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Search results 101 to 200 out of 260 for Mtm1

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Type Details Score
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication
First Author: Gaudet P
Year: 2011
Journal: Brief Bioinform
Title: Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium.
Volume: 12
Issue: 5
Pages: 449-62
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
DO Term
Allele
Name: X-linked myotubular myopathy gene 1; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Transgene
Type: transgene
Organism: mouse, laboratory
HT Experiment  
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
Publication
First Author: Wang Y
Year: 2021
Journal: Nature
Title: SLC25A39 is necessary for mitochondrial glutathione import in mammalian cells.
Volume: 599
Issue: 7883
Pages: 136-140
Publication
First Author: Tsujita K
Year: 2004
Journal: J Biol Chem
Title: Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction.
Volume: 279
Issue: 14
Pages: 13817-24
Publication  
First Author: Whittaker MM
Year: 2015
Journal: Arch Biochem Biophys
Title: The Mtm1p carrier and pyridoxal 5'-phosphate cofactor trafficking in yeast mitochondria.
Volume: 568
Pages: 64-70
Protein Domain
Type: Family
Description: This entry represents a group of mitochondrial carrier proteins, including Mtm1 from budding yeasts and SLC25A39/40 from humans. Mtm1 is apyridoxal 5'-phosphate (PLP) transporter and is involved in mitochondrial iron homeostasis []. SLC25A39 and its paralogue SLC25A40 are mitochondrial transporters essential for glutathione import into mitochondria, which is required for the activity and stability of proteins containing iron-sulfur clusters, as well as erythropoiesis []. Knockdown of SLC25A39 in a zebrafish model has been shown to disrupt heme biosynthesis and results in profound anemia [].
Protein Domain
Type: Family
Description: Myotubularin (MTM1) is a lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) [, ]. Myotubularin is essential in adult muscle []. MTM1 is involved in sarcoplasmic reticulum (SR) remodelling and promoting SR membrane curvature in skeletal muscle []. It also controls desmin intermediate filament architecture and mitochondrial dynamics in skeletal muscle [], and functions in late endosomal trafficking and vacuolar morphology [].Mutation in MTM1 cause X-linked centronuclear myopathy (XLCNM), a congenital muscle disorder characterised by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles [, ].
Publication
First Author: de Gouyon B
Year: 1996
Journal: Mamm Genome
Title: Comparative mapping on the mouse X chromosome defines a myotubular myopathy equivalent region.
Volume: 7
Issue: 8
Pages: 575-9
Publication
First Author: Nilsson R
Year: 2009
Journal: Cell Metab
Title: Discovery of genes essential for heme biosynthesis through large-scale gene expression analysis.
Volume: 10
Issue: 2
Pages: 119-30
Protein
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
Publication
First Author: Luo S
Year: 2021
Journal: Hum Mol Genet
Title: SPEG binds with desmin and its deficiency causes defects in triad and focal adhesion proteins.
Volume: 29
Issue: 24
Pages: 3882-3891
Publication
First Author: Reifler A
Year: 2014
Journal: Am J Pathol
Title: Conditional knockout of pik3c3 causes a murine muscular dystrophy.
Volume: 184
Issue: 6
Pages: 1819-30
Publication
First Author: Ketel K
Year: 2016
Journal: Nature
Title: A phosphoinositide conversion mechanism for exit from endosomes.
Volume: 529
Issue: 7586
Pages: 408-12
Publication
First Author: Chen X
Year: 2020
Journal: J Biol Chem
Title: The intragenic microRNA miR199A1 in the dynamin 2 gene contributes to the pathology of X-linked centronuclear myopathy.
Volume: 295
Issue: 26
Pages: 8656-8667
Protein
Organism: Mus musculus/domesticus
Length: 82  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: true
Protein Domain
Type: Family
Description: The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].
Publication
First Author: Buj-Bello A
Year: 2002
Journal: Hum Mol Genet
Title: Muscle-specific alternative splicing of myotubularin-related 1 gene is impaired in DM1 muscle cells.
Volume: 11
Issue: 19
Pages: 2297-307
Publication
First Author: Reifler A
Year: 2013
Journal: Skelet Muscle
Title: Murine Fig4 is dispensable for muscle development but required for muscle function.
Volume: 3
Issue: 1
Pages: 21
Protein
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
Publication
First Author: Taylor GS
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate.
Volume: 97
Issue: 16
Pages: 8910-5
Publication
First Author: Blondeau F
Year: 2000
Journal: Hum Mol Genet
Title: Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway.
Volume: 9
Issue: 15
Pages: 2223-9
Publication
First Author: Mochizuki Y
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9.
Volume: 100
Issue: 17
Pages: 9768-73
Protein
Organism: Mus musculus/domesticus
Length: 337  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: true
Publication
First Author: Guo L
Year: 2013
Journal: Proc Natl Acad Sci U S A
Title: Lipid phosphatases identified by screening a mouse phosphatase shRNA library regulate T-cell differentiation and protein kinase B AKT signaling.
Volume: 110
Issue: 20
Pages: E1849-56
Publication
First Author: Gupta VA
Year: 2013
Journal: PLoS Genet
Title: Loss of catalytically inactive lipid phosphatase myotubularin-related protein 12 impairs myotubularin stability and promotes centronuclear myopathy in zebrafish.
Volume: 9
Issue: 6
Pages: e1003583
Protein
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: true
Publication
First Author: Nandurkar HH
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: Characterization of an adapter subunit to a phosphatidylinositol (3)P 3-phosphatase: identification of a myotubularin-related protein lacking catalytic activity.
Volume: 98
Issue: 17
Pages: 9499-504
Publication
First Author: Zou J
Year: 2012
Journal: Proc Natl Acad Sci U S A
Title: Myotubularin-related protein (MTMR) 9 determines the enzymatic activity, substrate specificity, and role in autophagy of MTMR8.
Volume: 109
Issue: 24
Pages: 9539-44
Publication
First Author: Mei J
Year: 2009
Journal: PLoS One
Title: Cooperation of Mtmr8 with PI3K regulates actin filament modeling and muscle development in zebrafish.
Volume: 4
Issue: 3
Pages: e4979
Publication  
First Author: Mei J
Year: 2010
Journal: BMC Dev Biol
Title: Mtmr8 is essential for vasculature development in zebrafish embryos.
Volume: 10
Pages: 96
Protein Domain
Type: Domain
Description: Myotubularin-related protein 7 (MTMR7) is a member of the myotubularin (MTM) family. MTMR9 is a binding partner of MTMR7, and binding of MTMR9 increases the phosphatase activity of MTMR7 []. MTMR9 and MTMR7 may be involved in regulating T-helper (Th) cells differentiation [].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].MTMR7 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. This entry represents the PH-GRAM domain of MTMR7.
Protein Domain
Type: Family
Description: Myotubularin-related protein 8 (MTMR8) is a catalytically active member of the myotubularin (MTM) family, which possess 3-phosphatase activity dephosphorylating phosphatidylinositol-3-phoshate [PI(3)P]and phosphatidylinositol-3,5-bisphosphate [PI(3,5)P]. MTMR8 dimerises with the catalytically inactive MTMR9. Complex formation increases its catalytic activity and alters the substrate specificity; the MTMR8/R9 complex prefers PI(3)P as a substrate and reduces cellular PtdIns(3)P levels [, ]. The MTMR8/R9 complex inhibits autophagy []. In zebrafish, MTMR8 has been shown to cooperate with PI3K to regulate actin filament modeling, and vascular and muscle development [, ].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].
Protein Domain
Type: Family
Description: MTMR1 (myotubularin-related protein 1) is a lipid phosphatase that uses phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2]as substrates []. MTMR1 is abnormally expressed in myotonic dystrophy type1 (DM1) and in myotonic dystrophy type 2 (DM2), in correlation with muscle pathological features [].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].
Protein Domain
Type: Family
Description: Myotubularin-related protein 7 (MTMR7) is a member of the myotubularin (MTM) family. MTMR9 is a binding partner of MTMR7, and binding of MTMR9 increases the phosphatase activity of MTMR7 []. MTMR9 and MTMR7 may be involved in regulating T-helper (Th) cells differentiation [].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, sixof the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].
Protein Domain
Type: Family
Description: Myotubularin-related protein 12 (MTMR12), also known 3-phosphatase adapter protein (3-PAP), belongs to the myotubularin family. It is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularin intracellular location [, ]. Knockdown of the mtmr12 gene in zebrafish results in skeletal muscle defects and impaired motor function [].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].
Publication
First Author: Hnia K
Year: 2012
Journal: Trends Mol Med
Title: Myotubularin phosphoinositide phosphatases: cellular functions and disease pathophysiology.
Volume: 18
Issue: 6
Pages: 317-27
Protein
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: true
Publication
First Author: Santoro M
Year: 2010
Journal: Exp Mol Pathol
Title: Analysis of MTMR1 expression and correlation with muscle pathological features in juvenile/adult onset myotonic dystrophy type 1 (DM1) and in myotonic dystrophy type 2 (DM2).
Volume: 89
Issue: 2
Pages: 158-68
Protein
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: false
Publication
First Author: Nakhro K
Year: 2013
Journal: Neurology
Title: SET binding factor 1 (SBF1) mutation causes Charcot-Marie-Tooth disease type 4B3.
Volume: 81
Issue: 2
Pages: 165-73
Publication
First Author: Kim SA
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Regulation of myotubularin-related (MTMR)2 phosphatidylinositol phosphatase by MTMR5, a catalytically inactive phosphatase.
Volume: 100
Issue: 8
Pages: 4492-7
Publication
First Author: Mruk DD
Year: 2011
Journal: Biochem J
Title: The myotubularin family of lipid phosphatases in disease and in spermatogenesis.
Volume: 433
Issue: 2
Pages: 253-62
Publication  
First Author: Kerk D
Year: 2010
Journal: BMC Evol Biol
Title: A phylogenetic survey of myotubularin genes of eukaryotes: distribution, protein structure, evolution, and gene expression.
Volume: 10
Pages: 196
Protein Domain
Type: Domain
Description: MTMR1 (myotubularin-related protein 1) is a lipid phosphatase that uses phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2]as substrates []. MTMR1 is abnormally expressed in myotonic dystrophy type1 (DM1) and in myotonic dystrophy type 2 (DM2), in correlation with muscle pathological features [].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region []. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold [].
Protein Domain
Type: Family
Description: Myotubularin-related protein 4 (MTMR4) is a member of the myotubularin (MTM) family. It is the only family member that possesses a FYVE domain (a zinc finger domain) at its C terminus []. MTMR4 has dual-specificity phosphatase activity []; some studies have shown that it can dephosphorylate PI3P or PI(3,5)P2, suggesting that MTMR4 is also a lipid phosphatase []. MTMR4 has a unique distribution to endosomes []and has been shown to function in early and recycling endosomes [, ]. MTMR4 attenuates TGF-beta signalling by dephosphorylating intracellular signalling mediator R-Smads []. Similarly, it acts as a negative modulator for the homeostasis of bone morphogenetic proteins (BMPs) signalling [].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].
Protein Domain
Type: Family
Description: Myotubularin-related protein 5 (MTMR5), also known as SET-binding factor 1 (SBF1), belongs to the myotubularin family and is a pseudophosphatase. It lacks several amino acids in the catalytic pocket which renders it catalytically inactive as a phosphatase. It interacts with MTMR2. Through this interaction, MTMR5 increases the enzymatic activity of MTMR2 and dictates its subcellular localisation []. MTMR2 and MTMR5 are highly expressed in the testis, and could have a role in spermatogenesis []. MTMR5 may also function as a guanine nucleotide exchange factor (GEF) that activates Rab28 (a Rab GTPase) []. Mutations in MTMR5/SBF1 cause Charcot-Marie-Tooth disease type 4B3 (CMT4B3), which is a disorder of the peripheral nervous system [].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].
Protein Domain
Type: Domain
Description: Myotubularin-related protein 6 (MTMR6) is a catalytically active member of the myotubularin (MTM) family, which possess 3-phosphatase activity dephosphorylating phosphatidylinositol-3-phoshate and phosphatidylinositol-3,5-bisphosphate. MTMR6 forms a heteromer with enzymatically inactive MTMR9. MTMR9 increases MTMR6 binding to phospholipids and increases the 3-phosphatase activity of MTMR6 []. MTMR6 is reported to be involved in the regulation of the Ca2+-activated K+ channel KCa3.1 []and apoptosis []. The cellular localisation of MTMR6 is regulated by Rab1B in the early secretory and autophagic pathways [].The myotubularin family constitutes a large group of conserved proteins, with 14 members in humans consisting of myotubularin (MTM1) and 13 myotubularin-related proteins (MTMR1-MTMR13). Orthologues have been found throughout the eukaryotic kingdom, but not in bacteria. MTM1 dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) to phosphatidylinositol and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2]to phosphatidylinositol 5-monophosphate (PI5P) [, ]. The substrate phosphoinositides (PIs) are known to regulate traffic within the endosomal-lysosomal pathway []. MTMR1, MTMR2, MTMR3, MTMR4, and MTMR6 have also been shown to utilise PI(3)P as a substrate, suggesting that this activity is intrinsic to all active family members. On the other hand, six of the MTM family members encode for catalytically inactive phosphatases. Inactive myotubularin phosphatases contain substitutions in the Cys and Arg residues of the Cys-X5-Arg motif. MTM pseudophosphatases have been found to interact with MTM catalytic phosphatases []. The myotubularin family includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer [].MTMR6 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. This entry represents the PH-GRAM domain of MTMR6.
Protein
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
Publication
First Author: Robinson FL
Year: 2006
Journal: Trends Cell Biol
Title: Myotubularin phosphatases: policing 3-phosphoinositides.
Volume: 16
Issue: 8
Pages: 403-12
Publication
First Author: Lorenzo O
Year: 2006
Journal: J Cell Sci
Title: Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions.
Volume: 119
Issue: Pt 14
Pages: 2953-9
Publication
First Author: Mochizuki Y
Year: 2013
Journal: J Biol Chem
Title: Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6) is regulated by small GTPase Rab1B in the early secretory and autophagic pathways.
Volume: 288
Issue: 2
Pages: 1009-21
Protein
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
Publication
First Author: Srivastava S
Year: 2005
Journal: Mol Cell Biol
Title: The phosphatidylinositol 3-phosphate phosphatase myotubularin- related protein 6 (MTMR6) is a negative regulator of the Ca2+-activated K+ channel KCa3.1.
Volume: 25
Issue: 9
Pages: 3630-8
Publication
First Author: Zou J
Year: 2009
Journal: J Biol Chem
Title: MTMR9 increases MTMR6 enzyme activity, stability, and role in apoptosis.
Volume: 284
Issue: 4
Pages: 2064-71
Protein
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 572  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: true