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Search results 501 to 510 out of 510 for Mtmr7

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Type

Details

Score

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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HT Experiment

E-GEOD-14059 | Transcription profiling of mouse heterozygous periphilin knockouts compared to wt littermates

Series Id:	GSE14059
Experiment Type:	transcription profiling by array
Study Type:	WT vs. Mutant
Source:	ArrayExpress

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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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Publication

23800850 | J:223200

First Author:	Chu PL
Year:	2013
Journal:	Physiol Genomics
Title:	A novel genetic locus modulates infarct volume independently of the extent of collateral circulation.
Volume:	45
Issue:	17
Pages:	751-63

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