Laforin

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Structures	Swiss-model
Domains	InterPro

epilepsy, progressive myoclonus type 2A, Lafora disease (laforin)
epilepsy, progressive myoclonus type 2A, Lafora disease (laforin)
Identifiers
Symbol	EPM2A
NCBI gene	7957
HGNC	3413
OMIM	607566
PDB	4RKK
RefSeq	NM_001018041
UniProt	O95278
Other data
Locus	Chr. 6 q24
Structures
Search for
Structures	Swiss-model
Domains	InterPro

EPM2A
Identifiers
Aliases	EPM2A, EPM2, MELF, epilepsy, progressive myoclonus type 2A, Lafora disease (laforin), laforin glucan phosphatase, EPM2A glucan phosphatase, laforin
External IDs	OMIM: 607566; MGI: 1341085; GeneCards: EPM2A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4R30, 4RKK
Enzyme activity
Gene location (Human)
Chr.	Chromosome 6 (human)
End	145,736,023 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	11,335,388 bp
RNA expression pattern
	Top expressed in
	Skeletal muscle tissue of rectus abdominis; ; biceps brachii; ; muscle of thigh; ; gastrocnemius muscle; ; Skeletal muscle tissue of biceps brachii; ; vastus lateralis muscle; ; thoracic diaphragm; ; body of tongue; ; deltoid muscle; ; right ventricle;
	Top expressed in
	muscle of thigh; ; superior frontal gyrus; ; neural layer of retina; ; dentate gyrus of hippocampal formation granule cell; ; primary visual cortex; ; morula; ; cerebellar cortex; ; lip; ; skeletal muscle tissue; ; embryo;
	More reference expression data
	n/a
Gene ontology
Molecular function	phosphoprotein phosphatase activity; starch binding; hydrolase activity; protein tyrosine/serine/threonine phosphatase activity; protein binding; protein serine/threonine phosphatase activity; protein tyrosine phosphatase activity; phosphatase activity; carbohydrate phosphatase activity; carbohydrate binding; protein homodimerization activity; protein dimerization activity; glycogen binding; polysaccharide binding;
Cellular component	cytoplasm; polysome; membrane; endoplasmic reticulum; plasma membrane; cytosol; nucleoplasm; nucleus; cytoplasmic side of rough endoplasmic reticulum membrane; endoplasmic reticulum membrane; dendrite; perikaryon; cytoplasmic side of endoplasmic reticulum membrane;
Biological process	protein dephosphorylation; habituation; glycogen biosynthetic process; positive regulation of macroautophagy; nervous system development; autophagy; negative regulation of phosphatase activity; dephosphorylation; negative regulation of dephosphorylation; peptidyl-tyrosine dephosphorylation; phosphorylated carbohydrate dephosphorylation; glycogen metabolic process; carbohydrate metabolic process; autophagosome assembly; regulation of cell growth; regulation of protein phosphorylation; calcium ion transport; mitochondrion organization; regulation of gene expression; negative regulation of gene expression; glial cell proliferation; L-glutamate transmembrane transport; regulation of protein ubiquitination; negative regulation of peptidyl-serine phosphorylation; regulation of phosphorylation; proteasome-mediated ubiquitin-dependent protein catabolic process; cellular macromolecule metabolic process; negative regulation of cell cycle; regulation of protein kinase activity; regulation of proteasomal protein catabolic process; regulation of protein localization to plasma membrane; regulation of ubiquitin protein ligase activity; regulation of glycogen (starch) synthase activity; Wnt signaling pathway; regulation of protein import into nucleus; protein homooligomerization; negative regulation of TOR signaling;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	7957
	13853
	ENSG00000112425
	ENSMUSG00000055493
	O95278
	Q9WUA5
NM_001018041; NM_005670; NM_001360057; NM_001360064; NM_001360071;
	NM_001368129; NM_001368130; NM_001368131; NM_001368132
	NM_010146
NP_001018051; NP_005661; NP_001346986; NP_001346993; NP_001347000;
	NP_001355058; NP_001355059; NP_001355060; NP_001355061
	NP_034276
	Wikidata
View/Edit Human	View/Edit Mouse

Laforin, encoded by the EPM2A gene, is a phosphatase, with a carbohydrate-binding domain, which is mutated in patients with Lafora disease. It contains a dual specificity phosphatase domain (DSP) and a carbohydrate binding module subtype 20 (CBM20). Its physiological substrate has yet to be identified and the molecular mechanisms in which mutated laforin causes Lafora disease is unknown, though there has been progress made in the study by Ortolano et al. Laforin regulates autophagy via Mammalian target of rapamycin, which is impaired in Lafora disease.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000112425 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000055493 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 Ortolano S, Vieitez I, Agis-Balboa RC, Spuch C (January 2014). "Loss of GABAergic cortical neurons underlies the neuropathology of Lafora disease". Molecular Brain. 7: 7. doi:10.1186/1756-6606-7-7. PMC 3917365. PMID 24472629.
↑ Ganesh S, Agarwala KL, Ueda K, Akagi T, Shoda K, Usui T, Hashikawa T, Osada H, Delgado-Escueta AV, Yamakawa K (September 2000). "Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes". Human Molecular Genetics. 9 (15): 2251–61. doi:10.1093/oxfordjournals.hmg.a018916. PMID 11001928.
↑ "CAZy - CBM". Archived from the original on 2007-02-25. Retrieved 2007-03-28.
↑ Aguado C, Sarkar S, Korolchuk VI, Criado O, Vernia S, Boya P, Sanz P, de Córdoba SR, Knecht E, Rubinsztein DC (July 2010). "Laforin, the most common protein mutated in Lafora disease, regulates autophagy". Human Molecular Genetics. 19 (14): 2867–76. doi:10.1093/hmg/ddq190. PMC 2893813. PMID 20453062.

External links

GeneReviews/NCBI/NIH/UW entry on Progressive Myoclonus Epilepsy, Lafora Type

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000112425 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000055493 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[Ortolano-5] 1 2 Ortolano S, Vieitez I, Agis-Balboa RC, Spuch C (January 2014). "Loss of GABAergic cortical neurons underlies the neuropathology of Lafora disease". Molecular Brain. 7: 7. doi:10.1186/1756-6606-7-7. PMC 3917365. PMID 24472629.

[6] Ganesh S, Agarwala KL, Ueda K, Akagi T, Shoda K, Usui T, Hashikawa T, Osada H, Delgado-Escueta AV, Yamakawa K (September 2000). "Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes". Human Molecular Genetics. 9 (15): 2251–61. doi:10.1093/oxfordjournals.hmg.a018916. PMID 11001928.

[7] "CAZy - CBM". Archived from the original on 2007-02-25. Retrieved 2007-03-28.

[8] Aguado C, Sarkar S, Korolchuk VI, Criado O, Vernia S, Boya P, Sanz P, de Córdoba SR, Knecht E, Rubinsztein DC (July 2010). "Laforin, the most common protein mutated in Lafora disease, regulates autophagy". Human Molecular Genetics. 19 (14): 2867–76. doi:10.1093/hmg/ddq190. PMC 2893813. PMID 20453062.