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Q9ES52

- SHIP1_MOUSE

UniProt

Q9ES52 - SHIP1_MOUSE

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Protein
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
Gene
Inpp5d, 7a33, Ship, Ship1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 InsP6.19 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate.3 Publications

Enzyme regulationi

Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane.

GO - Molecular functioni

  1. PTB domain binding Source: MGI
  2. SH3 domain binding Source: MGI
  3. inositol-polyphosphate 5-phosphatase activity Source: MGI
  4. phosphatidylinositol trisphosphate phosphatase activity Source: MGI
  5. protein binding Source: IntAct

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. determination of adult lifespan Source: MGI
  3. immunoglobulin mediated immune response Source: MGI
  4. intracellular signal transduction Source: MGI
  5. negative regulation of B cell activation Source: MGI
  6. negative regulation of B cell proliferation Source: MGI
  7. negative regulation of bone resorption Source: MGI
  8. negative regulation of cell proliferation Source: MGI
  9. negative regulation of granulocyte differentiation Source: MGI
  10. negative regulation of immune response Source: MGI
  11. negative regulation of interleukin-6 biosynthetic process Source: MGI
  12. negative regulation of monocyte differentiation Source: MGI
  13. negative regulation of neutrophil differentiation Source: MGI
  14. negative regulation of osteoclast differentiation Source: MGI
  15. negative regulation of signal transduction Source: MGI
  16. phosphatidylinositol dephosphorylation Source: InterPro
  17. positive regulation of B cell differentiation Source: MGI
  18. positive regulation of apoptotic process Source: MGI
  19. positive regulation of erythrocyte differentiation Source: MGI
  20. positive regulation of lymphocyte differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Immunity

Enzyme and pathway databases

ReactomeiREACT_196473. Synthesis of IP3 and IP4 in the cytosol.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_210793. Interleukin receptor SHC signaling.
REACT_225145. Downstream TCR signaling.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Inpp5d
Synonyms:7a33, Ship, Ship1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:107357. Inpp5d.

Subcellular locationi

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.3 Publications
Isoform 5 : Cell membrane; Peripheral membrane protein
Note: Constitutively present at the cell membrane.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi676 – 6761D → G: Loss of function. 1 Publication
Mutagenesisi918 – 9181Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-1021. 3 Publications
Mutagenesisi1021 – 10211Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-918. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11911191Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
PRO_0000302867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei918 – 9181Phosphotyrosine1 Publication
Modified residuei935 – 9351Phosphoserine1 Publication
Modified residuei945 – 9451Phosphotyrosine1 Publication
Modified residuei1021 – 10211Phosphotyrosine1 Publication

Post-translational modificationi

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.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ES52.
PaxDbiQ9ES52.
PRIDEiQ9ES52.

PTM databases

PhosphoSiteiQ9ES52.

Expressioni

Tissue specificityi

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.4 Publications

Developmental stagei

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.2 Publications

Inductioni

By activin/TGF-beta (at protein level). Regulated by the Smad pathway. Isoform 3 is expressed during myeloid development.1 Publication

Gene expression databases

ArrayExpressiQ9ES52.
BgeeiQ9ES52.
CleanExiMM_INPP5D.
GenevestigatoriQ9ES52.

Interactioni

Subunit structurei

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.23 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIK3R1P237272EBI-1452545,EBI-520244From a different organism.
Plcg2Q8CIH53EBI-300210,EBI-617954

Protein-protein interaction databases

BioGridi200769. 24 interactions.
IntActiQ9ES52. 11 interactions.
MINTiMINT-205819.

Structurei

3D structure databases

ProteinModelPortaliQ9ES52.
SMRiQ9ES52. Positions 3-152, 405-717.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 10497SH2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1015 – 102915Interaction with DAB2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi127 – 1326SH3-binding 1
Motifi915 – 9184NPXY motif 1
Motifi970 – 9756SH3-binding 2
Motifi1018 – 10214NPXY motif 2
Motifi1039 – 105012SH3-binding 3
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi962 – 1153192Pro-rich
Add
BLAST

Domaini

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.1 Publication
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.1 Publication

Sequence similaritiesi

Contains 1 SH2 domain.

Keywords - Domaini

Repeat, SH2 domain, SH3-binding

Phylogenomic databases

eggNOGiCOG5411.
GeneTreeiENSGT00750000117420.
HOVERGENiHBG106726.
InParanoidiQ9ES52.
KOiK03084.
OMAiRKEPPPC.
OrthoDBiEOG75F4CD.
PhylomeDBiQ9ES52.
TreeFamiTF323475.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9ES52-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR     50
NCVYTYRILP NEDDKFTVQA SEGVPMRFFT KLDQLIDFYK KENMGLVTHL 100
QYPVPLEEED AIDEAEEDTV ESVMSPPELP PRNIPMSAGP SEAKDLPLAT 150
ENPRAPEVTR LSLSETLFQR LQSMDTSGLP EEHLKAIQDY LSTQLLLDSD 200
FLKTGSSNLP HLKKLMSLLC KELHGEVIRT LPSLESLQRL FDQQLSPGLR 250
PRPQVPGEAS PITMVAKLSQ LTSLLSSIED KVKSLLHEGS ESTNRRSLIP 300
PVTFEVKSES LGIPQKMHLK VDVESGKLIV KKSKDGSEDK FYSHKKILQL 350
IKSQKFLNKL VILVETEKEK ILRKEYVFAD SKKREGFCQL LQQMKNKHSE 400
QPEPDMITIF IGTWNMGNAP PPKKITSWFL SKGQGKTRDD SADYIPHDIY 450
VIGTQEDPLG EKEWLELLRH SLQEVTSMTF KTVAIHTLWN IRIVVLAKPE 500
HENRISHICT DNVKTGIANT LGNKGAVGVS FMFNGTSLGF VNSHLTSGSE 550
KKLRRNQNYM NILRFLALGD KKLSPFNITH RFTHLFWLGD LNYRVELPTW 600
EAEAIIQKIK QQQYSDLLAH DQLLLERKDQ KVFLHFEEEE ITFAPTYRFE 650
RLTRDKYAYT KQKATGMKYN LPSWCDRVLW KSYPLVHVVC QSYGSTSDIM 700
TSDHSPVFAT FEAGVTSQFV SKNGPGTVDS QGQIEFLACY ATLKTKSQTK 750
FYLEFHSSCL ESFVKSQEGE NEEGSEGELV VRFGETLPKL KPIISDPEYL 800
LDQHILISIK SSDSDESYGE GCIALRLETT EAQHPIYTPL THHGEMTGHF 850
RGEIKLQTSQ GKMREKLYDF VKTERDESSG MKCLKNLTSH DPMRQWEPSG 900
RVPACGVSSL NEMINPNYIG MGPFGQPLHG KSTLSPDQQL TAWSYDQLPK 950
DSSLGPGRGE GPPTPPSQPP LSPKKFSSST ANRGPCPRVQ EARPGDLGKV 1000
EALLQEDLLL TKPEMFENPL YGSVSSFPKL VPRKEQESPK MLRKEPPPCP 1050
DPGISSPSIV LPKAQEVESV KGTSKQAPVP VLGPTPRIRS FTCSSSAEGR 1100
MTSGDKSQGK PKASASSQAP VPVKRPVKPS RSEMSQQTTP IPAPRPPLPV 1150
KSPAVLQLQH SKGRDYRDNT ELPHHGKHRQ EEGLLGRTAM Q 1191
Length:1,191
Mass (Da):133,542
Last modified:September 11, 2007 - v2
Checksum:iAF9F21326A59EC7A
GO
Isoform 2 (identifier: Q9ES52-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: Missing.

Show »
Length:1,190
Mass (Da):133,443
Checksum:iDF81F3046F33A07F
GO
Isoform 3 (identifier: Q9ES52-3) [UniParc]FASTAAdd to Basket

Also known as: 135 kDa SHIP

The sequence of this isoform differs from the canonical sequence as follows:
     920-980: Missing.

Show »
Length:1,130
Mass (Da):127,199
Checksum:iC3E2F1EB206034BF
GO
Isoform 4 (identifier: Q9ES52-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:959
Mass (Da):108,345
Checksum:iB95D49476957345E
GO
Isoform 5 (identifier: Q9ES52-5) [UniParc]FASTAAdd to Basket

Also known as: s-SHIP

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: Missing.

Show »
Length:928
Mass (Da):104,101
Checksum:i7390D08E57505B82
GO
Isoform 6 (identifier: Q9ES52-6) [UniParc]FASTAAdd to Basket

Also known as: s-SHIPD183

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: Missing.
     920-980: Missing.

Show »
Length:867
Mass (Da):97,758
Checksum:iF848515DE853AD65
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 263263Missing in isoform 5 and isoform 6.
VSP_027980Add
BLAST
Alternative sequencei120 – 1201Missing in isoform 2 and isoform 4.
VSP_027981
Alternative sequencei920 – 98061Missing in isoform 3 and isoform 6.
VSP_027982Add
BLAST
Alternative sequencei920 – 96041GMGPF…PGRGE → VFIFHSQPRSLPQGARGKTW GSGKGGSSAPGGPAADEARD V in isoform 4.
VSP_027983Add
BLAST
Alternative sequencei961 – 1191231Missing in isoform 4.
VSP_027984Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431Y → C in AAB18937. 1 Publication
Sequence conflicti527 – 5271V → A in AAC53023. 1 Publication
Sequence conflicti534 – 5341N → I in AAC53023. 1 Publication
Sequence conflicti905 – 9051C → E AA sequence 1 Publication
Sequence conflicti981 – 9811A → T in AAB18937. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35655.1. [Q9ES52-1]
CCDS48310.1. [Q9ES52-3]
CCDS48311.1. [Q9ES52-2]
PIRiJC6118.
RefSeqiNP_001103662.1. NM_001110192.1. [Q9ES52-2]
NP_001103663.1. NM_001110193.1. [Q9ES52-3]
NP_034696.2. NM_010566.2. [Q9ES52-1]
UniGeneiMm.15105.

Genome annotation databases

EnsembliENSMUST00000042275; ENSMUSP00000044647; ENSMUSG00000026288. [Q9ES52-2]
ENSMUST00000072999; ENSMUSP00000072763; ENSMUSG00000026288. [Q9ES52-4]
ENSMUST00000167032; ENSMUSP00000126569; ENSMUSG00000026288. [Q9ES52-5]
ENSMUST00000168783; ENSMUSP00000131244; ENSMUSG00000026288. [Q9ES52-3]
ENSMUST00000169754; ENSMUSP00000127941; ENSMUSG00000026288. [Q9ES52-1]
ENSMUST00000170300; ENSMUSP00000132384; ENSMUSG00000026288. [Q9ES52-6]
GeneIDi16331.
KEGGimmu:16331.
UCSCiuc007bxc.2. mouse. [Q9ES52-1]
uc007bxd.2. mouse. [Q9ES52-3]
uc007bxf.2. mouse. [Q9ES52-2]
uc007bxg.2. mouse. [Q9ES52-6]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35655.1. [Q9ES52-1 ]
CCDS48310.1. [Q9ES52-3 ]
CCDS48311.1. [Q9ES52-2 ]
PIRi JC6118.
RefSeqi NP_001103662.1. NM_001110192.1. [Q9ES52-2 ]
NP_001103663.1. NM_001110193.1. [Q9ES52-3 ]
NP_034696.2. NM_010566.2. [Q9ES52-1 ]
UniGenei Mm.15105.

3D structure databases

ProteinModelPortali Q9ES52.
SMRi Q9ES52. Positions 3-152, 405-717.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200769. 24 interactions.
IntActi Q9ES52. 11 interactions.
MINTi MINT-205819.

PTM databases

PhosphoSitei Q9ES52.

Proteomic databases

MaxQBi Q9ES52.
PaxDbi Q9ES52.
PRIDEi Q9ES52.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000042275 ; ENSMUSP00000044647 ; ENSMUSG00000026288 . [Q9ES52-2 ]
ENSMUST00000072999 ; ENSMUSP00000072763 ; ENSMUSG00000026288 . [Q9ES52-4 ]
ENSMUST00000167032 ; ENSMUSP00000126569 ; ENSMUSG00000026288 . [Q9ES52-5 ]
ENSMUST00000168783 ; ENSMUSP00000131244 ; ENSMUSG00000026288 . [Q9ES52-3 ]
ENSMUST00000169754 ; ENSMUSP00000127941 ; ENSMUSG00000026288 . [Q9ES52-1 ]
ENSMUST00000170300 ; ENSMUSP00000132384 ; ENSMUSG00000026288 . [Q9ES52-6 ]
GeneIDi 16331.
KEGGi mmu:16331.
UCSCi uc007bxc.2. mouse. [Q9ES52-1 ]
uc007bxd.2. mouse. [Q9ES52-3 ]
uc007bxf.2. mouse. [Q9ES52-2 ]
uc007bxg.2. mouse. [Q9ES52-6 ]

Organism-specific databases

CTDi 3635.
MGIi MGI:107357. Inpp5d.

Phylogenomic databases

eggNOGi COG5411.
GeneTreei ENSGT00750000117420.
HOVERGENi HBG106726.
InParanoidi Q9ES52.
KOi K03084.
OMAi RKEPPPC.
OrthoDBi EOG75F4CD.
PhylomeDBi Q9ES52.
TreeFami TF323475.

Enzyme and pathway databases

Reactomei REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_210793. Interleukin receptor SHC signaling.
REACT_225145. Downstream TCR signaling.

Miscellaneous databases

NextBioi 289418.
PROi Q9ES52.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ES52.
Bgeei Q9ES52.
CleanExi MM_INPP5D.
Genevestigatori Q9ES52.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProi IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view ]
Pfami PF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [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. "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 SER-935 AND TYR-945, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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.
  31. "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.
  32. "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.
  33. "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.
  34. "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.
  35. "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.
  36. "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.
  37. "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.
  38. "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.
  39. "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.
  40. "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.
  41. "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.
  42. "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.
  43. "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.
  44. "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.
  45. "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.
  46. "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.
  47. "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.
  48. "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.
  49. "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.
  50. "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.
  51. "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.
  52. Cited for: FUNCTION.

Entry informationi

Entry nameiSHIP1_MOUSE
AccessioniPrimary (citable) accession number: Q9ES52
Secondary accession number(s): Q3UPF9
, Q4U212, Q61034, Q61173, Q61181, Q9JKR7, Q9JLF9, Q9JLG0, Q9QVN8, Q9WUC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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