Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Loss of catalytically inactive lipid phosphatase myotubularin-related protein 12 impairs myotubularin stability and promotes centronuclear myopathy in zebrafish.
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Cell and animal experiments distinguish inactive MTMR12 from its catalytically active MTM1 partner and support a protein-stability mechanism.
"MTMR12 primarily regulates the function of myotubularin protein by affecting protein levels instead of modulating the enzymatic activity"
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Partial compensation in zebrafish supports noncatalytic MTMR12 function, not intrinsic phosphoinositide phosphatase activity.
"the catalytically inactive MTMR12 only partially but significantly rescues myotubularin function"
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In mouse skeletal muscle MTMR12 colocalizes with MTM1 at triads and partly with the SR marker RyR1, not with Z-lines.
"The expression of MTMR12 was restricted to triads as no co-localization was observed with α-actinin at Z-lines"
Identification of myotubularin as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein, 3-PAP.
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Human 3-PAP (MTMR12) is catalytically inactive, coprecipitates myotubularin and relocates it from the plasma membrane to the cytosol.
"coexpression of 3-PAP with myotubularin led to attenuation of the plasma membrane phenotype, associated with myotubularin relocalization to the cytosol"
Exact Mtmr12 product-to-reference sequence comparison
Mtmr12 re-review sequence comparison (2026-10-21)
Machine-fetched exact rat MTMR12 record; signal peptide is computational
Frozen exact-input ProtNLM output and UniProt sequence for A0A8I5ZMD5