Search results for MTMR2

Showing 18 results out of 27

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Species

Types

Compartments

Reaction types

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Protein (1 results from a total of 1)

Identifier: R-HSA-1604662
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: MTMR2: Q13614

Reaction (6 results from a total of 15)

Identifier: R-HSA-6809785
Species: Homo sapiens
Compartment: cytosol
MTMR2 forms a homodimer (Berger et al. 2006).
Identifier: R-NUL-6810026
Species: Homo sapiens, Mus musculus
Compartment: cytosol
Based on a high throughput study of human interactome in HeLa cells stably expressing tagged mouse Mtmr2 (97% identical to human MTMR2) under the control of mouse Mtmr2 promoter, Mtmr2 forms a complex with endogenous human MTMR10 (Hein et al. 2015).
Identifier: R-HSA-6809793
Species: Homo sapiens
Compartment: cytosol
MTMR2 dimer forms a complex with myotubularin protein SBF2 (MTMR13, an enzymatically inactive myotubularin family member) dimer. Binding to SBF2 sequesters MTMR2 from endosomal membranes to the cytosol (Berger et al. 2006).
Identifier: R-HSA-6809707
Species: Homo sapiens
Compartment: cytosol
MTMR2 forms a complex with MTMR12, an enzymatically inactive myotubularin family member. The consequences of this interaction on enzymatic activity and localization of MTMR2 have not been examined (Nandurkar et al. 2003).
Identifier: R-HSA-6809764
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
MTMR2 forms a heterodimer with SBF1 (MTMR5), an enzymatically inactive myotubularin family member. The interaction of MTMR2 and SBF1 involves coiled-coil domains of both proteins. SBF1 promotes perinuclear localization of MTMR2 (Kim et al. 2003), presumably to the endoplasmic reticulum(ER) membrane, as both proteins can localize to the ER membrane (Berger et al. 2003, Li et al. 2014).
Identifier: R-HSA-6810030
Species: Homo sapiens
Compartment: cytosol
Based on a high throughput study of human interactome in HeLa cells, MTMR2 forms a complex with MTMR10, an enzymatically inactive myotubularin family member. The function of this complex has not been examined (Hein et al. 2015).

Complex (6 results from a total of 6)

Identifier: R-HSA-6809787
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-6809761
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Identifier: R-HSA-6810024
Species: Homo sapiens
Compartment: cytosol
Identifier: R-NUL-6810029
Species: Mus musculus, Homo sapiens
Compartment: cytosol
Identifier: R-HSA-6809705
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-6809791
Species: Homo sapiens
Compartment: cytosol

Set (2 results from a total of 2)

Identifier: R-HSA-1806263
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-1806231
Species: Homo sapiens
Compartment: cytosol

Pathway (3 results from a total of 3)

Identifier: R-HSA-1660517
Species: Homo sapiens
At the late endosome membrane, the primary event is the dephosphorylation of the phosphoinositide phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P) and phosphatidylinositol 5-phosphate (PI5P) (Sbrissa et al. 2007, Sbrissa et al. 2008, Cao et al. 2007, Cao et al. 2008, Arcaro et al. 2000, Kim et al. 2002).
Identifier: R-HSA-1660516
Species: Homo sapiens
At the early endosome membrane, phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) is generated in two steps from phosphatidylinositol 3,4-bisphosphate PI(3,4)P2 by the action of various kinases and phosphatases (Sbrissa et al. 2007, Sbrissa et al. 2008, Cao et al. 2007, Cao et al. 2008, Arcaro et al. 2000, Kim et al. 2002).
Identifier: R-HSA-1660499
Species: Homo sapiens
At the plasma membrane, subsequent phosphorylation of phosphatidylinositol 4-phosphate (PI4P) produces phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) while the actions of various other kinases and phosphatases produces phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 5-phosphate (PI5P), phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2), and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) (Zhang et al. 1997, Gurung et al. 2003, Guo et al. 1999, Vanhaesebroeck et al. 1997, Tolias et al. 1998, Schaletzky et al. 2003, Kim et al. 2002, Clarke et al. 2010). Many of the phosphatidylinositol phosphatases that act at the plasma membrane belong to the myotubularin family. Enzymatically inactive myotubularin family members can heterodimerize with catalytically active mytotubularins to regulate their stability, activity and/or substrate specificity (Berger et al. 2006, Zou et al. 2012).
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