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

Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase (EC 3.1.3.86, SHIP1, SHIP2, SHIP, p150Ship) is an enzyme with systematic name 1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 5-phosphohydrolase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H₂O

\rightleftharpoons

1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate

This enzyme hydroylses 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2.

References

↑ Lioubin, M.N.; Algate, P.A.; Tsai, S.; Carlberg, K.; Aebersold, A.; Rohrschneider, L.R. (1996). "p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity". Genes Dev. 10: 1084–1095. doi:10.1101/gad.10.9.1084. PMID 8654924.
↑ Damen, J.E.; Liu, L.; Rosten, P.; Humphries, R.K.; Jefferson, A.B.; Majerus, P.W.; Krystal, G. (1996). "The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase". Proc. Natl. Acad. Sci. USA. 93: 1689–1693. doi:10.1073/pnas.93.4.1689. PMC 40003. PMID 8643691.
↑ Giuriato, S.; Payrastre, B.; Drayer, A.L.; Plantavid, M.; Woscholski, R.; Parker, P.; Erneux, C.; Chap, H. (1997). "Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets". J. Biol. Chem. 272: 26857–26863. doi:10.1074/jbc.272.43.26857. PMID 9341117.
↑ Drayer, A.L.; Pesesse, X.; De Smedt, F.; Woscholski, R.; Parker, P.; Erneux, C. (1996). "Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase". Biochem. Biophys. Res. Commun. 225: 243–249. doi:10.1006/bbrc.1996.1161. PMID 8769125.
↑ Pesesse, X.; Moreau, C.; Drayer, A.L.; 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): 301–303. doi:10.1016/S0014-5793(98)01255-1. PMID 9824312.

External links

Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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