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Search results 201 to 300 out of 327 for Mtmr6

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Type Details Score
Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
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
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
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).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
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
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
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
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Protein Domain
IPR035998 | MTMR6_PH-GRAM
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.
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Protein
B8JJF6
Organism: Mus musculus/domesticus
Length: 82  
Fragment?: false
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Protein
Q80U24
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: true
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Protein
F6T2Q0
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: true
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Protein Domain
IPR030564 | Myotubularin_fam
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 [].
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Publication
10900271 | -
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
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Publication
11001925 | -
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
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Publication
22578719 | -
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
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Protein
A7M7R1
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
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Protein
A7M7R0
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: true
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Publication
23630283 | J:197327
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
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Publication
23818870 | -
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
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Protein
Q8R3K8
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: true
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Publication
11504939 | -
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
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Publication
22647598 | -
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
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Publication
19325702 | -
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
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Publication
20815916 | -
 
First Author: Mei J
Year: 2010
Journal: BMC Dev Biol
Title: Mtmr8 is essential for vasculature development in zebrafish embryos.
Volume: 10
Pages: 96
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Protein Domain
IPR036003 | MTMR7_PH-GRAM
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.
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Protein Domain
IPR030591 | MTMR8
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 [].
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Protein Domain
IPR030587 | MTMR1
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 [].
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Protein Domain
IPR030572 | MTMR7
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 [].
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Protein Domain
IPR030576 | MTMR12
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 [].
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Publication
16828287 | -
First Author: Robinson FL
Year: 2006
Journal: Trends Cell Biol
Title: Myotubularin phosphatases: policing 3-phosphoinositides.
Volume: 16
Issue: 8
Pages: 403-12
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Publication
16787938 | -
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
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Protein
Q8CIU5
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: true
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Protein
Q8CIU7
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: true
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Protein
F6S251
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
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Protein
I7HPV7
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
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Protein
G3XA69
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
Q8CIU4
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
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Protein
Q8CIU6
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
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Protein
Q8CIU3
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: true
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Publication
20685272 | -
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
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Protein
A0A0U1RQ60
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: false
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Publication
23749797 | -
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
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Publication
12668758 | -
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
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Publication
21175430 | -
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
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Publication
20576132 | -
 
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
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Protein Domain
IPR037857 | MTMR1_PH-GRAM
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 [].
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Protein Domain
IPR030590 | MTMR4
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 [].
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Protein Domain
IPR030574 | MTMR5
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 [].
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Protein
B8JJF3
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
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Protein
G3UYB7
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: true
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Protein
Q8C489
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: true
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Protein
Q5ND05
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: true
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Protein
F6T9H9
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: true
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Protein
F6QG63
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
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Protein
Q3UDN6
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Publication
12847286 | -
First Author: Nandurkar HH
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Identification of myotubularin as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein, 3-PAP.
Volume: 100
Issue: 15
Pages: 8660-5
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Publication
26143924 | -
First Author: Yoo KY
Year: 2015
Journal: Acta Crystallogr D Biol Crystallogr
Title: Structure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidation.
Volume: 71
Issue: Pt 7
Pages: 1528-39
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Publication
23150675 | -
First Author: Yu J
Year: 2013
Journal: J Biol Chem
Title: Myotubularin-related protein 4 (MTMR4) attenuates BMP/Dpp signaling by dephosphorylation of Smad proteins.
Volume: 288
Issue: 1
Pages: 79-88
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Publication
20061380 | -
First Author: Yu J
Year: 2010
Journal: J Biol Chem
Title: MTMR4 attenuates transforming growth factor beta (TGFbeta) signaling by dephosphorylating R-Smads in endosomes.
Volume: 285
Issue: 11
Pages: 8454-62
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Publication
12925573 | -
 
First Author: Laporte J
Year: 2003
Journal: Hum Mol Genet
Title: Myotubularins, a large disease-associated family of cooperating catalytically active and inactive phosphoinositides phosphatases.
Volume: 12 Spec No 2
Pages: R285-92
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Publication
20736309 | -
First Author: Naughtin MJ
Year: 2010
Journal: J Cell Sci
Title: The myotubularin phosphatase MTMR4 regulates sorting from early endosomes.
Volume: 123
Issue: Pt 18
Pages: 3071-83
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Publication
11302699 | -
First Author: Zhao R
Year: 2001
Journal: Exp Cell Res
Title: FYVE-DSP2, a FYVE domain-containing dual specificity protein phosphatase that dephosphorylates phosphotidylinositol 3-phosphate.
Volume: 265
Issue: 2
Pages: 329-38
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Protein
Q80TA6
Organism: Mus musculus/domesticus
Length: 747  
Fragment?: false
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Protein
G3UZ04
Organism: Mus musculus/domesticus
Length: 526  
Fragment?: false
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Protein
F7AWK3
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: true
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Protein
Q9Z2C9
Organism: Mus musculus/domesticus
Length: 660  
Fragment?: false
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Protein
Q9Z2C4
Organism: Mus musculus/domesticus
Length: 669  
Fragment?: false
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Protein
I6L9A6
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
I7HJQ9
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
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Protein
G3V027
Organism: Mus musculus/domesticus
Length: 498  
Fragment?: false
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Protein
D6RG52
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
Q8BQ73
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: true
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Protein
G3UYZ2
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: true
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Protein
H3BKD9
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: true
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Protein
Q6PE02
Organism: Mus musculus/domesticus
Length: 902  
Fragment?: false
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Protein
Q9Z2D0
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
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Protein
Q7TPM9
Organism: Mus musculus/domesticus
Length: 771  
Fragment?: false
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Protein
Q3V1L6
Organism: Mus musculus/domesticus
Length: 700  
Fragment?: false
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Protein
D6RIK1
Organism: Mus musculus/domesticus
Length: 273  
Fragment?: false
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Protein
Q3V415
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: true
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Protein
Q3U896
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
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Protein
Q8CCE6
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
Q8CD00
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
F7BBM8
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: true
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Protein
A0A286YE22
Organism: Mus musculus/domesticus
Length: 139  
Fragment?: true
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Protein
Q8CEB8
Organism: Mus musculus/domesticus
Length: 335  
Fragment?: false
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Protein
F6ZDC5
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: true
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Protein
F6QZ02
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: true
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Protein
Q9Z2D2
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: true
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Publication
20937701 | -
First Author: Yoshimura S
Year: 2010
Journal: J Cell Biol
Title: Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors.
Volume: 191
Issue: 2
Pages: 367-81
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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