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Search results 301 to 327 out of 327 for Mtmr3

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0.017s

Type

Details

Score

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: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

Q9Z2D0

Organism:	Mus musculus/domesticus
Length:	545
Fragment?:	false

•

Publication

15840652 | -

First Author:	Lorenzo O
Year:	2005
Journal:	J Cell Sci
Title:	Analysis of phosphoinositide binding domain properties within the myotubularin-related protein MTMR3.
Volume:	118
Issue:	Pt 9
Pages:	2005-12

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Protein Domain

IPR035888 | MTMR3_PH-GRAM

Type:

Domain

Description:

MTMR3 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR3 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro []. The protein can self-associate and also form heteromers with MTMR4 [].Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome []. Six of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules []. This entry represents the PH-GRAM domain of myotubularin-related protein 3.

•

Publication

16289848 | -

First Author:	Begley MJ
Year:	2005
Journal:	Curr Opin Struct Biol
Title:	The structure and regulation of myotubularin phosphatases.
Volume:	15
Issue:	6
Pages:	614-20

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Publication

11676921 | -

First Author:	Walker DM
Year:	2001
Journal:	Curr Biol
Title:	Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity.
Volume:	11
Issue:	20
Pages:	1600-5

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Publication

10733931 | -

First Author:	Zhao R
Year:	2000
Journal:	Biochem Biophys Res Commun
Title:	FYVE-DSP1, a dual-specificity protein phosphatase containing an FYVE domain.
Volume:	270
Issue:	1
Pages:	222-9

•

Publication

25659891 | -

First Author:	St-Denis N
Year:	2015
Journal:	Mol Cell Proteomics
Title:	Myotubularin-related proteins 3 and 4 interact with polo-like kinase 1 and centrosomal protein of 55 kDa to ensure proper abscission.
Volume:	14
Issue:	4
Pages:	946-60

•

Protein Domain

IPR046352 | MTMR3_Pase_dom

Type:

Domain

Description:

This entry represents the phosphatase domain of Myotubularin-related protein 3 (Mtmf3). Proteins in this entry are specific to chordates. Mtmr3 is a phosphatase that acts on lipids with a phosphoinositol head-group such as phosphatidyl-inositol 3-phosphate and phosphatidyl-inositol 3,5-bisphosphate []. It may also de-phosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues []. This enzyme has shown to play a regulatory role in the regulation of abscission, the final step of mitosis [], and innate immune responses to viral DNA through the modulation of STING trafficking [].

•

Publication

15998640 | -

First Author:	Robinson FL
Year:	2005
Journal:	J Biol Chem
Title:	The phosphoinositide-3-phosphatase MTMR2 associates with MTMR13, a membrane-associated pseudophosphatase also mutated in type 4B Charcot-Marie-Tooth disease.
Volume:	280
Issue:	36
Pages:	31699-707

•

Publication

25195910 | -

First Author:	Lee JU
Year:	2014
Journal:	Acta Crystallogr F Struct Biol Commun
Title:	Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4.
Volume:	70
Issue:	Pt 9
Pages:	1280-3

•

Protein Domain

IPR035997 | MTMR4_PH-GRAM

Type:

Domain

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 [].Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome []. Six of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules []. 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 myotubularin-related protein 4.

•

Protein

M0QW74

Organism:	Mus musculus/domesticus
Length:	1075
Fragment?:	false

•

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

•

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

•

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

•

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

•

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

Q8K296

Organism:	Mus musculus/domesticus
Length:	1196
Fragment?:	false

•

Protein

R4GML8

Organism:	Mus musculus/domesticus
Length:	1195
Fragment?:	true

•

Protein

B1ATD5

Organism:	Mus musculus/domesticus
Length:	1159
Fragment?:	false

•

Protein

B1ATD4

Organism:	Mus musculus/domesticus
Length:	1167
Fragment?:	true

•

Protein

Q66I45

Organism:	Mus musculus/domesticus
Length:	1159
Fragment?:	false

•

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

•

Protein

Q91XS1

Organism:	Mus musculus/domesticus
Length:	1190
Fragment?:	false

•

Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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