Varaico: Literature-Extracted Genetic Variants

Gene:MTMR3
Variant:p.C413S
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MTMR3

NM_021090.4:p.C413S

Associated Papers

MTMR regulates KRAS function by controlling plasma membrane levels of phospholipids.

Lange TE et al.

Biorxiv : the Preprint Server for Biology, 2025

STEEP mediates STING ER exit and activation of signaling.

Zhang BC et al.

Nature Immunology, 2020

32690950 (PubMed )
Supplement: EMS117976-supplement-Statistical_Source_Data_ED_Fig_6.xlsx › Fig_S6f

The PtdIns3-phosphatase MTMR3 interacts with mTORC1 and suppresses its activity.

Hao F et al.

Febs Letters, 2016

Myotubularin-related proteins 3 and 4 interact with polo-like kinase 1 and centrosomal protein of 55 kDa to ensure proper abscission.

St-Denis N et al.

Molecular & Cellular Proteomics : Mcp, 2015

PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex.

He S et al.

Nature Cell Biology, 2013

The PTEN and Myotubularin phosphoinositide 3-phosphatases: linking lipid signalling to human disease.

Davies EM et al.

Sub-cellular Biochemistry, 2012

Charcot-Marie-Tooth type 4B demyelinating neuropathy: deciphering the role of MTMR phosphatases.

Previtali SC et al.

Expert Reviews in Molecular Medicine, 2007

Myotubularin phosphatases: policing 3-phosphoinositides.

Robinson FL et al.

Trends in Cell Biology, 2006

Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions.

Lorenzo O et al.

Journal of Cell Science, 2006

The myotubularin family of lipid phosphatases.

Clague MJ et al.

Traffic (copenhagen, Denmark), 2005

Analysis of phosphoinositide binding domain properties within the myotubularin-related protein MTMR3.

Lorenzo O et al.

Journal of Cell Science, 2005

Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity.

Walker DM et al.

Current Biology : Cb, 2001

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Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."