INPPL1

INPPL1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2K4P, 2KSO, 2MK2, 3NR8, 4A9C
Identifiers
Aliases	INPPL1 , OPSMD, SHIP2, inositol polyphosphate phosphatase like 1
External IDs	OMIM: 600829 MGI: 1333787 HomoloGene: 1204 GeneCards: INPPL1
Gene location (Human)
Chr.	Chromosome 11 (human)
End	72,239,105 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	101,487,436 bp
RNA expression pattern
	Top expressed in
	gastric mucosa; ; stromal cell of endometrium; ; right lobe of thyroid gland; ; left lobe of thyroid gland; ; right uterine tube; ; left uterine tube; ; canal of the cervix; ; anterior pituitary; ; body of stomach; ; right lung;
	Top expressed in
	digastric muscle; ; extraocular muscle; ; internal carotid artery; ; temporal muscle; ; ankle; ; sternocleidomastoid muscle; ; external carotid artery; ; soleus muscle; ; triceps brachii muscle; ; semen;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	SH3 domain binding ; SH2 domain binding ; protein binding ; actin binding ; hydrolase activity ; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity ; inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity ;
Cellular component	Golgi apparatus ; cell projection ; membrane ; filopodium ; plasma membrane ; cytoskeleton ; lamellipodium ; cytoplasm ; cytosol ;
Biological process	endocytosis ; cellular lipid metabolic process ; actin filament organization ; immune system process ; inositol phosphate metabolic process ; endochondral ossification ; post-embryonic development ; negative regulation of gene expression ; response to insulin ; cell adhesion ; phosphatidylinositol dephosphorylation ; glucose metabolic process ; phosphatidylinositol biosynthetic process ; ruffle assembly ; negative regulation of cell population proliferation ; cytokine-mediated signaling pathway ;
	Sources:Amigo / QuickGO
Orthologs
	3636
	16332
	ENSG00000165458
	ENSMUSG00000032737
	O15357
	Q6P549
	NM_001567
	NM_001122739 ; NM_010567
	NP_001558
	NP_001116211 ; NP_034697
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

SH2-domain containing Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 is an enzyme that in humans is encoded by the INPPL1 gene.^[5]^[6]

Interactions

INPPL1 has been shown to interact with:

Related Research Articles

<span class="mw-page-title-main">Phosphatidylinositol (3,4,5)-trisphosphate</span> Chemical compound

Phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P₃), abbreviated PIP₃, is the product of the class I phosphoinositide 3-kinases (PI 3-kinases) phosphorylation of phosphatidylinositol (4,5)-bisphosphate (PIP₂). It is a phospholipid that resides on the plasma membrane.

<span class="mw-page-title-main">PTPN11</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) also known as protein-tyrosine phosphatase 1D (PTP-1D), Src homology region 2 domain-containing phosphatase-2 (SHP-2), or protein-tyrosine phosphatase 2C (PTP-2C) is an enzyme that in humans is encoded by the PTPN11 gene. PTPN11 is a protein tyrosine phosphatase (PTP) Shp2.

Son of sevenless homolog 1 is a protein that in humans is encoded by the SOS1 gene.

Phosphatidylinositol 3-kinase regulatory subunit alpha is an enzyme that in humans is encoded by the PIK3R1 gene.

Cbl is a mammalian gene encoding the protein CBL which is an E3 ubiquitin-protein ligase involved in cell signalling and protein ubiquitination. Mutations to this gene have been implicated in a number of human cancers, particularly acute myeloid leukaemia.

RAS p21 protein activator 1 or RasGAP, also known as RASA1, is a 120-kDa cytosolic human protein that provides two principal activities:

Docking protein 1 is a protein that in humans is encoded by the DOK1 gene.

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 is an enzyme that in humans is encoded by the PLCG2 gene.

Src homology 2 (SH2) domain containing inositol polyphosphate 5-phosphatase 1(SHIP1) is an enzyme with phosphatase activity. SHIP1 is structured by multiple domain and is encoded by the INPP5D gene in humans. SHIP1 is expressed predominantly by hematopoietic cells but also, for example, by osteoblasts and endothelial cells. This phosphatase is important for the regulation of cellular activation. Not only catalytic but also adaptor activities of this protein are involved in this process. Its movement from the cytosol to the cytoplasmic membrane, where predominantly performs its function, is mediated by tyrosine phosphorylation of the intracellular chains of cell surface receptors that SHIP1 binds. Insufficient regulation of SHIP1 leads to different pathologies.

Tyrosine-protein phosphatase non-receptor type 12 is an enzyme that in humans is encoded by the PTPN12 gene.

Receptor-type tyrosine-protein phosphatase alpha is an enzyme that in humans is encoded by the PTPRA gene.

Cytoplasmic tyrosine-protein kinase BMX is an enzyme that in humans is encoded by the BMX gene.

Type I inositol-3,4-bisphosphate 4-phosphatase is an enzyme that in humans is encoded by the INPP4A gene.

Ras GTPase-activating protein 3 is an enzyme that in humans is encoded by the RASA3 gene.

Tyrosine-protein phosphatase non-receptor type 9 is an enzyme that in humans is encoded by the PTPN9 gene.

Type I inositol-1,4,5-trisphosphate 5-phosphatase is an enzyme that in humans is encoded by the INPP5A gene.

SKIP is an acronym for Skeletal muscle and kidney enriched inositol phosphatase, which is a human gene.

A non-receptor tyrosine kinase (nRTK) is a cytosolic enzyme that is responsible for catalysing the transfer of a phosphate group from a nucleoside triphosphate donor, such as ATP, to tyrosine residues in proteins. Non-receptor tyrosine kinases are a subgroup of protein family tyrosine kinases, enzymes that can transfer the phosphate group from ATP to a tyrosine residue of a protein (phosphorylation). These enzymes regulate many cellular functions by switching on or switching off other enzymes in a cell.

Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase is an enzyme with systematic name 1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 5-phosphohydrolase, that has two isoforms: SHIP1 and SHIP2 (INPPL1).

Inositol polyphosphate-5-phosphatase F is a protein that in humans is encoded by the INPP5F gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000165458 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032737 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: INPPL1 inositol polyphosphate phosphatase-like 1".
↑ Prasad N, Topping RS, Decker SJ (February 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. PMC 99593 . PMID 11158326.
↑ Dyson JM, O'Malley CJ, Becanovic J, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA (December 2001). "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. PMC 2150887 . PMID 11739414.
↑ Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, 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. 93 (8): 2707–20. doi:10.1182/blood.V93.8.2707. PMID 10194451.
↑ 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. 276 (30): 28348–55. doi: 10.1074/jbc.M103537200 . PMID 11349134.
↑ Habib T, Hejna JA, Moses RE, Decker SJ (July 1998). "Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein". J. Biol. Chem. 273 (29): 18605–9. doi: 10.1074/jbc.273.29.18605 . PMID 9660833.
↑ Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I (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. 300 (2): 494–500. doi:10.1016/s0006-291x(02)02894-2. PMID 12504111.

Pesesse X, Deleu S, De Smedt F, Drayer L, Erneux C (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. doi: 10.1074/jbc.273.29.18605 . PMID 9660833.
Pesesse X, Moreau C, Drayer AL, Woscholski R, Parker P, Erneux C (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. doi: 10.1016/S0014-5793(98)01255-1 . PMID 9824312. S2CID 22837416.
Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B (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. doi:10.1182/blood.V93.8.2707. PMID 10194451.
Bruyns C, Pesesse X, Moreau C, Blero D, Erneux C (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. doi:10.1515/BC.1999.120. PMID 10494849. S2CID 42081112.
Schurmans S, Carrió R, Behrends J, Pouillon V, Merino J, Clément S (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, Daëron M, Erneux C (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. doi:10.1016/S0165-2478(00)00162-0. 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. PMC 99593 . PMID 11158326.
Wada T, Sasaoka T, Funaki M, Hori H, Murakami S, Ishiki M, Haruta T, Asano T, Ogawa W, Ishihara H, Kobayashi M (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. PMC 86709 . PMID 11238900.
Pesesse X, Dewaste V, De Smedt F, Laffargue M, Giuriato S, Moreau C, Payrastre B, Erneux C (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, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA (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. PMC 2150887 . PMID 11739414.
Marion E, Kaisaki PJ, Pouillon V, Gueydan C, Levy JC, Bodson A, Krzentowski G, Daubresse JC, Mockel J, Behrends J, Servais G, Szpirer C, Kruys V, Gauguier D, Schurmans S (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. doi: 10.2337/diabetes.51.7.2012 . PMID 12086927.
Giuriato S, Blero D, Robaye B, Bruyns C, Payrastre B, Erneux C (2002). "SHIP2 overexpression strongly reduces the proliferation rate of K562 erythroleukemia cell line". Biochem. Biophys. Res. Commun. 296 (1): 106–10. doi:10.1016/S0006-291X(02)00787-8. 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. doi: 10.1242/jcs.00070 . 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. doi: 10.4049/jimmunol.169.8.4370 . PMID 12370370.
Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I (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. doi:10.1016/S0006-291X(02)02894-2. PMID 12504111.
Salomon AR, Ficarro SB, Brill LM, Brinker A, Phung QT, Ericson C, Sauer K, Brock A, Horn DM, Schultz PG, Peters EC (2003). "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 443–8. Bibcode:2003PNAS..100..443S. doi: 10.1073/pnas.2436191100 . PMC 141014 . PMID 12522270.
Pengal RA, Ganesan LP, Fang H, Marsh CB, Anderson CL, Tridandapani S (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, Sebag-Montefiore L, Wilder SP, Menzel S, Vionnet N, Marion E, Riveline JP, Charpentier G, Schurmans S, Levy JC, Lathrop M, Farrall M, Gauguier D (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. doi: 10.2337/diabetes.53.7.1900 . PMID 15220217.
Hughes AE, Bradley DT, Campbell M, Lechner J, Dash DP, Simpson DA, Willoughby CE (2011). "Mutation Altering the miR-184 Seed Region Causes Familial Keratoconus with Cataract". The American Journal of Human Genetics. 89 (5): 628–33. doi:10.1016/j.ajhg.2011.09.014. PMC 3213395 . PMID 21996275.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000165458 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032737 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8530088-5] 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.

[entrez-6] 1 2 "Entrez Gene: INPPL1 inositol polyphosphate phosphatase-like 1".

[pmid11158326-7] Prasad N, Topping RS, Decker SJ (February 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. PMC 99593 . PMID 11158326.

[pmid11739414-8] Dyson JM, O'Malley CJ, Becanovic J, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA (December 2001). "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. PMC 2150887 . PMID 11739414.

[pmid10194451-9] Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, 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. 93 (8): 2707–20. doi:10.1182/blood.V93.8.2707. PMID 10194451.

[pmid11349134-10] 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. 276 (30): 28348–55. doi: 10.1074/jbc.M103537200 . PMID 11349134.

[pmid9660833-11] Habib T, Hejna JA, Moses RE, Decker SJ (July 1998). "Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein". J. Biol. Chem. 273 (29): 18605–9. doi: 10.1074/jbc.273.29.18605 . PMID 9660833.

[pmid12504111-12] Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I (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. 300 (2): 494–500. doi:10.1016/s0006-291x(02)02894-2. PMID 12504111.

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INPPL1

Contents

Interactions

Related Research Articles

References

Further reading