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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O95278: Variant p.Thr187Ala

Laforin
Gene: EPM2A
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Variant information Variant position: help 187 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Threonine (T) to Alanine (A) at position 187 (T187A, p.Thr187Ala). 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: help Change from medium size and polar (T) to small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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
Variant description: help In MELF1; abolishes interaction with NHLRC1. Any additional useful information about the variant.


Sequence information Variant position: help 187 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 331 The length of the canonical sequence.
Location on the sequence: help GSCPRQVEHVTIKLKHELGI T AVMNFQTEWDIVQNSSGCNR 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GSCPRQVEHVTIKLKHELGITAVMNFQTEWDIVQNSSGCNR

                              GSCPRQVEHITIKLKHELGITAVMNFQTEWDIVQNSSGCNR

Mouse                         GSCPRQLEHVTIKLKHELGVTAVMNFQTEWDIIQNSSGCNR

Rat                           GSCPRQLEHVTIKLKHELGITAVMNFQTEWDIIQNSSGCNR
Sequence annotation in neighborhood: help 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 156 – 323 Tyrosine-protein phosphatase
Binding site 197 – 197
Alternative sequence 1 – 243 Missing. In isoform 6.
Alternative sequence 102 – 199 NGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIV -> IASRRLPPAQSGSSGPHPQPGPRPRAGPAGPGGARPGLFARVPAHSPGDLG. In isoform 4.
Alternative sequence 160 – 293 Missing. In isoform 5.
Mutagenesis 168 – 168 S -> AD. Abolishes interaction with NHLRC1.
Mutagenesis 169 – 169 C -> S. No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity.
Mutagenesis 169 – 169 C -> S. No effect on phosphatase activity.
Mutagenesis 171 – 171 R -> A. No effect on phosphatase activity.
Mutagenesis 187 – 187 T -> D. Abolishes interaction with NHLRC1.
Mutagenesis 194 – 194 T -> D. Does not affect interaction with NHLRC1, PPP1R3C or PRKAA2.
Mutagenesis 197 – 197 D -> A. Strongly decreased phosphatase activity. No effect on glycogen binding.
Mutagenesis 205 – 205 C -> S. No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity.



Literature citations
Two novel mutations in the EPM2A gene in a Korean patient with Lafora's progressive myoclonus epilepsy.
Ki C.S.; Kong S.Y.; Seo D.W.; Hong S.B.; Kim H.J.; Kim J.W.;
J. Hum. Genet. 48:51-54(2003)
Cited for: VARIANT MELF1 ALA-187;
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.