Variant position: 84 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 VELAAEEAAQDGAEPGRVDT FWYKFLKREPGGELSWEGNGP
Mouse VELEAYEEA-GGAEPGRVDT FWYKFLQREPGGELHWEGNGP
Rat VELAPEEEAADGAEPGRIDT FWYKFLQREPGGELHWEGNGP
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
1 – 124 CBM20
87 – 87 Substrate
1 – 243 Missing. In isoform 6.
1 – 159 MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSR -> MIFNK. In isoform 7.
1 – 138 Missing. In isoform 8.
87 – 87 K -> A. Loss of phosphatase activity. Abolishes glycogen binding.
99 – 99 W -> A. Strongly reduces phosphatase activity. Strongly reduces glycogen binding.
84 – 91
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;
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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