Sequence Detail

ID/Version

Q9WUA5 G5E8E2 Q8BY80 (UniProt | EBI)

Last sequence update: 2012-10-03
Last annotation update: 2024-03-27

Sequence description from provider

RecName: Full=Laforin {ECO:0000303|PubMed:16971387}; EC=3.1.3.- {ECO:0000269|PubMed:16971387, ECO:0000269|PubMed:18040046, ECO:0000269|PubMed:24430976}; EC=3.1.3.16; EC=3.1.3.48 {ECO:0000269|PubMed:16971387};AltName: Full=Glucan ph

Provider

SWISS-PROT

Sequence

Polypeptide 330 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Epm2a	epilepsy, progressive myoclonic epilepsy, type 2 gene alpha	90	99	3	11

Sequence references in MGI

J:54186 Ganesh S, et al., Isolation and characterization of mouse homologue for the human epilepsy gene, EPM2A. Biochem Biophys Res Commun. 1999 Apr 2;257(1):24-8
J:69660 Ganesh S, et al., Regional and developmental expression of epm2a gene and its evolutionary conservation. Biochem Biophys Res Commun. 2001 May 25;283(5):1046-53
J:76688 Ganesh S, et al., Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice. Hum Mol Genet. 2002 May 15;11(11):1251-62
J:99680 The FANTOM Consortium and RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group), The Transcriptional Landscape of the Mammalian Genome. Science. 2005;309(5740):1559-1563
J:117255 Liu Y, et al., Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling. J Biol Chem. 2006 Nov 17;281(46):34768-74
J:128494 Tagliabracci VS, et al., Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. Proc Natl Acad Sci U S A. 2007 Dec 4;104(49):19262-6
J:144589 Tagliabracci VS, et al., Abnormal metabolism of glycogen phosphate as a cause for Lafora disease. J Biol Chem. 2008 Dec 5;283(49):33816-25
J:153450 Puri R, et al., Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an animal model for Lafora disease. J Biol Chem. 2009 Aug 21;284(34):22657-63
J:161320 Aguado C, et al., Laforin, the most common protein mutated in Lafora disease, regulates autophagy. Hum Mol Genet. 2010 Jul 15;19(14):2867-76
J:199271 Nitschke F, et al., Hyperphosphorylation of glucosyl C6 carbons and altered structure of glycogen in the neurodegenerative epilepsy Lafora disease. Cell Metab. 2013 May 7;17(5):756-67
J:244333 Gayarre J, et al., The phosphatase activity of laforin is dispensable to rescue Epm2a-/- mice from Lafora disease. Brain. 2014 Mar;137(Pt 3):806-18
J:274442 Tiberia E, et al., Increased laforin and laforin binding to glycogen underlie Lafora body formation in malin-deficient Lafora disease. J Biol Chem. 2012 Jul 20;287(30):25650-9
J:274449 Liu Y, et al., Laforin-malin complex degrades polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase. Mol Neurobiol. 2014 Apr;49(2):645-57