INPPL1

From Wikipedia, the free encyclopedia

Inositol polyphosphate phosphatase-like 1

Identifiers

External IDs

OMIM: 600829 MGI: 1333787 HomoloGene: 1204

Gene ontology
Molecular Function:	• inositol or phosphatidylinositol phosphatase activity
Cellular Component:	• cellular_component
Biological Process:	• phosphate metabolic process • intracellular signaling cascade • biological_process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001567 (mRNA)
NP_001558 (protein)

NM_010567 (mRNA)
NP_034697 (protein)

Location

Chr 11: 71.58 - 71.63 Mb

Chr 7: 101.7 - 101.71 Mb

Pubmed search

[1]

[2]

Inositol polyphosphate phosphatase-like 1, also known as INPPL1, is a human gene.^[1]

INPPL1 encodes inositol polyphosphate-5 phosphatase-like 1, a protein that in addition to the phosphatase domain contains an SH2 (src-homology domain 2) motif.^[1]

[edit] References

^ ^a ^b Entrez Gene: INPPL1 inositol polyphosphate phosphatase-like 1.

[edit] Further reading

Hejna JA, Saito H, Merkens LS, et al. (1996). "Cloning and characterization of a human cDNA (INPPL1) sharing homology with inositol polyphosphate phosphatases.". Genomics 29 (1): 285–7. doi:10.1006/geno.1995.1247. PMID 8530088.
Pesesse X, Deleu S, De Smedt F, et al. (1997). "Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP.". Biochem. Biophys. Res. Commun. 239 (3): 697–700. doi:10.1006/bbrc.1997.7538. PMID 9367831.
Habib T, Hejna JA, Moses RE, Decker SJ (1998). "Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein.". J. Biol. Chem. 273 (29): 18605–9. PMID 9660833.
Pesesse X, Moreau C, Drayer AL, et al. (1998). "The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity.". FEBS Lett. 437 (3): 301–3. PMID 9824312.
Wisniewski D, Strife A, Swendeman S, et al. (1999). "A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells.". Blood 93 (8): 2707–20. PMID 10194451.
Bruyns C, Pesesse X, Moreau C, et al. (1999). "The two SH2-domain-containing inositol 5-phosphatases SHIP1 and SHIP2 are coexpressed in human T lymphocytes.". Biol. Chem. 380 (7-8): 969–74. PMID 10494849.
Schurmans S, Carrió R, Behrends J, et al. (2000). "The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse.". Genomics 62 (2): 260–71. doi:10.1006/geno.1999.5995. PMID 10610720.
Muraille E, Bruhns P, Pesesse X, et al. (2000). "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.". Immunol. Lett. 72 (1): 7–15. PMID 10789675.
Prasad N, Topping RS, Decker SJ (2001). "SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading.". Mol. Cell. Biol. 21 (4): 1416–28. doi:10.1128/MCB.21.4.1416-1428.2001. PMID 11158326.
Wada T, Sasaoka T, Funaki M, et al. (2001). "Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3-L1 adipocytes via its 5'-phosphatase catalytic activity.". Mol. Cell. Biol. 21 (5): 1633–46. doi:10.1128/MCB.21.5.1633-1646.2001. PMID 11238900.
Pesesse X, Dewaste V, De Smedt F, et al. (2001). "The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells.". J. Biol. Chem. 276 (30): 28348–55. doi:10.1074/jbc.M103537200. PMID 11349134.
Dyson JM, O'Malley CJ, Becanovic J, et al. (2002). "The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin.". J. Cell Biol. 155 (6): 1065–79. doi:10.1083/jcb.200104005. PMID 11739414.
Marion E, Kaisaki PJ, Pouillon V, et al. (2002). "The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate for type 2 diabetes in rat and man.". Diabetes 51 (7): 2012–7. PMID 12086927.
Giuriato S, Blero D, Robaye B, et al. (2002). "SHIP2 overexpression strongly reduces the proliferation rate of K562 erythroleukemia cell line.". Biochem. Biophys. Res. Commun. 296 (1): 106–10. PMID 12147234.
Prasad N, Topping RS, Decker SJ (2003). "Src family tyrosine kinases regulate adhesion-dependent tyrosine phosphorylation of 5'-inositol phosphatase SHIP2 during cell attachment and spreading on collagen I.". J. Cell. Sci. 115 (Pt 19): 3807–15. PMID 12235291.
Tridandapani S, Wang Y, Marsh CB, Anderson CL (2002). "Src homology 2 domain-containing inositol polyphosphate phosphatase regulates NF-kappa B-mediated gene transcription by phagocytic Fc gamma Rs in human myeloid cells.". J. Immunol. 169 (8): 4370–8. PMID 12370370.
Vandenbroere I, Paternotte N, Dumont JE, et al. (2003). "The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2.". Biochem. Biophys. Res. Commun. 300 (2): 494–500. PMID 12504111.
Salomon AR, Ficarro SB, Brill LM, et al. (2003). "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 443–8. doi:10.1073/pnas.2436191100. PMID 12522270.
Pengal RA, Ganesan LP, Fang H, et al. (2003). "SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling.". J. Biol. Chem. 278 (25): 22657–63. doi:10.1074/jbc.M302907200. PMID 12690104.
Kaisaki PJ, Delépine M, Woon PY, et al. (2004). "Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase (INPPL1, SHIP2) are associated with physiological abnormalities of the metabolic syndrome.". Diabetes 53 (7): 1900–4. PMID 15220217.