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Acyl-CoA thioesterase 13

THEM2, thioesterase superfamily member 2, acyl-CoA thioesterase 13, Acot13
This gene encodes a member of the thioesterase superfamily. In humans, the protein co-localizes with microtubules and is essential for sustained cell proliferation. The orthologous mouse protein forms a homotetramer and is associated with mitochondria. The mouse protein functions as a medium- and long-chain acyl-CoA thioesterase. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, May 2009] (from NCBI)
Top mentioned proteins: PC-TP, ACID, TTRAP, Insulin, XRCC1
Papers on THEM2
Crystal structure and potential physiological role of zebra fish thioesterase superfamily member 2 (fTHEM2).
New
Zhou et al., Beijing, China. In Biochem Biophys Res Commun, Sep 2015
Thioesterase superfamily member 2 (THEM2) is an essential protein for mammalian cell proliferation.
Thioesterase superfamily member 2 (Them2) and phosphatidylcholine transfer protein (PC-TP) interact to promote fatty acid oxidation and control glucose utilization.
Cohen et al., Boston, United States. In Mol Cell Biol, 2014
Thioesterase superfamily member 2 (Them2) is a mitochondrion-associated long-chain fatty acyl coenzyme A (CoA) thioesterase that is highly expressed in the liver and oxidative tissues.
Thioesterase superfamily member 2/Acyl-CoA thioesterase 13 (Them2/Acot13) regulates adaptive thermogenesis in mice.
Cohen et al., Boston, United States. In J Biol Chem, 2013
Thioesterase superfamily member 2 (Them2; synonym Acot13) is enriched in oxidative tissues, associated with mitochondria, and relatively specific for long chain fatty acyl-CoA substrates.
Lack of association between genetic polymorphisms in ROBO1, MRPL19/C2ORF3 and THEM2 with developmental dyslexia.
Ramachandra et al., Mysore, India. In Gene, 2013
To identify the role of SNPs of four candidate genes namely, MRPL19/C2ORF3, ROBO1 and THEM2 in an Indian population, we genotyped eight SNPs of these genes in 157 children with DD and 212 normal readers using a MassARRAY technique with a MALDI-TOF MS analyzer.
Phosphatidylcholine transfer protein interacts with thioesterase superfamily member 2 to attenuate insulin signaling.
Cohen et al., Boston, United States. In Sci Signal, 2013
Phosphatidylcholine transfer protein (PC-TP) is a phospholipid-binding protein that is enriched in liver and that interacts with thioesterase superfamily member 2 (THEM2).
Molecular cloning, expression, purification and crystallographic analysis of zebrafish THEM2.
Gong et al., Beijing, China. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013
Thioesterase superfamily member 2 (THEM2) is essential for cell proliferation of mammalian cells.
Thioesterase superfamily member 2/acyl-CoA thioesterase 13 (Them2/Acot13) regulates hepatic lipid and glucose metabolism.
Cohen et al., Boston, United States. In Faseb J, 2012
Thioesterase superfamily member 2 (Them2; synonym Acot13) is a broadly expressed mitochondria-associated Acot.
Genetic variants of FOXP2 and KIAA0319/TTRAP/THEM2 locus are associated with altered brain activation in distinct language-related regions.
GeneRIF
Dehaene et al., Gif-sur-Yvette, France. In J Neurosci, 2012
The results of this study confirmed that both FOXP2 and KIAA0319/TTRAP/THEM2 genes play an important role in human language development, but probably through different cerebral pathways.
Potential role of single hotdog fold thioesterase in the antiviral response of Fenneropenaeus chinensis.
Wang et al., Zhenjiang, China. In Fish Shellfish Immunol, 2011
Thioesterase superfamily member 2 (Them2) is a single hotdog fold thioesterase domain-containing protein.
PC-TP/StARD2: Of membranes and metabolism.
Review
Cohen et al., Boston, United States. In Trends Endocrinol Metab, 2010
PC-TP appears to limit access of fatty acids to mitochondria by stimulating the activity of thioesterase superfamily member 2, a newly characterized long-chain fatty acyl-coenzyme A thioesterase.
Thioesterase superfamily member 2 (Them2)/acyl-CoA thioesterase 13 (Acot13): a homotetrameric hotdog fold thioesterase with selectivity for long-chain fatty acyl-CoAs.
Cohen et al., Boston, United States. In Biochem J, 2009
Them2 (thioesterase superfamily member 2) is a 140-amino-acid protein of unknown biological function that comprises a single hotdog fold thioesterase domain.
The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis.
GeneRIF
Dunaway-Mariano et al., Albuquerque, United States. In Biochemistry, 2009
The physiological role of hTHEM2 involves catalysis of the hydrolysis of cytosolic medium-to-long-chain acyl-CoA thioesters.
HNF4 alpha orchestrates a set of 14 genes to down-regulate cell proliferation in kidney cells.
Ryffel et al., Essen, Germany. In Biol Chem, 2008
In addition, the genes SEPP1, THEM2, BPHL, DSC2, ANK3, ALDH6A1, EPHX2, NELL2, EFHD1 and PROS1 are also part of the network of HNF4 alpha target genes that regulate proliferation in HEK293 cells.
Interacting proteins dictate function of the minimal START domain phosphatidylcholine transfer protein/StarD2.
GeneRIF
Cohen et al., Boston, United States. In J Biol Chem, 2007
Yeast two-hybrid screening using libraries prepared from mouse liver and embryo identified Them2 (thioesterase superfamily member 2) and the homeodomain transcription factor Pax3 (paired box gene 3), respectively, as PC-TP-interacting proteins.
Human thioesterase superfamily member 2 (hTHEM2) is co-localized with beta-tubulin onto the microtubule.
GeneRIF
Gong et al., Hefei, China. In Biochem Biophys Res Commun, 2007
Small interference RNA silencing in cell line HCT116 shows that the hthem2 gene is essential for the cell sustained proliferation.
Crystal structure of human thioesterase superfamily member 2.
GeneRIF
Gong et al., Hefei, China. In Biochem Biophys Res Commun, 2006
analysis of human thioesterase superfamily member 2 crystal structure
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