UniProtKB/Swiss-Prot Q13496: Variant p.Arg241Cys

Myotubularin
Gene: MTM1
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Variant information Variant position:

241 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Arginine (R) to Cysteine (C) at position 241 (R241C, p.Arg241Cys). 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:

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:

-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:

In CNMX; mild to moderate; abolishes interaction with DES, but not with MTMR12; reduces MTMR12 protein levels in myotubes. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs132630305 [ dbSNP | Ensembl ]

Sequence information Variant position:

241 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

603 The length of the canonical sequence.
Location on the sequence:

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:

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:

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.

Type	Positions	Description
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 controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle.
Hnia K.; Tronchere H.; Tomczak K.K.; Amoasii L.; Schultz P.; Beggs A.H.; Payrastre B.; Mandel J.L.; Laporte J.;
J. Clin. Invest. 121:70-85(2011)
Cited for: FUNCTION; INTERACTION WITH DES; CHARACTERIZATION OF VARIANTS GLY-184; LEU-205; CYS-241 AND GLN-421; MUTAGENESIS OF HIS-181; TYR-206; SER-209; LYS-255; LYS-269; ASP-278; CYS-375; ASP-380 AND SER-420; 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; 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; Identification of novel mutations in the MTM1 gene causing severe and mild forms of X-linked myotubular myopathy.
Buj-Bello A.; Biancalana V.; Moutou C.; Laporte J.; Mandel J.-L.;
Hum. Mutat. 14:320-325(1999)
Cited for: VARIANTS CNMX SER-179; THR-225; CYS-241; SER-264; GLY-294 DEL; ARG-378 AND ASN-510; Characterization of 34 novel and six known MTM1 gene mutations in 47 unrelated X-linked myotubular myopathy patients.
Tanner S.M.; Schneider V.; Thomas N.S.T.; Clarke A.; Lazarou L.; Liechti-Gallati S.;
Neuromuscul. Disord. 9:41-49(1999)
Cited for: VARIANTS CNMX LEU-205; THR-225; CYS-230; ARG-232; CYS-241; ARG-402 AND TYR-444; 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; 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.