Variant position: 25 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 FGVVVPPAVAGARPELLVVG SRPELGRWEPRGAVRLRPAGT
Mouse FGVVVPPAVAGARQELLLAG SRPELGRWEPHGAVRLRPAGT
Rat FGVVVPPAVAGTRLELLLAG SRPELGRWEPRGAVRLRPAGT
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
32 – 32 Substrate
25 – 25 Phosphoserine; by AMPK
1 – 243 Missing. In isoform 6.
1 – 159 MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSR -> MIFNK. In isoform 7.
1 – 138 Missing. In isoform 8.
8 – 8 V -> A. Loss of phosphatase activity. No effect on glycogen binding.
25 – 25 S -> A. Partial loss of phosphatase activity. Abolishes homodimerization. Abolishes interaction with NHLRC1, PPP1R3C and PRKAA2. Does not affect glycogen binding. Reduces stability of the protein.
25 – 25 S -> D. Partial loss of phosphatase activity. Increases interaction with NHLRC1. Does not affect interaction with NHLRC1, PPP1R3C or PRKAA2. Does not affect binding to carbohydrate. Does not affect homodimerization.
19 – 26
The carbohydrate-binding domain of Lafora disease protein targets Lafora polyglucosan bodies.
Ganesh S.; Tsurutani N.; Suzuki T.; Hoshii Y.; Ishihara T.; Delgado-Escueta A.V.; Yamakawa K.;
Biochem. Biophys. Res. Commun. 313:1101-1109(2004)
Cited for: BINDING TO GLYCOGEN AND LAFORA BODIES; DOMAIN; CHARACTERIZATION OF VARIANTS EPM2 PRO-25; LYS-28; GLY-32 AND LEU-88; CHARACTERIZATION OF VARIANT PRO-46;
Genotype-phenotype correlations for EPM2A mutations in Lafora's progressive myoclonus epilepsy: exon 1 mutations associate with an early-onset cognitive deficit subphenotype.
Ganesh S.; Delgado-Escueta A.V.; Suzuki T.; Francheschetti S.; Riggio C.; Avanzini G.; Rabinowicz A.; Bohlega S.; Bailey J.; Alonso M.E.; Rasmussen A.; Thomson A.E.; Ochoa A.; Prado A.J.; Medina M.T.; Yamakawa K.;
Hum. Mol. Genet. 11:1263-1271(2002)
Cited for: VARIANTS EPM2 PRO-25; CYS-108; HIS-171 AND LEU-293; CHARACTERIZATION OF VARIANTS EPM2 GLY-32; CYS-108; ILE-194; SER-279 AND ASN-294;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.