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Q92835

- SHIP1_HUMAN

UniProt

Q92835 - SHIP1_HUMAN

Protein

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

Gene

INPP5D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      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. 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 InsP6.2 Publications

    Catalytic activityi

    1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate.2 Publications

    Enzyme regulationi

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

    GO - Molecular functioni

    1. inositol-polyphosphate 5-phosphatase activity Source: ProtInc
    2. phosphatidylinositol trisphosphate phosphatase activity Source: Ensembl
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. blood coagulation Source: Reactome
    3. determination of adult lifespan Source: Ensembl
    4. immunoglobulin mediated immune response Source: Ensembl
    5. inositol phosphate metabolic process Source: Reactome
    6. intracellular signal transduction Source: Ensembl
    7. leukocyte migration Source: Reactome
    8. negative regulation of B cell proliferation Source: Ensembl
    9. negative regulation of bone resorption Source: Ensembl
    10. negative regulation of immune response Source: Ensembl
    11. negative regulation of interleukin-6 biosynthetic process Source: Ensembl
    12. negative regulation of monocyte differentiation Source: Ensembl
    13. negative regulation of neutrophil differentiation Source: Ensembl
    14. negative regulation of osteoclast differentiation Source: Ensembl
    15. negative regulation of signal transduction Source: Ensembl
    16. phosphate-containing compound metabolic process Source: ProtInc
    17. phosphatidylinositol biosynthetic process Source: Reactome
    18. phosphatidylinositol dephosphorylation Source: InterPro
    19. phospholipid metabolic process Source: Reactome
    20. positive regulation of apoptotic process Source: Ensembl
    21. positive regulation of B cell differentiation Source: Ensembl
    22. positive regulation of erythrocyte differentiation Source: Ensembl
    23. signal transduction Source: ProtInc
    24. small molecule metabolic process Source: Reactome
    25. T cell receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Apoptosis, Immunity

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09849-MONOMER.
    ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
    REACT_12519. PECAM1 interactions.
    REACT_12555. Downstream TCR signaling.
    REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_23891. Interleukin receptor SHC signaling.
    SignaLinkiQ92835.

    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
    Short name:
    hp51CN
    Gene namesi
    Name:INPP5D
    Synonyms:SHIP, SHIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6079. INPP5D.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication
    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 By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29887.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11891189Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1PRO_0000302866Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei915 – 9151Phosphotyrosine1 Publication
    Modified residuei934 – 9341PhosphoserineBy similarity
    Modified residuei944 – 9441PhosphotyrosineBy similarity
    Modified residuei1022 – 10221PhosphotyrosineBy similarity

    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.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ92835.
    PaxDbiQ92835.
    PRIDEiQ92835.

    PTM databases

    PhosphoSiteiQ92835.

    Expressioni

    Tissue specificityi

    Specifically expressed in immune and hematopoietic cells. Expressed in bone marrow and blood cells. Levels vary considerably within this compartment. Present in at least 74% of immature CD34+ cells, whereas within the more mature population of CD33+ cells, it is present in only 10% of cells. Present in the majority of T-cells, while it is present in a minority of B-cells (at protein level).4 Publications

    Gene expression databases

    ArrayExpressiQ92835.
    BgeeiQ92835.
    CleanExiHS_INPP5D.
    GenevestigatoriQ92835.

    Organism-specific databases

    HPAiCAB016300.

    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 By similarity. Interacts with MILR1 (tyrosine-phosphorylated). Can weakly interact (via NPXY motif 2) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FCGR2BP319942EBI-1380477,EBI-724784
    SH3KBP1Q96B976EBI-1380477,EBI-346595

    Protein-protein interaction databases

    BioGridi109847. 33 interactions.
    IntActiQ92835. 16 interactions.
    MINTiMINT-123561.
    STRINGi9606.ENSP00000352575.

    Structurei

    Secondary structure

    1
    1189
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi12 – 2211
    Beta strandi27 – 326
    Beta strandi39 – 457
    Beta strandi50 – 578
    Beta strandi63 – 653
    Beta strandi70 – 723
    Beta strandi76 – 783
    Helixi79 – 857
    Beta strandi88 – 958

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YSXNMR-A1-112[»]
    ProteinModelPortaliQ92835.
    SMRiQ92835. Positions 1-112, 402-714.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92835.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 10197SH2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1016 – 103015Interaction with DAB2By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi124 – 1296SH3-binding 1
    Motifi912 – 9154NPXY motif 1
    Motifi969 – 9746SH3-binding 2
    Motifi1019 – 10224NPXY motif 2
    Motifi1040 – 105112SH3-binding 3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi920 – 1148229Pro-richAdd
    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 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 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain, SH3-binding

    Phylogenomic databases

    eggNOGiCOG5411.
    HOVERGENiHBG106726.
    KOiK03084.
    OrthoDBiEOG75F4CD.
    PhylomeDBiQ92835.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92835-1) [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

    MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV     50
    YTYRILPNED DKFTVQASEG VSMRFFTKLD QLIEFYKKEN MGLVTHLQYP 100
    VPLEEEDTGD DPEEDTVESV VSPPELPPRN IPLTASSCEA KEVPFSNENP 150
    RATETSRPSL SETLFQRLQS MDTSGLPEEH LKAIQDYLST QLAQDSEFVK 200
    TGSSSLPHLK KLTTLLCKEL YGEVIRTLPS LESLQRLFDQ QLSPGLRPRP 250
    QVPGEANPIN MVSKLSQLTS LLSSIEDKVK ALLHEGPESP HRPSLIPPVT 300
    FEVKAESLGI PQKMQLKVDV ESGKLIIKKS KDGSEDKFYS HKKILQLIKS 350
    QKFLNKLVIL VETEKEKILR KEYVFADSKK REGFCQLLQQ MKNKHSEQPE 400
    PDMITIFIGT WNMGNAPPPK KITSWFLSKG QGKTRDDSAD YIPHDIYVIG 450
    TQEDPLSEKE WLEILKHSLQ EITSVTFKTV AIHTLWNIRI VVLAKPEHEN 500
    RISHICTDNV KTGIANTLGN KGAVGVSFMF NGTSLGFVNS HLTSGSEKKL 550
    RRNQNYMNIL RFLALGDKKL SPFNITHRFT HLFWFGDLNY RVDLPTWEAE 600
    TIIQKIKQQQ YADLLSHDQL LTERREQKVF LHFEEEEITF APTYRFERLT 650
    RDKYAYTKQK ATGMKYNLPS WCDRVLWKSY PLVHVVCQSY GSTSDIMTSD 700
    HSPVFATFEA GVTSQFVSKN GPGTVDSQGQ IEFLRCYATL KTKSQTKFYL 750
    EFHSSCLESF VKSQEGENEE GSEGELVVKF GETLPKLKPI ISDPEYLLDQ 800
    HILISIKSSD SDESYGEGCI ALRLEATETQ LPIYTPLTHH GELTGHFQGE 850
    IKLQTSQGKT REKLYDFVKT ERDESSGPKT LKSLTSHDPM KQWEVTSRAP 900
    PCSGSSITEI INPNYMGVGP FGPPMPLHVK QTLSPDQQPT AWSYDQPPKD 950
    SPLGPCRGES PPTPPGQPPI SPKKFLPSTA NRGLPPRTQE SRPSDLGKNA 1000
    GDTLPQEDLP LTKPEMFENP LYGSLSSFPK PAPRKDQESP KMPRKEPPPC 1050
    PEPGILSPSI VLTKAQEADR GEGPGKQVPA PRLRSFTCSS SAEGRAAGGD 1100
    KSQGKPKTPV SSQAPVPAKR PIKPSRSEIN QQTPPTPTPR PPLPVKSPAV 1150
    LHLQHSKGRD YRDNTELPHH GKHRPEEGPP GPLGRTAMQ 1189
    Length:1,189
    Mass (Da):133,292
    Last modified:September 11, 2007 - v2
    Checksum:i7958E91A64A4B68B
    GO
    Isoform 2 (identifier: Q92835-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         117-117: Missing.

    Show »
    Length:1,188
    Mass (Da):133,193
    Checksum:i335673E161C5FFAD
    GO
    Isoform 3 (identifier: Q92835-3) [UniParc]FASTAAdd to Basket

    Also known as: SIP-110

    The sequence of this isoform differs from the canonical sequence as follows:
         1-212: Missing.
         213-222: TTLLCKELYG → MFTLSPAPR

    Show »
    Length:976
    Mass (Da):109,294
    Checksum:i2B90E6DD584DD048
    GO

    Sequence cautioni

    The sequence AAC50454.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 262DG → GT in AAB49680. (PubMed:9058707)Curated
    Sequence conflicti1029 – 10291P → H in AAB49680. (PubMed:9058707)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti685 – 6851V → E in one patient with acute myeloid leukemya; somatic mutation. 1 Publication
    VAR_034979
    Natural varianti1169 – 11691H → Y.2 Publications
    Corresponds to variant rs9247 [ dbSNP | Ensembl ].
    VAR_059358

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 212212Missing in isoform 3. 1 PublicationVSP_027977Add
    BLAST
    Alternative sequencei117 – 1171Missing in isoform 2. 3 PublicationsVSP_027978
    Alternative sequencei213 – 22210TTLLCKELYG → MFTLSPAPR in isoform 3. 1 PublicationVSP_027979

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98429 mRNA. Translation: CAA67071.1.
    U57650 mRNA. Translation: AAB53573.1.
    U50040 mRNA. Translation: AAC50453.1.
    U50041 mRNA. Translation: AAC50454.1. Different initiation.
    U84400 mRNA. Translation: AAB49680.1.
    U53470 mRNA. Translation: AAD00081.1.
    BC062985 mRNA. Translation: AAH62985.1.
    BC099920 mRNA. Translation: AAH99920.1.
    BC113580 mRNA. Translation: AAI13581.1.
    BC113582 mRNA. Translation: AAI13583.1.
    PIRiJC4889.
    RefSeqiNP_001017915.1. NM_001017915.2. [Q92835-1]
    NP_005532.2. NM_005541.4. [Q92835-2]
    UniGeneiHs.262886.
    Hs.601911.

    Genome annotation databases

    EnsembliENST00000359570; ENSP00000352575; ENSG00000168918.
    GeneIDi3635.
    KEGGihsa:3635.
    UCSCiuc010zmo.2. human. [Q92835-1]
    uc010zmp.2. human. [Q92835-2]

    Polymorphism databases

    DMDMi158564077.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98429 mRNA. Translation: CAA67071.1 .
    U57650 mRNA. Translation: AAB53573.1 .
    U50040 mRNA. Translation: AAC50453.1 .
    U50041 mRNA. Translation: AAC50454.1 . Different initiation.
    U84400 mRNA. Translation: AAB49680.1 .
    U53470 mRNA. Translation: AAD00081.1 .
    BC062985 mRNA. Translation: AAH62985.1 .
    BC099920 mRNA. Translation: AAH99920.1 .
    BC113580 mRNA. Translation: AAI13581.1 .
    BC113582 mRNA. Translation: AAI13583.1 .
    PIRi JC4889.
    RefSeqi NP_001017915.1. NM_001017915.2. [Q92835-1 ]
    NP_005532.2. NM_005541.4. [Q92835-2 ]
    UniGenei Hs.262886.
    Hs.601911.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YSX NMR - A 1-112 [» ]
    ProteinModelPortali Q92835.
    SMRi Q92835. Positions 1-112, 402-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109847. 33 interactions.
    IntActi Q92835. 16 interactions.
    MINTi MINT-123561.
    STRINGi 9606.ENSP00000352575.

    Chemistry

    ChEMBLi CHEMBL1781870.

    PTM databases

    PhosphoSitei Q92835.

    Polymorphism databases

    DMDMi 158564077.

    Proteomic databases

    MaxQBi Q92835.
    PaxDbi Q92835.
    PRIDEi Q92835.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359570 ; ENSP00000352575 ; ENSG00000168918 .
    GeneIDi 3635.
    KEGGi hsa:3635.
    UCSCi uc010zmo.2. human. [Q92835-1 ]
    uc010zmp.2. human. [Q92835-2 ]

    Organism-specific databases

    CTDi 3635.
    GeneCardsi GC02P233924.
    H-InvDB HIX0057065.
    HGNCi HGNC:6079. INPP5D.
    HPAi CAB016300.
    MIMi 601582. gene.
    neXtProti NX_Q92835.
    PharmGKBi PA29887.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5411.
    HOVERGENi HBG106726.
    KOi K03084.
    OrthoDBi EOG75F4CD.
    PhylomeDBi Q92835.
    TreeFami TF323475.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09849-MONOMER.
    Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
    REACT_12519. PECAM1 interactions.
    REACT_12555. Downstream TCR signaling.
    REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_23891. Interleukin receptor SHC signaling.
    SignaLinki Q92835.

    Miscellaneous databases

    ChiTaRSi INPP5D. human.
    EvolutionaryTracei Q92835.
    GeneWikii INPP5D.
    GenomeRNAii 3635.
    NextBioi 14225.
    PROi Q92835.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92835.
    Bgeei Q92835.
    CleanExi HS_INPP5D.
    Genevestigatori Q92835.

    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

    1. "Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase."
      Drayer A.L., Pesesse X., De Smedt F., Woscholski R., Parker P., Erneux C.
      Biochem. Biophys. Res. Commun. 225:243-249(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ENZYME ACTIVITY, TISSUE SPECIFICITY, VARIANT TYR-1169.
    2. "Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation."
      Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., Krystal G.
      Blood 88:2833-2840(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH SHC1.
    3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-1139 (ISOFORM 1), ENZYME ACTIVITY, INTERACTION WITH GRB2.
      Tissue: Lung.
    4. "The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood."
      Geier S.J., Algate P.A., Carlberg K., Flowers D., Friedman C., Trask B., Rohrschneider L.R.
      Blood 89:1876-1885(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    5. "Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl."
      Odai H., Sasaki K., Iwamatsu A., Nakamoto T., Ueno H., Yamagata T., Mitani K., Yazaki Y., Hirai H.
      Blood 89:2745-2756(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH GRB2.
    6. "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), VARIANT TYR-1169.
      Tissue: B-cell and Lymph.
    7. "CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis."
      Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A., Sidorenko S.P.
      J. Immunol. 162:5719-5727(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLAMF1.
    8. "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells."
      Dunant N.M., Wisniewski D., Strife A., Clarkson B., Resh M.D.
      Cell. Signal. 12:317-326(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH DOK1.
    9. "Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors."
      Freeburn R.W., Wright K.L., Burgess S.J., Astoul E., Cantrell D.A., Ward S.G.
      J. Immunol. 169:5441-5450(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "The Src homology 2-containing inositol 5-phosphatase 1 (SHIP1) is involved in CD32a signaling in human neutrophils."
      Vaillancourt M., Levasseur S., Tremblay M.-L., Marois L., Rollet-Labelle E., Naccache P.H.
      Cell. Signal. 18:2022-2032(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Solution structure of the human SHIP SH2 domain."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-112.
    14. "Possible dominant-negative mutation of the SHIP gene in acute myeloid leukemia."
      Luo J.-M., Yoshida H., Komura S., Ohishi N., Pan L., Shigeno K., Hanamura I., Miura K., Iida S., Ueda R., Naoe T., Akao Y., Ohno R., Ohnishi K.
      Leukemia 17:1-8(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLU-685.

    Entry informationi

    Entry nameiSHIP1_HUMAN
    AccessioniPrimary (citable) accession number: Q92835
    Secondary accession number(s): O00145
    , Q13544, Q13545, Q6P5A4, Q92656, Q9UE80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3