INPPL1

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Inositol polyphosphate phosphatase-like 1
Protein INPPL1 PDB 2K4P.png
Rendering based on PDB 2K4P.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols INPPL1 ; OPSMD; SHIP2
External IDs OMIM600829 MGI1333787 HomoloGene1204 GeneCards: INPPL1 Gene
EC number 3.1.3.86
RNA expression pattern
PBB GE INPPL1 201598 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3636 16332
Ensembl ENSG00000165458 ENSMUSG00000032737
UniProt O15357 Q6P549
RefSeq (mRNA) NM_001567 NM_001122739
RefSeq (protein) NP_001558 NP_001116211
Location (UCSC) Chr 11:
71.93 – 71.95 Mb
Chr 7:
101.82 – 101.84 Mb
PubMed search [1] [2]

SH2-domain containing Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 is an enzyme that in humans is encoded by the INPPL1 gene.[1][2]

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.[2]

Interactions[edit]

INPPL1 has been shown to interact with BCAR1,[3] SORBS1,[4] FLNC[5] and SHC1.[6][7][8]

References[edit]

  1. ^ Hejna JA, Saito H, Merkens LS, Tittle TV, Jakobs PM, Whitney MA, Grompe M, Friedberg AS, Moses RE (February 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. 
  2. ^ a b "Entrez Gene: INPPL1 inositol polyphosphate phosphatase-like 1". 
  3. ^ Prasad, N; Topping R S; Decker S J (February 2001). "SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading". Mol. Cell. Biol. (United States) 21 (4): 1416–28. doi:10.1128/MCB.21.4.1416-1428.2001. ISSN 0270-7306. PMC 99593. PMID 11158326. 
  4. ^ Vandenbroere, Isabelle; Paternotte Nathalie; Dumont Jacques E; Erneux Christophe; Pirson Isabelle (January 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. (United States) 300 (2): 494–500. doi:10.1016/S0006-291X(02)02894-2. ISSN 0006-291X. PMID 12504111. 
  5. ^ Dyson, J M; O'Malley C J; Becanovic J; Munday A D; Berndt M C; Coghill I D; Nandurkar H H; Ooms L M; Mitchell C A (December 2001). "The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin". J. Cell Biol. (United States) 155 (6): 1065–79. doi:10.1083/jcb.200104005. ISSN 0021-9525. PMC 2150887. PMID 11739414. 
  6. ^ Wisniewski, D; Strife A; Swendeman S; Erdjument-Bromage H; Geromanos S; Kavanaugh W M; Tempst P; Clarkson B (April 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 (UNITED STATES) 93 (8): 2707–20. ISSN 0006-4971. PMID 10194451. 
  7. ^ Pesesse, X; Dewaste V; De Smedt F; Laffargue M; Giuriato S; Moreau C; Payrastre B; Erneux C (July 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. (United States) 276 (30): 28348–55. doi:10.1074/jbc.M103537200. ISSN 0021-9258. PMID 11349134. 
  8. ^ Habib, T; Hejna J A; Moses R E; Decker S J (July 1998). "Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein". J. Biol. Chem. (UNITED STATES) 273 (29): 18605–9. doi:10.1074/jbc.273.29.18605. ISSN 0021-9258. PMID 9660833. 

Further reading[edit]