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Q6P549

- SHIP2_MOUSE

UniProt

Q6P549 - SHIP2_MOUSE

Protein

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2

Gene

Inppl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity is enhanced in the presence of phosphatidylserine By similarity.By similarity

    GO - Molecular functioni

    1. hydrolase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin filament organization Source: Ensembl
    2. cell adhesion Source: UniProtKB-KW
    3. cellular lipid metabolic process Source: MGI
    4. endochondral ossification Source: UniProtKB
    5. endocytosis Source: Ensembl
    6. glucose metabolic process Source: MGI
    7. immune system process Source: UniProtKB-KW
    8. negative regulation of cell proliferation Source: MGI
    9. negative regulation of gene expression Source: MGI
    10. phosphatidylinositol biosynthetic process Source: MGI
    11. phosphatidylinositol dephosphorylation Source: InterPro
    12. post-embryonic development Source: MGI
    13. response to insulin Source: MGI
    14. ruffle assembly Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell adhesion, Immunity

    Keywords - Ligandi

    Actin-binding

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC:3.1.3.86)
    Alternative name(s):
    AblSH3-binding protein
    Inositol polyphosphate phosphatase-like protein 1
    Short name:
    INPPL-1
    SH2 domain-containing inositol 5'-phosphatase 2
    Short name:
    SH2 domain-containing inositol phosphatase 2
    Short name:
    SHIP-2
    Gene namesi
    Name:Inppl1
    Synonyms:Ship2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1333787. Inppl1.

    Subcellular locationi

    Cytoplasmcytosol. Cytoplasmcytoskeleton By similarity. Membrane; Peripheral membrane protein. Cell projectionfilopodium By similarity. Cell projectionlamellipodium By similarity
    Note: Translocates to membrane ruffles 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). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB-SubCell
    4. filopodium Source: UniProtKB-SubCell
    5. Golgi apparatus Source: Ensembl
    6. lamellipodium Source: UniProtKB-SubCell
    7. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable, have normal glucose and insulin levels, and normal insulin and glucose tolerance. They are however highly resistant to weight gain when placed on a high-fat diet, suggesting that inhibition of Inppl1 would be useful in the effort to ameliorate diet-induced obesity. According to preliminary results from PubMed:11343120, mice display increased sensitivity to insulin, characterized by severe neonatal hypoglycemia, deregulated expression of the genes involved in gluconeogenesis, and perinatal death. They display increased glucose tolerance and insulin sensitivity associated with an increased recruitment of the Slc2a4/Glut4 glucose transporter and increased glycogen synthesis in skeletal muscles. However, these knockout mice also contain a deletion of the last exon of Phox2a gene. It is therefore unknown whether the insulin sensitivity observed in these mice result from inactivation of either Inppl1 or Phox2a.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi47 – 471R → A: Does not affect the ability to inhibit PKB activity. 1 Publication
    Mutagenesisi608 – 6081D → A: Abolishes both enzyme activity and ability to inhibit PKB activity. 1 Publication
    Mutagenesisi690 – 6901C → A: Induces little effect. 1 Publication
    Mutagenesisi692 – 6921R → A: Still partially active. 1 Publication
    Mutagenesisi987 – 9871Y → F: Does not affect the ability to inhibit PKB activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12571257Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2PRO_0000302871Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei132 – 1321Phosphoserine1 Publication
    Modified residuei165 – 1651PhosphothreonineBy similarity
    Modified residuei241 – 2411PhosphoserineBy similarity
    Modified residuei987 – 9871PhosphotyrosineBy similarity
    Modified residuei1136 – 11361PhosphotyrosineBy similarity
    Modified residuei1161 – 11611PhosphotyrosineBy similarity

    Post-translational modificationi

    Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-987 following cell attachment and spreading. Phosphorylated at Tyr-1161 following EGF signaling pathway stimulation By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6P549.
    PaxDbiQ6P549.
    PRIDEiQ6P549.

    PTM databases

    PhosphoSiteiQ6P549.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Developmental stagei

    In E15.5 embryos, it is strongly expressed in the liver, specific regions of the central nervous system, the thymus, the lung, and the cartilage perichondrium. In adult it is markedly present in the brain and the thymus and at different stages of spermatozoa maturation in the seminiferous tubules.1 Publication

    Inductioni

    Overexpressed in diabetic db/db mice.1 Publication

    Gene expression databases

    BgeeiQ6P549.
    CleanExiMM_INPPL1.
    GenevestigatoriQ6P549.

    Interactioni

    Subunit structurei

    Interacts with tyrosine phosphorylated form of SHC1, Interacts with EGFR. Upon stimulation by the EGF signaling pathway, it forms a complex with SHC1 and EGFR. Interacts with cytoskeletal protein SORBS3/vinexin, promoting its localization to the periphery of cells. Forms a complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and submembraneous actin. Interacts with c-Met/MET, when c-Met/MET is phosphorylated on 'Tyr-1356'. Interacts with p130Cas/BCAR1. Interacts with CENTD3/ARAP3 via its SAM domain. Interacts with c-Cbl/CBL and CAP/SORBS1. Interacts with activated EPHA2 receptor. Interacts with receptors FCGR2A and FCGR2B. Interacts with tyrosine kinases ABL1 and TEC. Interacts with CSF1R.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Itsn1Q9Z0R4-22EBI-2642932,EBI-8052786

    Protein-protein interaction databases

    BioGridi200770. 5 interactions.
    IntActiQ6P549. 5 interactions.
    STRINGi10090.ENSMUSP00000048057.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6P549.
    SMRiQ6P549. Positions 20-147, 423-732, 1193-1257.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 11797SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1195 – 125763SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi945 – 9506SH3-binding
    Motifi984 – 9874NPXY motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi936 – 1170235Pro-richAdd
    BLAST

    Domaini

    The SH2 domain interacts with tyrosine phosphorylated forms of proteins such as SHC1 or FCGR2A. It also mediates the interaction with p130Cas/BCAR1 By similarity.By similarity
    The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.By similarity

    Sequence similaritiesi

    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3-binding

    Phylogenomic databases

    eggNOGiCOG5411.
    GeneTreeiENSGT00750000117420.
    HOGENOMiHOG000004836.
    HOVERGENiHBG106726.
    InParanoidiQ6P549.
    KOiK15909.
    OMAiYQKHVHT.
    OrthoDBiEOG75F4CD.
    PhylomeDBiQ6P549.
    TreeFamiTF323475.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    3.30.505.10. 1 hit.
    3.60.10.10. 1 hit.
    InterProiIPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR000980. SH2.
    [Graphical view]
    PfamiPF03372. Exo_endo_phos. 1 hit.
    PF00536. SAM_1. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    SMARTiSM00128. IPPc. 1 hit.
    SM00454. SAM. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56219. SSF56219. 1 hit.
    PROSITEiPS50105. SAM_DOMAIN. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6P549-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASVCGTPSP GGALGSPAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE     50
    SVAGAFALCV LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG 100
    LYAQPNQGLV CALLLPVEGE REPDPPDDRD ASDVEDEKPP LPPRSGSTSI 150
    SAPVGPSSPL PTPETPTTPA AESTPNGLST VSHEYLKGSY GLDLEAVRGG 200
    ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS SPMVTRLLQQ 250
    QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP 300
    SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ 350
    RDSQEDWTTF THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR 400
    KREAFCQLLQ LMKNRHSKQD EPDMISVFIG TWNMGSVPPP KNVTSWFTSK 450
    GLGKALDEVT VTIPHDIYVF GTQENSVGDR EWLDLLRGGL KELTDLDYRP 500
    IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG NKGAVGVSFM 550
    FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF 600
    THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR 650
    FSEEEISFPP TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE 700
    THIICNSYGC TDDIVTSDHS PVFGTFEVGV TSQFISKKGL SKTSDQAYIE 750
    FESIEAIVKT ASRTKFFIEF YSTCLEEYKK SFENDAQSSD NINFLKVQWS 800
    SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV ALKSMIGSTA 850
    QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK 900
    SKVPSVSRGS QEHRSGSRKP ASTETSCPLS KLFEEPEKPP PTGRPPAPPR 950
    AVPREEPLNP RLKSEGTSEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL 1000
    EPPSLARAPL PPATKNKVAI TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP 1050
    PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG RSGGEARGPP PPKAHPRPPL 1100
    PPGTSPASTF LGEVASGDDR SCSVLQMAKT LSEVDYAPGP GRSALLPNPL 1150
    ELQPPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM 1200
    GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL 1250
    DTLQLSK 1257
    Length:1,257
    Mass (Da):138,973
    Last modified:July 5, 2004 - v1
    Checksum:iB66DF96BEF22F01E
    GO

    Sequence cautioni

    The sequence AAI19454.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti412 – 4121M → I in AAF28187. (PubMed:10610720)Curated
    Sequence conflicti506 – 5061L → I in AAF28187. (PubMed:10610720)Curated
    Sequence conflicti705 – 7051C → S in AAB82337. (PubMed:9126384)Curated
    Sequence conflicti972 – 9721G → V in AAF28187. (PubMed:10610720)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF162781 mRNA. Translation: AAF28187.1.
    BC049961 mRNA. Translation: AAH49961.1.
    BC063080 mRNA. Translation: AAH63080.1.
    BC119453 mRNA. Translation: AAI19454.1. Different initiation.
    U92477 mRNA. Translation: AAB82337.1.
    CCDSiCCDS21515.1.
    RefSeqiNP_001116211.1. NM_001122739.1.
    NP_034697.2. NM_010567.2.
    XP_006507454.1. XM_006507391.1.
    UniGeneiMm.476000.

    Genome annotation databases

    EnsembliENSMUST00000035836; ENSMUSP00000048057; ENSMUSG00000032737.
    ENSMUST00000165052; ENSMUSP00000132883; ENSMUSG00000032737.
    GeneIDi16332.
    KEGGimmu:16332.
    UCSCiuc009ipg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF162781 mRNA. Translation: AAF28187.1 .
    BC049961 mRNA. Translation: AAH49961.1 .
    BC063080 mRNA. Translation: AAH63080.1 .
    BC119453 mRNA. Translation: AAI19454.1 . Different initiation.
    U92477 mRNA. Translation: AAB82337.1 .
    CCDSi CCDS21515.1.
    RefSeqi NP_001116211.1. NM_001122739.1.
    NP_034697.2. NM_010567.2.
    XP_006507454.1. XM_006507391.1.
    UniGenei Mm.476000.

    3D structure databases

    ProteinModelPortali Q6P549.
    SMRi Q6P549. Positions 20-147, 423-732, 1193-1257.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200770. 5 interactions.
    IntActi Q6P549. 5 interactions.
    STRINGi 10090.ENSMUSP00000048057.

    Chemistry

    ChEMBLi CHEMBL2331063.

    PTM databases

    PhosphoSitei Q6P549.

    Proteomic databases

    MaxQBi Q6P549.
    PaxDbi Q6P549.
    PRIDEi Q6P549.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000035836 ; ENSMUSP00000048057 ; ENSMUSG00000032737 .
    ENSMUST00000165052 ; ENSMUSP00000132883 ; ENSMUSG00000032737 .
    GeneIDi 16332.
    KEGGi mmu:16332.
    UCSCi uc009ipg.2. mouse.

    Organism-specific databases

    CTDi 3636.
    MGIi MGI:1333787. Inppl1.

    Phylogenomic databases

    eggNOGi COG5411.
    GeneTreei ENSGT00750000117420.
    HOGENOMi HOG000004836.
    HOVERGENi HBG106726.
    InParanoidi Q6P549.
    KOi K15909.
    OMAi YQKHVHT.
    OrthoDBi EOG75F4CD.
    PhylomeDBi Q6P549.
    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.

    Miscellaneous databases

    ChiTaRSi INPPL1. mouse.
    NextBioi 289422.
    PROi Q6P549.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6P549.
    CleanExi MM_INPPL1.
    Genevestigatori Q6P549.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    3.30.505.10. 1 hit.
    3.60.10.10. 1 hit.
    InterProi IPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR000980. SH2.
    [Graphical view ]
    Pfami PF03372. Exo_endo_phos. 1 hit.
    PF00536. SAM_1. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    SMARTi SM00128. IPPc. 1 hit.
    SM00454. SAM. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56219. SSF56219. 1 hit.
    PROSITEi PS50105. SAM_DOMAIN. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse."
      Schurmans S., Carrio R., Behrends J., Pouillon V., Merino J., Clement S.
      Genomics 62:260-271(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. "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].
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain and Kidney.
    3. "Examining the specificity of Src homology 3 domain -- ligand interactions with alkaline phosphatase fusion proteins."
      Yamabhai M., Kay B.K.
      Anal. Biochem. 247:143-151(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 705-1183.
    4. "The SH2 domain containing inositol 5-phosphatase SHIP2 associates to the immunoreceptor tyrosine-based inhibition motif of Fc gammaRIIB in B cells under negative signaling."
      Muraille E., Bruhns P., Pesesse X., Daeeron M., Erneux C.
      Immunol. Lett. 72:7-15(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCGR2B, PHOSPHORYLATION.
    5. "5' phospholipid phosphatase SHIP-2 causes protein kinase B inactivation and cell cycle arrest in glioblastoma cells."
      Taylor V., Wong M., Brandts C., Reilly L., Dean N.M., Cowsert L.M., Moodie S., Stokoe D.
      Mol. Cell. Biol. 20:6860-6871(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF ARG-47; ASP-608; CYS-690; ARG-692 AND TYR-987.
    6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Association of SH2-containing inositol phosphatase 2 with the insulin resistance of diabetic db/db mice."
      Hori H., Sasaoka T., Ishihara H., Wada T., Murakami S., Ishiki M., Kobayashi M.
      Diabetes 51:2387-2394(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "SH2-containing inositol phosphatase 2 predominantly regulates Akt2, and not Akt1, phosphorylation at the plasma membrane in response to insulin in 3T3-L1 adipocytes."
      Sasaoka T., Wada T., Fukui K., Murakami S., Ishihara H., Suzuki R., Tobe K., Kadowaki T., Kobayashi M.
      J. Biol. Chem. 279:14835-14843(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "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.
    10. "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.
    11. "SHIP2 is recruited to the cell membrane upon macrophage colony-stimulating factor (M-CSF) stimulation and regulates M-CSF-induced signaling."
      Wang Y., Keogh R.J., Hunter M.G., Mitchell C.A., Frey R.S., Javaid K., Malik A.B., Schurmans S., Tridandapani S., Marsh C.B.
      J. Immunol. 173:6820-6830(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH CSF1R.
    12. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    13. "The inositol phosphatase SHIP-2 down-regulates FcgammaR-mediated phagocytosis in murine macrophages independently of SHIP-1."
      Ai J., Maturu A., Johnson W., Wang Y., Marsh C.B., Tridandapani S.
      Blood 107:813-820(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiSHIP2_MOUSE
    AccessioniPrimary (citable) accession number: Q6P549
    Secondary accession number(s): O08611
    , Q0VDX5, Q80YB9, Q9JLL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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