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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13496: Variant p.Arg69Cys

Myotubularin
Gene: MTM1
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Variant information Variant position: help 69 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 Cysteine (C) at position 69 (R69C, p.Arg69Cys). 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 polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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; mild; reduced response to PI5P and reduced binding to PI(3,5)P2; abolishes interaction with MTMR12. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 69 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 VIYICPFNGPIKGRVYITNY R LYLRSLETDSSLILDVPLGV 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                         VIYICPFNGPIKGRVYITNYRLYLRSLETDSSLILDVPLGV

Mouse                         VIYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGV

Rat                           VIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGV

Bovine                        VIYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGV

Xenopus laevis                VIYMCPFYGPVKGRIYVTNYKLYFKGEEMEPLITFAVPLGV

Xenopus tropicalis            VIYMCPFYGPVKGRIHVTNYKLYFKGEEMEPLISFSVPLGV

Baker's yeast                 ----CSCDG----------------AAEVPNAVSSGSKMKT
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 29 – 97 GRAM



Literature citations
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; Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction.
Tsujita K.; Itoh T.; Ijuin T.; Yamamoto A.; Shisheva A.; Laporte J.; Takenawa T.;
J. Biol. Chem. 279:13817-13824(2004)
Cited for: FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; SUBCELLULAR LOCATION; ROLE OF GRAM DOMAIN; CHARACTERIZATION OF VARIANTS PHE-49; CYS-69; PHE-70 AND PRO-87; Loss of catalytically inactive lipid phosphatase myotubularin-related protein 12 impairs myotubularin stability and promotes centronuclear myopathy in zebrafish.
Gupta V.A.; Hnia K.; Smith L.L.; Gundry S.R.; McIntire J.E.; Shimazu J.; Bass J.R.; Talbot E.A.; Amoasii L.; Goldman N.E.; Laporte J.; Beggs A.H.;
PLoS Genet. 9:E1003583-E1003583(2013)
Cited for: FUNCTION; INTERACTION WITH MTMR12; MUTAGENESIS OF CYS-375 AND 421-ARG--PHE-603; VARIANTS CNMX PHE-49; CYS-69; GLY-184; LEU-205; CYS-241 AND GLN-421; 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; Mutations in the MTM1 gene implicated in X-linked myotubular myopathy.
Laporte J.; Guiraud-Chaumeil C.; Vincent M.-C.; Mandel J.-L.; Tanner S.M.; Liechti-Gallati S.; Wallgren-Pettersson C.; Dahl N.; Kress W.; Bolhuis P.A.; Fardeau M.; Samson F.; Bertini E.;
Hum. Mol. Genet. 6:1505-1511(1997)
Cited for: VARIANTS CNMX CYS-69; PHE-70; PRO-87; SER-189; LEU-205; PRO-229; CYS-241; ASN-376; ARG-378; CYS-397; ALA-402; GLN-421; ASN-431; ASN-433 AND PRO-469; Characterization of mutations in fifty North American patients with X-linked myotubular myopathy.
Herman G.E.; Kopacz K.; Zhao W.; Mills P.L.; Metzenberg A.; Das S.;
Hum. Mutat. 19:114-121(2002)
Cited for: VARIANTS CNMX PHE-49; CYS-69; SER-179; ILE-186; LEU-205; MET-227; PRO-228; CYS-241; GLY-279; ARG-378; PRO-391; CYS-397; ARG-402 AND GLN-421;
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.