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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13496: Variant p.Leu70Phe

Myotubularin
Gene: MTM1
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Variant information Variant position: help 70 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 Leucine (L) to Phenylalanine (F) at position 70 (L70F, p.Leu70Phe). 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 hydrophobic (L) to large size and aromatic (F) 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 CNMX; mild; reduced binding to PI(3,5)P2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 70 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 IYICPFNGPIKGRVYITNYR L YLRSLETDSSLILDVPLGVI 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                         IYICPFNGPIKGRVYITNYRLYLRSLETDSSLILDVPLGVI

Mouse                         IYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGVI

Rat                           IYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVI

Bovine                        IYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGVI

Xenopus laevis                IYMCPFYGPVKGRIYVTNYKLYFKGEEMEPLITFAVPLGVI

Xenopus tropicalis            IYMCPFYGPVKGRIHVTNYKLYFKGEEMEPLISFSVPLGVI

Baker's yeast                 ---CSCDG----------------AAEVPNAVSSGSKMKTF
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
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; 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; Characterisation of mutations in 77 patients with X-linked myotubular myopathy, including a family with a very mild phenotype.
Biancalana V.; Caron O.; Gallati S.; Baas F.; Kress W.; Novelli G.; D'Apice M.R.; Lagier-Tourenne C.; Buj-Bello A.; Romero N.B.; Mandel J.-L.;
Hum. Genet. 112:135-142(2003)
Cited for: VARIANTS CNMX LYS-47 DEL; ASP-68; PRO-69; SER-69; PHE-70; LYS-180; LEU-184; SER-202; LEU-205; THR-226; CYS-230; CYS-241; CYS-346; GLY-364; ASP-389; CYS-397; GLN-421; PRO-469; PRO-470 AND TYR-481;
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.