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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13496: Variant p.Arg241Leu

Myotubularin
Gene: MTM1
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Variant information Variant position: help 241 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 Arginine (R) to Leucine (L) at position 241 (R241L, p.Arg241Leu). 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 large size and basic (R) to medium size and hydrophobic (L) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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
Variant description: help In CNMX; severe; loss of activity. Any additional useful information about the variant.


Sequence information Variant position: help 241 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 603 The length of the canonical sequence.
Location on the sequence: help SRNRIPVLSWIHPENKTVIV R CSQPLVGMSGKRNKDDEKYL 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                         SRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKDDEKYL

Mouse                         SRNRLPVLSWIHPENKMVIMRCSQPLVGMSGKRNKDDEKYL

Rat                           SRNRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYL

Bovine                        SRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKEDERYL

Xenopus laevis                SRNRIPVLSWLHPENQSAIMRCSQPLVGMSGKRNKDDERYL

Xenopus tropicalis            SRNRIPVLSWLHPENQSAIMRCSQPLVGMSGKRNKDDERYL

Baker's yeast                 AATSIAPLELVKTKLQSI-------------PRSSKSTKTW
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 – 603 Myotubularin
Domain 163 – 538 Myotubularin phosphatase
Mutagenesis 255 – 255 K -> A. Disrupts interaction with DES.
Mutagenesis 257 – 257 D -> A. No effect on subcellular location.



Literature citations
Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate.
Taylor G.S.; Maehama T.; Dixon J.E.;
Proc. Natl. Acad. Sci. U.S.A. 97:8910-8915(2000)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS LEU-205; LEU-241; ASN-376; ARG-378 AND CYS-397; MUTAGENESIS OF CYS-375; Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases.
Schaletzky J.; Dove S.K.; Short B.; Lorenzo O.; Clague M.J.; Barr F.A.;
Curr. Biol. 13:504-509(2003)
Cited for: FUNCTION; CATALYTIC ACTIVITY; ACTIVITY REGULATION; CHARACTERIZATION OF VARIANTS CYS-69; GLY-184; LEU-241 AND GLN-421; MUTAGENESIS OF LYS-114; ARG-220 AND CYS-375; Characterization of mutations in the myotubularin gene in twenty six patients with X-linked myotubular myopathy.
de Gouyon B.M.; Zhao W.; Laporte J.; Mandel J.-L.; Metzenberg A.; Herman G.E.;
Hum. Mol. Genet. 6:1499-1504(1997)
Cited for: VARIANTS CNMX CYS-69; GLY-184; ASN-198; LEU-241; ARG-317; CYS-397; LYS-404; PRO-406; GLN-421 AND ARG-499;
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.