Reviewed, UniProtKB/Swiss-Prot Q9ES52 (SHIP1_MOUSE)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1
    EC=3.1.3.n1
Alternative name(s):
    SH2 domain-containing inositol-5'-phosphatase 1
      Short name=SH2 domain-containing inositol phosphatase 1
      Short name=SHIP-1
    Inositol polyphosphate-5-phosphatase of 145 kDa
      Short name=SIP-145
    p150Ship

Gene names

Name:	Inpp5d
Synonyms:	7a33, Ship, Ship1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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.21 Ref.22 Ref.23 Ref.24 Ref.30 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.43 Ref.46 Ref.49
Catalytic activity	Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 3,4-bisphosphate + phosphate. Ref.1 Ref.2 Ref.17
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. Isoform 5 interacts with IL6ST/gp130. Ref.1 Ref.35 Ref.38 Ref.43 Ref.2 Ref.4 Ref.14 Ref.15 Ref.16 Ref.18 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.34 Ref.41 Ref.42 Ref.44 Ref.47
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 to membrane localization. Ref.34 Ref.19 Ref.45 Isoform 5: Cell membrane; Peripheral membrane protein. Note: Constitutively present at the cell membrane. Ref.34 Ref.19 Ref.45
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 co-expressed with other isoforms in hematopoietic stem cells, and disapears with differentiation. Ref.1 Ref.2 Ref.4 Ref.20
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.20
Induction	By activin/TGF-beta (at protein level). Regulated by the Smad pathway. Isoform 3 is expressed during myeloid development. Ref.36
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.35 Ref.4 Ref.15 Ref.25 Ref.27 Ref.12 Ref.48 Ref.50
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.21 Ref.24 Ref.37
Sequence similarities	Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family. Contains 1 SH2 domain.

Ontologies

Keywords
Biological process	Apoptosis Immune response
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat SH2 domain SH3-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW determination of adult lifespan Ref.24 Inferred from mutant phenotype. Source: MGI immunoglobulin mediated immune response Inferred from mutant phenotype. Source: MGI intracellular signaling cascade Inferred from mutant phenotype. Source: MGI negative regulation of B cell proliferation Inferred from mutant phenotype. Source: MGI negative regulation of bone resorption Ref.37 Inferred from mutant phenotype. Source: MGI negative regulation of immune response Inferred from mutant phenotype. Source: MGI negative regulation of interleukin-6 biosynthetic process Ref.37 Inferred from mutant phenotype. Source: MGI negative regulation of monocyte differentiation Ref.24 Inferred from mutant phenotype. Source: MGI negative regulation of neutrophil differentiation Ref.24 Inferred from mutant phenotype. Source: MGI negative regulation of osteoclast differentiation Ref.37 Inferred from mutant phenotype. Source: MGI negative regulation of signal transduction Ref.24 Ref.37 Inferred from mutant phenotype. Source: MGI positive regulation of B cell differentiation Ref.24 Inferred from mutant phenotype. Source: MGI positive regulation of apoptosis Ref.37 Inferred from mutant phenotype. Source: MGI positive regulation of erythrocyte differentiation Ref.24 Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	PTB domain binding Ref.1 Inferred from direct assay. Source: MGI SH3 domain binding Ref.2 Inferred from direct assay. Source: MGI inositol-polyphosphate 5-phosphatase activity Ref.2 Inferred from direct assay. Source: MGI phosphatidylinositol trisphosphate phosphatase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cd22	P35329	1	EBI-300210,EBI-300059
Grb2	Q60631	1	EBI-1452545,EBI-1688
Grb2	Q60631	1	EBI-1452551,EBI-1688
PIK3R1	P23727	1	EBI-1452545,EBI-520244	From a different organism.
PIK3R1	P23727	1	EBI-1452551,EBI-520244	From a different organism.
Plcg1	Q62077	1	EBI-300210,EBI-300133
Shc1	P98083	1	EBI-1452545,EBI-300201
Shc1	P98083	1	EBI-1452551,EBI-300201

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.

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.

Note: Constitutively present at the cell membrane. Ref.34 Ref.19 Ref.45

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
	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	374	1	N6-acetyllysine By similarity
	Modified residue	868	1	Phosphotyrosine Ref.48 Ref.50
	Modified residue	918	1	Phosphotyrosine Ref.15
	Modified residue	935	1	Phosphoserine Ref.48
	Modified residue	945	1	Phosphotyrosine Ref.48
	Modified residue	972	1	Phosphoserine Ref.50
	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.30
	Mutagenesis	918	1	Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-1021. Ref.30 Ref.15 Ref.31
	Mutagenesis	1021	1	Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-918. Ref.30 Ref.15 Ref.31
	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	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
	Isoform 2. Checksum: DF81F3046F33A07F	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
	Isoform 3 (135 kDa SHIP). Checksum: C3E2F1EB206034BF	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
	Isoform 4 (SHIPdelta). Checksum: B95D49476957345E	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
	Isoform 5 (s-SHIP). Checksum: 7390D08E57505B82	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
	Isoform 6 (s-SHIPD183). Checksum: F848515DE853AD65	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

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: 8654924] [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: 8643691] [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: 9027494] [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: 10068665] [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: 11013080] [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: 11567986] [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. , 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. Science 309:1559-1563(2005) [PubMed: 16141072] [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: 15489334] [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: 8632995] [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: 8723348] [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: 8805703] [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: 8805618] [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: 9244303] [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: 9083021] [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: 9099679] [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: 9110989] [Abstract] Cited for: INTERACTION WITH PTPN11.
[17]	"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: 9341117] [Abstract] Cited for: ENZYME ACTIVITY.
[18]	"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: 9393882] [Abstract] Cited for: INTERACTION WITH PTPN11.
[19]	"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: 9694708] [Abstract] Cited for: SUBCELLULAR LOCATION.
[20]	"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: 9531585] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[21]	"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: 9857188] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[22]	"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: 9763612] [Abstract] Cited for: FUNCTION.
[23]	"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: 9736736] [Abstract] Cited for: FUNCTION.
[24]	"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: 9620849] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[25]	"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: 10395202] [Abstract] Cited for: INTERACTION WITH SHC1 AND FCGR2B, PHOSPHORYLATION.
[26]	"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: 10794720] [Abstract] Cited for: INTERACTION WITH SRC.
[27]	"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: 10660611] [Abstract] Cited for: INTERACTION WITH EPOR, PHOSPHORYLATION.
[28]	"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: 11016922] [Abstract] Cited for: INTERACTION WITH FCGR2B.
[29]	"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: 10779347] [Abstract] Cited for: INTERACTION WITH FCGR2B.
[30]	"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: 11222379] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-676; TYR-918 AND TYR-1021.
[31]	"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: 11031258] [Abstract] Cited for: INTERACTION WITH DOK1 AND CRKL, MUTAGENESIS OF TYR-918 AND TYR-1021.
[32]	"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: 11359765] [Abstract] Cited for: FUNCTION.
[33]	"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: 11136821] [Abstract] Cited for: FUNCTION.
[34]	"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: 12393695] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FCGR3.
[35]	"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: 12370370] [Abstract] Cited for: FUNCTION, INTERACTION WITH FCGR2A, PHOSPHORYLATION.
[36]	"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: 12447389] [Abstract] Cited for: FUNCTION, INDUCTION.
[37]	"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: 12161749] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[38]	"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: 11896575] [Abstract] Cited for: FUNCTION, INTERACTION WITH MET.
[39]	"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: 12882960] [Abstract] Cited for: FUNCTION.
[40]	"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: 15166241] [Abstract] Cited for: FUNCTION.
[41]	"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: 15456754] [Abstract] Cited for: INTERACTION WITH FCGR2B.
[42]	"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: 15492005] [Abstract] Cited for: INTERACTION WITH TEC.
[43]	"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: 14993273] [Abstract] Cited for: FUNCTION, INTERACTION WITH DOK3.
[44]	"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: 16000869] [Abstract] Cited for: INTERACTION WITH PLCG1.
[45]	"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: 16406061] [Abstract] Cited for: SUBCELLULAR LOCATION.
[46]	"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: 17142780] [Abstract] Cited for: FUNCTION.
[47]	"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: 17105399] [Abstract] Cited for: INTERACTION WITH IL6ST.
[48]	"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: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-868; SER-935 AND TYR-945, MASS SPECTROMETRY. Tissue: Mast cell.
[49]	"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: 17173042] [Abstract] Cited for: FUNCTION.
[50]	"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: 19144319] [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 , AF235496, AF235498, AF235499, AF235500, 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. NP_001103663.1. NP_034696.2.
UniGene	Mm.15105
3D structure databases
HSSP	HSSP built from PDB template 1QAD based on UniProtKB P23727.
SMR	Q9ES52. Positions 3-114, 390-716.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ES52. 10 interactions.
PTM databases
PhosphoSite	Q9ES52.
Proteomic databases
PRIDE	Q9ES52.
Genome annotation databases
Ensembl	ENSMUST00000042275; ENSMUSP00000044647; ENSMUSG00000026288; Mus musculus. [Genome view] ENSMUST00000072999; ENSMUSP00000072763; ENSMUSG00000026288; Mus musculus. [Genome view]
GeneID	16331.
KEGG	mmu:16331.
NMPDR	fig|10090.3.peg.725.
UCSC	uc007bxf.1. mouse.
Organism-specific databases
CTD	16331.
MGI	MGI:107357. Inpp5d.
Phylogenomic databases
HOVERGEN	Q9ES52.
InParanoid	Q9ES52.
OMA	PRKEQES.
PhylomeDB	Q9ES52.
Gene expression databases
ArrayExpress	Q9ES52.
Bgee	Q9ES52.
CleanEx	MM_INPP5D.
Genevestigator	Q9ES52.
Family and domain databases
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]
PROSITE	PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	289418.
SOURCE	Search...

Entry information

Entry name

SHIP1_MOUSE

Accession

Primary (citable) accession number: Q9ES52
Secondary accession number(s): Q3UPF9 , Q4U212, Q61034, Q61173, Q61181, Q9JKR7, Q9JLF9, Q9JLG0, Q9QVN8, Q9WUC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	February 9, 2010
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)