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Search results 101 to 126 out of 126 for Mtmr9

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Type Details Score
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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Publication
19038970 | -
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
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Protein Domain
IPR030581 | MTMR6
Type: Family
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 [].
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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
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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Publication
23188820 | -
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
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Publication
15831468 | -
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
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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
G3UYB7
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: true
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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
Q9Z2C9
Organism: Mus musculus/domesticus
Length: 660  
Fragment?: false
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Protein
I6L9A6
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
G3V027
Organism: Mus musculus/domesticus
Length: 498  
Fragment?: false
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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
G3UYZ2
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: true
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Protein
Q8VE11
Organism: Mus musculus/domesticus
Length: 617  
Fragment?: false
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