifier: Q9ES52-3) Also known as: 135 kDa SHIP; The sequence of this isoform differs from the canonical sequence as follows: 920-980: Missing.

Isoform 4 (identifier: Q9ES52-4) Also known as: SHIPdelta; The sequence of this isoform differs from the canonical sequence as follows: 120-120: Missing. 920-960: GMGPFGQPLH...DSSLGPGRGE → VFIFHSQPRS...GPAADEARDV 961-1191: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 5 (identifier: Q9ES52-5) Also known as: s-SHIP; The sequence of this isoform differs from the canonical sequence as follows: 1-263: Missing.

Isoform 6 (identifier: Q9ES52-6) Also known as: s-SHIPD183; The sequence of this isoform differs from the canonical sequence as follows: 1-263: Missing. 920-980: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1191

1191

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1

PRO_0000302867

Regions

Domain

8 – 104

97

SH2

Region

1015 – 1029

15

Interaction with DAB2

Motif

127 – 132

6

SH3-binding 1

Motif

915 – 918

4

NPXY motif 1

Motif

970 – 975

6

SH3-binding 2

Motif

1018 – 1021

4

NPXY motif 2

Motif

1039 – 1050

12

SH3-binding 3

Compositional bias

962 – 1153

192

Pro-rich

Amino acid modifications

Modified residue

868

1

Phosphotyrosine Ref.50 Ref.52

Modified residue

918

1

Phosphotyrosine Ref.15

Modified residue

935

1

Phosphoserine Ref.50

Modified residue

945

1

Phosphotyrosine Ref.50

Modified residue

972

1

Phosphoserine Ref.52

Modified residue

1021

1

Phosphotyrosine Ref.15

Natural variations

Alternative sequence

1 – 263

263

Missing in isoform 5 and isoform 6.

VSP_027980

Alternative sequence

120

1

Missing in isoform 2 and isoform 4.

VSP_027981

Alternative sequence

920 – 980

61

Missing in isoform 3 and isoform 6.

VSP_027982

Alternative sequence

920 – 960

41

GMGPF…PGRGE → VFIFHSQPRSLPQGARGKTW GSGKGGSSAPGGPAADEARD V in isoform 4.

VSP_027983

Alternative sequence

961 – 1191

231

Missing in isoform 4.

VSP_027984

Experimental info

Mutagenesis

676

1

D → G: Loss of function. Ref.32

Mutagenesis

918

1

Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-1021. Ref.15 Ref.32 Ref.33

Mutagenesis

1021

1

Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-918. Ref.15 Ref.32 Ref.33

Sequence conflict

43

1

Y → C in AAB18937. Ref.2

Sequence conflict

527

1

V → A in AAC53023. Ref.3

Sequence conflict

534

1

N → I in AAC53023. Ref.3

Sequence conflict

905

1

C → E AA sequence Ref.2

Sequence conflict

981

1

A → T in AAB18937. Ref.2

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: AF9F21326A59EC7A Show »	FASTA	1,191	133,542
10 20 30 40 50 60 MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR NCVYTYRILP 70 80 90 100 110 120 NEDDKFTVQA SEGVPMRFFT KLDQLIDFYK KENMGLVTHL QYPVPLEEED AIDEAEEDTV 130 140 150 160 170 180 ESVMSPPELP PRNIPMSAGP SEAKDLPLAT ENPRAPEVTR LSLSETLFQR LQSMDTSGLP 190 200 210 220 230 240 EEHLKAIQDY LSTQLLLDSD FLKTGSSNLP HLKKLMSLLC KELHGEVIRT LPSLESLQRL 250 260 270 280 290 300 FDQQLSPGLR PRPQVPGEAS PITMVAKLSQ LTSLLSSIED KVKSLLHEGS ESTNRRSLIP 310 320 330 340 350 360 PVTFEVKSES LGIPQKMHLK VDVESGKLIV KKSKDGSEDK FYSHKKILQL IKSQKFLNKL 370 380 390 400 410 420 VILVETEKEK ILRKEYVFAD SKKREGFCQL LQQMKNKHSE QPEPDMITIF IGTWNMGNAP 430 440 450 460 470 480 PPKKITSWFL SKGQGKTRDD SADYIPHDIY VIGTQEDPLG EKEWLELLRH SLQEVTSMTF 490 500 510 520 530 540 KTVAIHTLWN IRIVVLAKPE HENRISHICT DNVKTGIANT LGNKGAVGVS FMFNGTSLGF 550 560 570 580 590 600 VNSHLTSGSE KKLRRNQNYM NILRFLALGD KKLSPFNITH RFTHLFWLGD LNYRVELPTW 610 620 630 640 650 660 EAEAIIQKIK QQQYSDLLAH DQLLLERKDQ KVFLHFEEEE ITFAPTYRFE RLTRDKYAYT 670 680 690 700 710 720 KQKATGMKYN LPSWCDRVLW KSYPLVHVVC QSYGSTSDIM TSDHSPVFAT FEAGVTSQFV 730 740 750 760 770 780 SKNGPGTVDS QGQIEFLACY ATLKTKSQTK FYLEFHSSCL ESFVKSQEGE NEEGSEGELV 790 800 810 820 830 840 VRFGETLPKL KPIISDPEYL LDQHILISIK SSDSDESYGE GCIALRLETT EAQHPIYTPL 850 860 870 880 890 900 THHGEMTGHF RGEIKLQTSQ GKMREKLYDF VKTERDESSG MKCLKNLTSH DPMRQWEPSG 910 920 930 940 950 960 RVPACGVSSL NEMINPNYIG MGPFGQPLHG KSTLSPDQQL TAWSYDQLPK DSSLGPGRGE 970 980 990 1000 1010 1020 GPPTPPSQPP LSPKKFSSST ANRGPCPRVQ EARPGDLGKV EALLQEDLLL TKPEMFENPL 1030 1040 1050 1060 1070 1080 YGSVSSFPKL VPRKEQESPK MLRKEPPPCP DPGISSPSIV LPKAQEVESV KGTSKQAPVP 1090 1100 1110 1120 1130 1140 VLGPTPRIRS FTCSSSAEGR MTSGDKSQGK PKASASSQAP VPVKRPVKPS RSEMSQQTTP 1150 1160 1170 1180 1190 IPAPRPPLPV KSPAVLQLQH SKGRDYRDNT ELPHHGKHRQ EEGLLGRTAM Q « Hide
Isoform 2 [UniParc]. Checksum: DF81F3046F33A07F Show »	FASTA	1,190	133,443
10 20 30 40 50 60 MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR NCVYTYRILP 70 80 90 100 110 120 NEDDKFTVQA SEGVPMRFFT KLDQLIDFYK KENMGLVTHL QYPVPLEEED AIDEAEEDTE 130 140 150 160 170 180 SVMSPPELPP RNIPMSAGPS EAKDLPLATE NPRAPEVTRL SLSETLFQRL QSMDTSGLPE 190 200 210 220 230 240 EHLKAIQDYL STQLLLDSDF LKTGSSNLPH LKKLMSLLCK ELHGEVIRTL PSLESLQRLF 250 260 270 280 290 300 DQQLSPGLRP RPQVPGEASP ITMVAKLSQL TSLLSSIEDK VKSLLHEGSE STNRRSLIPP 310 320 330 340 350 360 VTFEVKSESL GIPQKMHLKV DVESGKLIVK KSKDGSEDKF YSHKKILQLI KSQKFLNKLV 370 380 390 400 410 420 ILVETEKEKI LRKEYVFADS KKREGFCQLL QQMKNKHSEQ PEPDMITIFI GTWNMGNAPP 430 440 450 460 470 480 PKKITSWFLS KGQGKTRDDS ADYIPHDIYV IGTQEDPLGE KEWLELLRHS LQEVTSMTFK 490 500 510 520 530 540 TVAIHTLWNI RIVVLAKPEH ENRISHICTD NVKTGIANTL GNKGAVGVSF MFNGTSLGFV 550 560 570 580 590 600 NSHLTSGSEK KLRRNQNYMN ILRFLALGDK KLSPFNITHR FTHLFWLGDL NYRVELPTWE 610 620 630 640 650 660 AEAIIQKIKQ QQYSDLLAHD QLLLERKDQK VFLHFEEEEI TFAPTYRFER LTRDKYAYTK 670 680 690 700 710 720 QKATGMKYNL PSWCDRVLWK SYPLVHVVCQ SYGSTSDIMT SDHSPVFATF EAGVTSQFVS 730 740 750 760 770 780 KNGPGTVDSQ GQIEFLACYA TLKTKSQTKF YLEFHSSCLE SFVKSQEGEN EEGSEGELVV 790 800 810 820 830 840 RFGETLPKLK PIISDPEYLL DQHILISIKS SDSDESYGEG CIALRLETTE AQHPIYTPLT 850 860 870 880 890 900 HHGEMTGHFR GEIKLQTSQG KMREKLYDFV KTERDESSGM KCLKNLTSHD PMRQWEPSGR 910 920 930 940 950 960 VPACGVSSLN EMINPNYIGM GPFGQPLHGK STLSPDQQLT AWSYDQLPKD SSLGPGRGEG 970 980 990 1000 1010 1020 PPTPPSQPPL SPKKFSSSTA NRGPCPRVQE ARPGDLGKVE ALLQEDLLLT KPEMFENPLY 1030 1040 1050 1060 1070 1080 GSVSSFPKLV PRKEQESPKM LRKEPPPCPD PGISSPSIVL PKAQEVESVK GTSKQAPVPV 1090 1100 1110 1120 1130 1140 LGPTPRIRSF TCSSSAEGRM TSGDKSQGKP KASASSQAPV PVKRPVKPSR SEMSQQTTPI 1150 1160 1170 1180 1190 PAPRPPLPVK SPAVLQLQHS KGRDYRDNTE LPHHGKHRQE EGLLGRTAMQ « Hide
Isoform 3 (135 kDa SHIP) [UniParc]. Checksum: C3E2F1EB206034BF Show »	FASTA	1,130	127,199
10 20 30 40 50 60 MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR NCVYTYRILP 70 80 90 100 110 120 NEDDKFTVQA SEGVPMRFFT KLDQLIDFYK KENMGLVTHL QYPVPLEEED AIDEAEEDTV 130 140 150 160 170 180 ESVMSPPELP PRNIPMSAGP SEAKDLPLAT ENPRAPEVTR LSLSETLFQR LQSMDTSGLP 190 200 210 220 230 240 EEHLKAIQDY LSTQLLLDSD FLKTGSSNLP HLKKLMSLLC KELHGEVIRT LPSLESLQRL 250 260 270 280 290 300 FDQQLSPGLR PRPQVPGEAS PITMVAKLSQ LTSLLSSIED KVKSLLHEGS ESTNRRSLIP 310 320 330 340 350 360 PVTFEVKSES LGIPQKMHLK VDVESGKLIV KKSKDGSEDK FYSHKKILQL IKSQKFLNKL 370 380 390 400 410 420 VILVETEKEK ILRKEYVFAD SKKREGFCQL LQQMKNKHSE QPEPDMITIF IGTWNMGNAP 430 440 450 460 470 480 PPKKITSWFL SKGQGKTRDD SADYIPHDIY VIGTQEDPLG EKEWLELLRH SLQEVTSMTF 490 500 510 520 530 540 KTVAIHTLWN IRIVVLAKPE HENRISHICT DNVKTGIANT LGNKGAVGVS FMFNGTSLGF 550 560 570 580 590 600 VNSHLTSGSE KKLRRNQNYM NILRFLALGD KKLSPFNITH RFTHLFWLGD LNYRVELPTW 610 620 630 640 650 660 EAEAIIQKIK QQQYSDLLAH DQLLLERKDQ KVFLHFEEEE ITFAPTYRFE RLTRDKYAYT 670 680 690 700 710 720 KQKATGMKYN LPSWCDRVLW KSYPLVHVVC QSYGSTSDIM TSDHSPVFAT FEAGVTSQFV 730 740 750 760 770 780 SKNGPGTVDS QGQIEFLACY ATLKTKSQTK FYLEFHSSCL ESFVKSQEGE NEEGSEGELV 790 800 810 820 830 840 VRFGETLPKL KPIISDPEYL LDQHILISIK SSDSDESYGE GCIALRLETT EAQHPIYTPL 850 860 870 880 890 900 THHGEMTGHF RGEIKLQTSQ GKMREKLYDF VKTERDESSG MKCLKNLTSH DPMRQWEPSG 910 920 930 940 950 960 RVPACGVSSL NEMINPNYIA NRGPCPRVQE ARPGDLGKVE ALLQEDLLLT KPEMFENPLY 970 980 990 1000 1010 1020 GSVSSFPKLV PRKEQESPKM LRKEPPPCPD PGISSPSIVL PKAQEVESVK GTSKQAPVPV 1030 1040 1050 1060 1070 1080 LGPTPRIRSF TCSSSAEGRM TSGDKSQGKP KASASSQAPV PVKRPVKPSR SEMSQQTTPI 1090 1100 1110 1120 1130 PAPRPPLPVK SPAVLQLQHS KGRDYRDNTE LPHHGKHRQE EGLLGRTAMQ « Hide
Isoform 4 (SHIPdelta) [UniParc]. Checksum: B95D49476957345E Show »	FASTA	959	108,345
10 20 30 40 50 60 MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR NCVYTYRILP 70 80 90 100 110 120 NEDDKFTVQA SEGVPMRFFT KLDQLIDFYK KENMGLVTHL QYPVPLEEED AIDEAEEDTE 130 140 150 160 170 180 SVMSPPELPP RNIPMSAGPS EAKDLPLATE NPRAPEVTRL SLSETLFQRL QSMDTSGLPE 190 200 210 220 230 240 EHLKAIQDYL STQLLLDSDF LKTGSSNLPH LKKLMSLLCK ELHGEVIRTL PSLESLQRLF 250 260 270 280 290 300 DQQLSPGLRP RPQVPGEASP ITMVAKLSQL TSLLSSIEDK VKSLLHEGSE STNRRSLIPP 310 320 330 340 350 360 VTFEVKSESL GIPQKMHLKV DVESGKLIVK KSKDGSEDKF YSHKKILQLI KSQKFLNKLV 370 380 390 400 410 420 ILVETEKEKI LRKEYVFADS KKREGFCQLL QQMKNKHSEQ PEPDMITIFI GTWNMGNAPP 430 440 450 460 470 480 PKKITSWFLS KGQGKTRDDS ADYIPHDIYV IGTQEDPLGE KEWLELLRHS LQEVTSMTFK 490 500 510 520 530 540 TVAIHTLWNI RIVVLAKPEH ENRISHICTD NVKTGIANTL GNKGAVGVSF MFNGTSLGFV 550 560 570 580 590 600 NSHLTSGSEK KLRRNQNYMN ILRFLALGDK KLSPFNITHR FTHLFWLGDL NYRVELPTWE 610 620 630 640 650 660 AEAIIQKIKQ QQYSDLLAHD QLLLERKDQK VFLHFEEEEI TFAPTYRFER LTRDKYAYTK 670 680 690 700 710 720 QKATGMKYNL PSWCDRVLWK SYPLVHVVCQ SYGSTSDIMT SDHSPVFATF EAGVTSQFVS 730 740 750 760 770 780 KNGPGTVDSQ GQIEFLACYA TLKTKSQTKF YLEFHSSCLE SFVKSQEGEN EEGSEGELVV 790 800 810 820 830 840 RFGETLPKLK PIISDPEYLL DQHILISIKS SDSDESYGEG CIALRLETTE AQHPIYTPLT 850 860 870 880 890 900 HHGEMTGHFR GEIKLQTSQG KMREKLYDFV KTERDESSGM KCLKNLTSHD PMRQWEPSGR 910 920 930 940 950 VPACGVSSLN EMINPNYIVF IFHSQPRSLP QGARGKTWGS GKGGSSAPGG PAADEARDV « Hide
Isoform 5 (s-SHIP) [UniParc]. Checksum: 7390D08E57505B82 Show »	FASTA	928	104,101
10 20 30 40 50 60 MVAKLSQLTS LLSSIEDKVK SLLHEGSEST NRRSLIPPVT FEVKSESLGI PQKMHLKVDV 70 80 90 100 110 120 ESGKLIVKKS KDGSEDKFYS HKKILQLIKS QKFLNKLVIL VETEKEKILR KEYVFADSKK 130 140 150 160 170 180 REGFCQLLQQ MKNKHSEQPE PDMITIFIGT WNMGNAPPPK KITSWFLSKG QGKTRDDSAD 190 200 210 220 230 240 YIPHDIYVIG TQEDPLGEKE WLELLRHSLQ EVTSMTFKTV AIHTLWNIRI VVLAKPEHEN 250 260 270 280 290 300 RISHICTDNV KTGIANTLGN KGAVGVSFMF NGTSLGFVNS HLTSGSEKKL RRNQNYMNIL 310 320 330 340 350 360 RFLALGDKKL SPFNITHRFT HLFWLGDLNY RVELPTWEAE AIIQKIKQQQ YSDLLAHDQL 370 380 390 400 410 420 LLERKDQKVF LHFEEEEITF APTYRFERLT RDKYAYTKQK ATGMKYNLPS WCDRVLWKSY 430 440 450 460 470 480 PLVHVVCQSY GSTSDIMTSD HSPVFATFEA GVTSQFVSKN GPGTVDSQGQ IEFLACYATL 490 500 510 520 530 540 KTKSQTKFYL EFHSSCLESF VKSQEGENEE GSEGELVVRF GETLPKLKPI ISDPEYLLDQ 550 560 570 580 590 600 HILISIKSSD SDESYGEGCI ALRLETTEAQ HPIYTPLTHH GEMTGHFRGE IKLQTSQGKM 610 620 630 640 650 660 REKLYDFVKT ERDESSGMKC LKNLTSHDPM RQWEPSGRVP ACGVSSLNEM INPNYIGMGP 670 680 690 700 710 720 FGQPLHGKST LSPDQQLTAW SYDQLPKDSS LGPGRGEGPP TPPSQPPLSP KKFSSSTANR 730 740 750 760 770 780 GPCPRVQEAR PGDLGKVEAL LQEDLLLTKP EMFENPLYGS VSSFPKLVPR KEQESPKMLR 790 800 810 820 830 840 KEPPPCPDPG ISSPSIVLPK AQEVESVKGT SKQAPVPVLG PTPRIRSFTC SSSAEGRMTS 850 860 870 880 890 900 GDKSQGKPKA SASSQAPVPV KRPVKPSRSE MSQQTTPIPA PRPPLPVKSP AVLQLQHSKG 910 920 RDYRDNTELP HHGKHRQEEG LLGRTAMQ « Hide
Isoform 6 (s-SHIPD183) [UniParc]. Checksum: F848515DE853AD65 Show »	FASTA	867	97,758
10 20 30 40 50 60 MVAKLSQLTS LLSSIEDKVK SLLHEGSEST NRRSLIPPVT FEVKSESLGI PQKMHLKVDV 70 80 90 100 110 120 ESGKLIVKKS KDGSEDKFYS HKKILQLIKS QKFLNKLVIL VETEKEKILR KEYVFADSKK 130 140 150 160 170 180 REGFCQLLQQ MKNKHSEQPE PDMITIFIGT WNMGNAPPPK KITSWFLSKG QGKTRDDSAD 190 200 210 220 230 240 YIPHDIYVIG TQEDPLGEKE WLELLRHSLQ EVTSMTFKTV AIHTLWNIRI VVLAKPEHEN 250 260 270 280 290 300 RISHICTDNV KTGIANTLGN KGAVGVSFMF NGTSLGFVNS HLTSGSEKKL RRNQNYMNIL 310 320 330 340 350 360 RFLALGDKKL SPFNITHRFT HLFWLGDLNY RVELPTWEAE AIIQKIKQQQ YSDLLAHDQL 370 380 390 400 410 420 LLERKDQKVF LHFEEEEITF APTYRFERLT RDKYAYTKQK ATGMKYNLPS WCDRVLWKSY 430 440 450 460 470 480 PLVHVVCQSY GSTSDIMTSD HSPVFATFEA GVTSQFVSKN GPGTVDSQGQ IEFLACYATL 490 500 510 520 530 540 KTKSQTKFYL EFHSSCLESF VKSQEGENEE GSEGELVVRF GETLPKLKPI ISDPEYLLDQ 550 560 570 580 590 600 HILISIKSSD SDESYGEGCI ALRLETTEAQ HPIYTPLTHH GEMTGHFRGE IKLQTSQGKM 610 620 630 640 650 660 REKLYDFVKT ERDESSGMKC LKNLTSHDPM RQWEPSGRVP ACGVSSLNEM INPNYIANRG 670 680 690 700 710 720 PCPRVQEARP GDLGKVEALL QEDLLLTKPE MFENPLYGSV SSFPKLVPRK EQESPKMLRK 730 740 750 760 770 780 EPPPCPDPGI SSPSIVLPKA QEVESVKGTS KQAPVPVLGP TPRIRSFTCS SSAEGRMTSG 790 800 810 820 830 840 DKSQGKPKAS ASSQAPVPVK RPVKPSRSEM SQQTTPIPAP RPPLPVKSPA VLQLQHSKGR 850 860 DYRDNTELPH HGKHRQEEGL LGRTAMQ « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity." Lioubin M.N., Algate P.A., Tsai S., Carlberg K., Aebersold A., Rohrschneider L.R. Genes Dev. 10:1084-1095(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 2-9 AND 1163-1173, FUNCTION, ENZYME ACTIVITY, PHOSPHORYLATION, TISSUE SPECIFICITY, INTERACTION WITH SHC1. Strain: DBA/2.
[2]	"The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase." Damen J.E., Liu L., Rosten P., Humphries R.K., Jefferson A.B., Majerus P.W., Krystal G. Proc. Natl. Acad. Sci. U.S.A. 93:1689-1693(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 902-916, ENZYME ACTIVITY, TISSUE SPECIFICITY, INTERACTION WITH GRB2 AND SHC1.
[3]	"Molecular cloning and chromosomal localization in human and mouse of the SH2-containing inositol phosphatase, INPP5D (SHIP)." Liu Q., Dumont D.J. Genomics 39:109-112(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"A novel spliced form of SH2-containing inositol phosphatase is expressed during myeloid development." Lucas D.M., Rohrschneider L.R. Blood 93:1922-1933(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PHOSPHORYLATION, INTERACTION WITH SHC1 AND GRB2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: BALB/c.
[5]	"Cloning of the genomic locus of mouse SH2 containing inositol 5-phosphatase (SHIP) and a novel 110-kDa splice isoform, SHIPdelta." Wolf I., Lucas D.M., Algate P.A., Rohrschneider L.R. Genomics 69:104-112(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 4). Strain: 129/Sv.
[6]	"Embryonic and hematopoietic stem cells express a novel SH2-containing inositol 5'-phosphatase isoform that partners with the Grb2 adapter protein." Tu Z., Ninos J.M., Ma Z., Wang J.-W., Lemos M.P., Desponts C., Ghansah T., Howson J.M., Kerr W.G. Blood 98:2028-2038(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[7]	"The transcriptional landscape of the mammalian genome." 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. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Spleen.
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Thyroid.
[9]	"Analysis of lipopolysaccharide-response genes in B-lineage cells demonstrates that they can have differentiation stage-restricted expression and contain SH2 domains." Kerr W.G., Heller M., Herzenberg L.A. Proc. Natl. Acad. Sci. U.S.A. 93:3947-3952(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-106.
[10]	"Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2." 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. Curr. Biol. 6:438-445(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[11]	"Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB." Ono M., Bolland S., Tempst P., Ravetch J.V. Nature 383:263-266(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP." Chacko G.W., Tridandapani S., Damen J.E., Liu L., Krystal G., Coggeshall K.M. J. Immunol. 157:2234-2238(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[13]	"Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling." Ono M., Okada H., Bolland S., Yanagi S., Kurosaki T., Ravetch J.V. Cell 90:293-301(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"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." Liu L., Damen J.E., Hughes M.R., Babic I., Jirik F.R., Krystal G. J. Biol. Chem. 272:8983-8988(1997) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN SH2, INTERACTION WITH SHC1.
[15]	"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." Lamkin T.D., Walk S.F., Liu L., Damen J.E., Krystal G., Ravichandran K.S. J. Biol. Chem. 272:10396-10401(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-918 AND TYR-1021, INTERACTION WITH SHC1, MUTAGENESIS OF TYR-918 AND TYR-1021.
[16]	"Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2." Liu L., Damen J.E., Ware M.D., Krystal G. J. Biol. Chem. 272:10998-11001(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPN11.
[17]	"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2." Morris S.M., Cooper J.A. Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAB2.
[18]	"An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E-mediated immediate hypersensitivity reactions." Hitomi K., Tahara-Hanaoka S., Someya S., Fujiki A., Tada H., Sugiyama T., Shibayama S., Shibuya K., Shibuya A. Nat. Immunol. 11:601-607(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MILR1.
[19]	"Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets." Giuriato S., Payrastre B., Drayer A.L., Plantavid M., Woscholski R., Parker P., Erneux C., Chap H. J. Biol. Chem. 272:26857-26863(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY.
[20]	"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." Sattler M., Salgia R., Shrikhande G., Verma S., Choi J.-L., Rohrschneider L.R., Griffin J.D. Oncogene 15:2379-2384(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPN11.
[21]	"Multiple forms of the SH2-containing inositol phosphatase, SHIP, are generated by C-terminal truncation." Damen J.E., Liu L., Ware M.D., Ermolaeva M., Majerus P.W., Krystal G. Blood 92:1199-1205(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[22]	"The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hematopoiesis and spermatogenesis." Liu Q., Shalaby F., Jones J., Bouchard D., Dumont D.J. Blood 91:2753-2759(1998) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[23]	"Targeted disruption of SHIP leads to Steel factor-induced degranulation of mast cells." Huber M., Helgason C.D., Scheid M.P., Duronio V., Humphries R.K., Krystal G. EMBO J. 17:7311-7319(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[24]	"The inositol polyphosphate 5-phosphatase ship is a crucial negative regulator of B cell antigen receptor signaling." 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. J. Exp. Med. 188:1333-1342(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[25]	"The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation." Huber M., Helgason C.D., Damen J.E., Liu L., Humphries R.K., Krystal G. Proc. Natl. Acad. Sci. U.S.A. 95:11330-11335(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[26]	"Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span." Helgason C.D., Damen J.E., Rosten P., Grewal R., Sorensen P., Chappel S.M., Borowski A., Jirik F., Krystal G., Humphries R.K. Genes Dev. 12:1610-1620(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[27]	"Role of SHIP in FcgammaRIIb-mediated inhibition of Ras activation in B cells." Tridandapani S., Phee H., Shivakumar L., Kelley T.W., Coggeshall K.M. Mol. Immunol. 35:1135-1146(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHC1 AND FCGR2B, PHOSPHORYLATION.
[28]	"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." Giuriato S., Bodin S., Erneux C., Woscholski R., Plantavid M., Chap H., Payrastre B. Biochem. J. 348:107-112(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRC.
[29]	"The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor." Mason J.M., Beattie B.K., Liu Q., Dumont D.J., Barber D.L. J. Biol. Chem. 275:4398-4406(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPOR, PHOSPHORYLATION.
[30]	"Molecular basis of the recruitment of the SH2 domain-containing inositol 5-phosphatases SHIP1 and SHIP2 by fcgamma RIIB." Bruhns P., Vely F., Malbec O., Fridman W.H., Vivier E., Daeeron M. J. Biol. Chem. 275:37357-37364(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCGR2B.
[31]	"Essential role for the C-terminal noncatalytic region of SHIP in FcgammaRIIB1-mediated inhibitory signaling." Aman M.J., Walk S.F., March M.E., Su H.-P., Carver D.J., Ravichandran K.S. Mol. Cell. Biol. 20:3576-3589(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCGR2B.
[32]	"SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation." Damen J.E., Ware M.D., Kalesnikoff J., Hughes M.R., Krystal G. Blood 97:1343-1351(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-676; TYR-918 AND TYR-1021.
[33]	"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." Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R., Griffin J.D. J. Biol. Chem. 276:2451-2458(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DOK1 AND CRKL, MUTAGENESIS OF TYR-918 AND TYR-1021.
[34]	"Src homology 2 domain-containing inositol 5-phosphatase 1 mediates cell cycle arrest by FcgammaRIIB." Malbec O., Schmitt C., Bruhns P., Krystal G., Fridman W.H., Daeeron M. J. Biol. Chem. 276:30381-30391(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[35]	"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)." Cox D., Dale B.M., Kashiwada M., Helgason C.D., Greenberg S. J. Exp. Med. 193:61-71(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[36]	"SH2-containing inositol phosphatase (SHIP-1) transiently translocates to raft domains and modulates CD16-mediated cytotoxicity in human NK cells." Galandrini R., Tassi I., Mattia G., Lenti L., Piccoli M., Frati L., Santoni A. Blood 100:4581-4589(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FCGR3.
[37]	"Src homology 2 domain-containing inositol polyphosphate phosphatase regulates NF-kappa B-mediated gene transcription by phagocytic Fc gamma Rs in human myeloid cells." Tridandapani S., Wang Y., Marsh C.B., Anderson C.L. J. Immunol. 169:4370-4378(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FCGR2A, PHOSPHORYLATION.
[38]	"Activin/TGF-beta induce apoptosis through Smad-dependent expression of the lipid phosphatase SHIP." Valderrama-Carvajal H., Cocolakis E., Lacerte A., Lee E.-H., Krystal G., Ali S., Lebrun J.-J. Nat. Cell Biol. 4:963-969(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[39]	"SHIP-deficient mice are severely osteoporotic due to increased numbers of hyper-resorptive osteoclasts." 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. Nat. Med. 8:943-949(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[40]	"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." Mancini A., Koch A., Wilms R., Tamura T. Oncogene 21:1477-1484(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MET.
[41]	"The inositol 5'-phosphatase SHIP-1 and the Src kinase Lyn negatively regulate macrophage colony-stimulating factor-induced Akt activity." Baran C.P., Tridandapani S., Helgason C.D., Humphries R.K., Krystal G., Marsh C.B. J. Biol. Chem. 278:38628-38636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[42]	"SHIP1 and Lyn kinase negatively regulate integrin alpha IIb beta 3 signaling in platelets." Maxwell M.J., Yuan Y., Anderson K.E., Hibbs M.L., Salem H.H., Jackson S.P. J. Biol. Chem. 279:32196-32204(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[43]	"Two distinct tyrosine-based motifs enable the inhibitory receptor FcgammaRIIB to cooperatively recruit the inositol phosphatases SHIP1/2 and the adapters Grb2/Grap." Isnardi I., Lesourne R., Bruhns P., Fridman W.H., Cambier J.C., Daeeron M. J. Biol. Chem. 279:51931-51938(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCGR2B.
[44]	"SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase." Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A. J. Biol. Chem. 279:55089-55096(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TEC.
[45]	"Inhibition of the Jun N-terminal protein kinase pathway by SHIP-1, a lipid phosphatase that interacts with the adaptor molecule Dok-3." Robson J.D., Davidson D., Veillette A. Mol. Cell. Biol. 24:2332-2343(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DOK3.
[46]	"Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity." Song M., Kim M.J., Ha S., Park J.B., Ryu S.H., Suh P.-G. Exp. Mol. Med. 37:161-168(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLCG1.
[47]	"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." Isnardi I., Bruhns P., Bismuth G., Fridman W.H., Daeeron M. Immunol. Lett. 104:156-165(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[48]	"SHIP1 negatively regulates proliferation of osteoclast precursors via Akt-dependent alterations in D-type cyclins and p27." Zhou P., Kitaura H., Teitelbaum S.L., Krystal G., Ross F.P., Takeshita S. J. Immunol. 177:8777-8784(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[49]	"s-SHIP associates with receptor complexes essential for pluripotent stem cell growth and survival." Desponts C., Ninos J.M., Kerr W.G. Stem Cells Dev. 15:641-646(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IL6ST.
[50]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-868; SER-935 AND TYR-945, MASS SPECTROMETRY. Tissue: Mast cell.
[51]	"Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1." 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. Nat. Cell Biol. 9:36-44(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[52]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-868 AND SER-972, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U51742 mRNA. Translation: AAC52606.1. U39203 mRNA. Translation: AAB18937.1. U52044 mRNA. Translation: AAC53023.1. AF125996 mRNA. Translation: AAD37118.1. AF235502 AF235501 Genomic DNA. Translation: AAG23922.1. AF228679 mRNA. Translation: AAF69143.1. AF184912 mRNA. Translation: AAF25823.1. AF184913 mRNA. Translation: AAF25824.1. AK143560 mRNA. Translation: BAE25436.1. BC108328 mRNA. Translation: AAI08329.1.
IPI	IPI00120516. IPI00124504. IPI00856529. IPI00857008. IPI00857200. IPI00857938.
PIR	JC6118.
RefSeq	NP_001103662.1. NM_001110192.1. NP_001103663.1. NM_001110193.1. NP_034696.2. NM_010566.2.
UniGene	Mm.15105.
3D structure databases
HSSP	HSSP built from PDB template 1QAD based on UniProtKB P23727.
ProteinModelPortal	Q9ES52.
SMR	Q9ES52. Positions 3-152, 405-717.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ES52. 9 interactions.
MINT	MINT-205819.
PTM databases
PhosphoSite	Q9ES52.
Proteomic databases
PaxDb	Q9ES52.
PRIDE	Q9ES52.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000042275; ENSMUSP00000044647; ENSMUSG00000026288. ENSMUST00000072999; ENSMUSP00000072763; ENSMUSG00000026288. ENSMUST00000167032; ENSMUSP00000126569; ENSMUSG00000026288. ENSMUST00000168783; ENSMUSP00000131244; ENSMUSG00000026288. ENSMUST00000169754; ENSMUSP00000127941; ENSMUSG00000026288. ENSMUST00000170300; ENSMUSP00000132384; ENSMUSG00000026288.
GeneID	16331.
KEGG	mmu:16331.
UCSC	uc007bxc.2. mouse. uc007bxd.2. mouse. uc007bxf.2. mouse. uc007bxg.2. mouse. uc007bxh.2. mouse.
Organism-specific databases
CTD	3635.
MGI	MGI:107357. Inpp5d.
Phylogenomic databases
eggNOG	COG5411.
GeneTree	ENSGT00700000104142.
HOVERGEN	HBG106726.
InParanoid	Q9ES52.
KO	K03084.
OMA	TREKYAY.
OrthoDB	EOG4M397X.
Gene expression databases
ArrayExpress	Q9ES52.
Bgee	Q9ES52.
CleanEx	MM_INPP5D.
Genevestigator	Q9ES52.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. IPR000980. SH2. [Graphical view]
Pfam	PF03372. Exo_endo_phos. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN.
SMART	SM00128. IPPc. 1 hit. SM00252. SH2. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
PROSITE	PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	289418.
SOURCE	Search...

Entry information

Entry name

SHIP1_MOUSE

Accession

Primary (citable) accession number: Q9ES52
Secondary accession number(s): Q3UPF9

Q9WUC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents