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Literature summary extracted from

  • Vergne, I.; Deretic, V.
    The role of PI3P phosphatases in the regulation of autophagy (2010), FEBS Lett., 584, 1313-1318.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.64 type III PI3K regulatory subunit hVps15 i.e. p150, MTMR2 binding results in inhibition of phosphatase activity and in diminution of hVps34-Rab7 interaction important for PI3P synthesis Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.64 endosome MTM1 is present on ruffles at the plasma membrane, on early endosomes and partially on late endosomes Homo sapiens 5768
-
3.1.3.64 intracellular
-
 Mus musculus 5622
-
3.1.3.64 intracellular
-
 Homo sapiens 5622
-
3.1.3.64 intracellular
-
 Saccharomyces cerevisiae 5622
-
3.1.3.64 plasma membrane MTM1 is present on ruffles at the plasma membrane, on early endosomes and partially on late endosomes Homo sapiens 5886
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O Mus musculus
-
 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O Homo sapiens
-
 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O Saccharomyces cerevisiae
-
 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O Mus musculus
-
 1-phosphatidyl-1D-myo-inositol + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O Homo sapiens
-
 1-phosphatidyl-1D-myo-inositol + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O Saccharomyces cerevisiae
-
 1-phosphatidyl-1D-myo-inositol + phosphate
-
 ?
3.1.3.64 additional information Mus musculus MTMR1, MTMR2, MTMR3, MTMR4, MTMR6, MTMR7, MTMR8 and Jumpy (also known as MTMR14), possess an active phosphatase domain, that specifically dephosphorylates 1-phosphatidyl-1D-myo-inositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate at position 3 on inositol ring ?
-
 ?
3.1.3.64 additional information Homo sapiens MTMR1, MTMR2, MTMR3, MTMR4, MTMR6, MTMR7, MTMR8 and Jumpy (also known as MTMR14), possess an active phosphatase domain, that specifically dephosphorylates 1-phosphatidyl-1D-myo-inositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate at position 3 on inositol ring ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.64 Homo sapiens
-
-
-
3.1.3.64 Mus musculus
-
-
-
3.1.3.64 Saccharomyces cerevisiae
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.64 neuron
-
 Mus musculus
-
3.1.3.64 neuron
-
 Homo sapiens
-
3.1.3.64 Schwann cell
-
 Homo sapiens
-
3.1.3.64 skeletal muscle
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
-
 Mus musculus 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
-
 Homo sapiens 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
-
 Saccharomyces cerevisiae 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O
-
 Mus musculus 1-phosphatidyl-1D-myo-inositol + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O
-
 Homo sapiens 1-phosphatidyl-1D-myo-inositol + phosphate
-
 ?
3.1.3.64 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O
-
 Saccharomyces cerevisiae 1-phosphatidyl-1D-myo-inositol + phosphate
-
 ?
3.1.3.64 additional information MTMR1, MTMR2, MTMR3, MTMR4, MTMR6, MTMR7, MTMR8 and Jumpy (also known as MTMR14), possess an active phosphatase domain, that specifically dephosphorylates 1-phosphatidyl-1D-myo-inositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate at position 3 on inositol ring Mus musculus ?
-
 ?
3.1.3.64 additional information MTMR1, MTMR2, MTMR3, MTMR4, MTMR6, MTMR7, MTMR8 and Jumpy (also known as MTMR14), possess an active phosphatase domain, that specifically dephosphorylates 1-phosphatidyl-1D-myo-inositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate at position 3 on inositol ring Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.64 More domain structure of the myotubularin family members, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.3.64 More the enzyme belongs to the myotubularin family Mus musculus
3.1.3.64 More the enzyme belongs to the myotubularin family Homo sapiens
3.1.3.64 More the enzyme belongs to the myotubularin family Saccharomyces cerevisiae
3.1.3.64 MTMR1
-
 Mus musculus
3.1.3.64 MTMR1
-
 Homo sapiens
3.1.3.64 MTMR14
-
 Mus musculus
3.1.3.64 MTMR14
-
 Homo sapiens
3.1.3.64 MTMR2
-
 Mus musculus
3.1.3.64 MTMR2
-
 Homo sapiens
3.1.3.64 MTMR3
-
 Mus musculus
3.1.3.64 MTMR3
-
 Homo sapiens
3.1.3.64 MTMR4
-
 Mus musculus
3.1.3.64 MTMR4
-
 Homo sapiens
3.1.3.64 MTMR6
-
 Mus musculus
3.1.3.64 MTMR6
-
 Homo sapiens
3.1.3.64 MTMR7
-
 Mus musculus
3.1.3.64 MTMR7
-
 Homo sapiens
3.1.3.64 MTMR8
-
 Mus musculus
3.1.3.64 MTMR8
-
 Homo sapiens
3.1.3.64 myotubularin
-
 Mus musculus
3.1.3.64 myotubularin
-
 Homo sapiens
3.1.3.64 myotubularin
-
 Saccharomyces cerevisiae
3.1.3.64 PI3P phosphatase
-
 Mus musculus
3.1.3.64 PI3P phosphatase
-
 Homo sapiens
3.1.3.64 Ymr1p
-
 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
3.1.3.64 malfunction four of the fifteen PI3P phosphatases present in mammals have been linked to serious human diseases. MTM1 defects cause X-linked myotubular myopathy also known as centronuclear myopathy, a severe congenital disorder affecting the physiology of skeletal muscle fibers and characterized by centrally localized nuclei and hypotonia. More than two hundred different mutations, truncations and missenses, in MTM1 are reported in XLMTM patients that result in loss or decrease of MTM1 level. MTMR2 and MTMR13 are mutated in two forms of Charcot-Marie-Tooth type 4B, CMT type 4, disease, an autosomal recessive disorder of the peripheral nervous system characterized by nerve demyelination and myelin outfoldings. CMT type 4B1 is caused by missense or deletion mutations in MTMR2 gene that result in MTMR2 loss of function. In addition to CMT4B1, one patient manifests azoospermia suggesting that MTMR2 also plays a role in testis Homo sapiens
3.1.3.64 malfunction MTMR2-deficient mice develop CMT4B1-like neuropathy and azoospermia. MTMR13-deficient mice manifest myelin outfoldings in peripheral nerves. Jumpy or MTMR14-/- mice display muscle weakness and fatigue similar to patients with centronuclear myopathy Mus musculus
3.1.3.64 metabolism autophagy initiation is strictly dependent on phosphatidylinositol 3-phosphate synthesis. PI3P production is under tight control of PI3Kinase, hVps34, in complex with Beclin-1. PI3P metabolism involved in autophagy initiation is further regulated by the PI3P phosphatases Jumpy and MTMR3, and other PI3P phosphatases might be involved in this process Mus musculus
3.1.3.64 metabolism autophagy initiation is strictly dependent on phosphatidylinositol 3-phosphate synthesis. PI3P production is under tight control of PI3Kinase, hVps34, in complex with Beclin-1. PI3P metabolism involved in autophagy initiation is further regulated by the PI3P phosphatases Jumpy and MTMR3, and other PI3P phosphatases might be involved in this process Homo sapiens
3.1.3.64 additional information PI3P is a substrate for PIP5-kinase, Fab1, also named PIKfyve, an enzyme that generates phosphoinositide 1-phosphatidyl-1D-myo-inositol 3,5-diphosphate Mus musculus
3.1.3.64 additional information PI3P is a substrate for PIP5-kinase, Fab1, also named PIKfyve, an enzyme that generates phosphoinositide 1-phosphatidyl-1D-myo-inositol 3,5-diphosphate Homo sapiens
3.1.3.64 physiological function the enzyme plays central role in autophagy, overview Saccharomyces cerevisiae
3.1.3.64 physiological function the enzyme plays central role in autophagy, overview. MTM1 might be involved in membrane traffic and regulates intracellular trafficking of Glut-4 and EGF receptor, respectively, on ruffles at the plasma membrane, on early endosomes and partially on late endosomes. In muscle fibers, MTMR14 regulates Ca2+ homeostasis by dephosphorylating PI3,5P2, an activator of Ca2+ release channel ryanodine receptor 1. In Schwann cells MTMR2 plays an important role in membrane homeostasis at the plasma membrane during the process of myelination. MTMR2 binds to type III PI3K regulatory subunit, hVps15 (p150), which results in inhibition of phosphatase activity and in diminution of hVps34-Rab7 interaction important for PI3P synthesis. Regulation and cellular functions of PI3P phosphatases, protein interacting partners of active PI3P phosphatases, overview Homo sapiens
3.1.3.64 physiological function the enzyme plays central role in autophagy, overview. Regulation and cellular functions of PI3P phosphatases, protein interacting partners of active PI3P phosphatases, overview Mus musculus