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UniProtKB/Swiss-Prot O95278: Variant p.Glu114Asp

Laforin
Gene: EPM2A
Variant information

Variant position:  114
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glutamate (E) to Aspartate (D) at position 114 (E114D, p.Glu114Asp).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Similar physico-chemical property. Both residues are medium size and acidic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  2
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page



Sequence information

Variant position:  114
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:   GGELSWEGNGPHHDRCCTYN  E NNLVDGVYCLPIGHWIEATG
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                         GGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATG

                              GGALSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATG

Mouse                         GGELHWEGNGPHHDRCCTYNEDNLVDGVYCLPVGHWIEATG

Rat                           GGELHWEGNGPHHDRCCTYNENNLVDGVYCLPVGHWIEATG

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.

TypePositionsDescription
Chain 1 – 331 Laforin
Domain 1 – 124 CBM20
Alternative sequence 1 – 243 Missing. In isoform 6.
Alternative sequence 1 – 159 MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSR -> MIFNK. In isoform 7.
Alternative sequence 1 – 138 Missing. In isoform 8.
Alternative sequence 102 – 199 NGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIV -> IASRRLPPAQSGSSGPHPQPGPRPRAGPAGPGGARPGLFARVPAHSPGDLG. In isoform 4.
Mutagenesis 99 – 99 W -> A. Strongly reduces phosphatase activity. Strongly reduces glycogen binding.
Mutagenesis 123 – 123 C -> S. No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity.
Mutagenesis 126 – 126 I -> T. Strongly decreased phosphatase activity. No effect on glycogen binding.
Helix 114 – 116


Literature citations

Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy.
Minassian B.A.; Lee J.R.; Herbrick J.-A.; Huizenga J.; Soder S.; Mungall A.J.; Dunham I.; Gardner R.; Fong C.G.; Carpenter S.; Jardim L.; Satishchandra P.; Andermann E.; Snead O.C. III; Lopes-Cendes I.; Tsui L.-C.; Delgado-Escueta A.V.; Rouleau G.A.; Scherer S.W.;
Nat. Genet. 20:171-174(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2); ALTERNATIVE SPLICING; TISSUE SPECIFICITY; VARIANTS EPM2 CYS-108; SER-279 AND LEU-293; VARIANT ASP-114;

Disclaimer: 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.