Variant position: 240 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 331 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human LYREEGLAYIWMPTPDMSTE GRVQMLPQAVCLLHALLEKGH
Mouse LYKEEGLSYIWMPTPDMSTE GRVQMLPQAVCLLHALLENGH
Rat LYKEEGLAYIWMPTPDMSTE GRVQMLPQAVCLLHALLENGH
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 331 Laforin
235 – 235 Substrate
241 – 241 Substrate
1 – 243 Missing. In isoform 6.
160 – 293 Missing. In isoform 5.
200 – 331 Missing. In isoform 4.
235 – 235 D -> A. Complete loss of phosphatase activity. Does not affect glycogen binding.
236 – 236 M -> A. Complete loss of phosphatase activity. No effect on glycogen binding.
250 – 250 C -> S. No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity.
251 – 251 L -> A. Impairs protein stability. Strongly reduces phosphatase activity. No effect on glycogen binding.
238 – 258
Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation.
Fernandez-Sanchez M.E.; Criado-Garcia O.; Heath K.E.; Garcia-Fojeda B.; Medrano-Fernandez I.; Gomez-Garre P.; Sanz P.; Serratosa J.M.; Rodriguez de Cordoba S.;
Hum. Mol. Genet. 12:3161-3171(2003)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SELF-INTERACTION; SUBCELLULAR LOCATION; GLYCOGEN-BINDING; INTERACTION WITH PPP1R3C; TISSUE SPECIFICITY; MUTAGENESIS OF ASP-235 AND CYS-266; ACTIVE SITE; CHARACTERIZATION OF VARIANTS EPM2 GLY-32; LEU-84; CYS-108; ILE-194; SER-240; SER-279; LEU-293; ASN-294 AND LEU-301;
Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease.
Raththagala M.; Brewer M.K.; Parker M.W.; Sherwood A.R.; Wong B.K.; Hsu S.; Bridges T.M.; Paasch B.C.; Hellman L.M.; Husodo S.; Meekins D.A.; Taylor A.O.; Turner B.D.; Auger K.D.; Dukhande V.V.; Chakravarthy S.; Sanz P.; Woods V.L. Jr.; Li S.; Vander Kooi C.W.; Gentry M.S.;
Mol. Cell 57:261-272(2015)
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-329 IN COMPLEX WITH MALTOHEXAOSE AND PHOSPHATE; CATALYTIC ACTIVITY; FUNCTION; SUBUNIT; MUTAGENESIS OF VAL-8; LYS-87; TRP-99; ILE-126; THR-142; ASP-197; MET-236 AND CYS-266; CHARACTERIZATION OF VARIANTS EPM2 GLY-32; HIS-171; SER-240; ASN-294 AND LEU-301;
Mutational spectrum of the EPM2A gene in progressive myoclonus epilepsy of Lafora: high degree of allelic heterogeneity and prevalence of deletions.
Gomez-Garre P.; Sanz Y.; Rodriguez de Cordoba S.R.; Serratosa J.M.;
Eur. J. Hum. Genet. 8:946-954(2000)
Cited for: VARIANTS EPM2 LEU-84; SER-240 AND LEU-301;
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