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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13496: Variant p.Val49Phe

Myotubularin
Gene: MTM1
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Variant information Variant position: help 49 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 Valine (V) to Phenylalanine (F) at position 49 (V49F, p.Val49Phe). 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 (V) to large size and aromatic (F) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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; greatly reduced binding to PI(3,5)P2; abolishes interaction with MTMR12; does not translocate to the late endosome following EGF stimulation; shows normal EGFR degradation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 49 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 RDLTEAVPRLPGETLITDKE V IYICPFNGPIKGRVYITNYR 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                         RDLTEAVP----RLPGETLITDKEVIYICPFNGPIKGRVYITNYR

Mouse                         QDVSETVP----RLPGELLITEKEVIYICPFNGPIKGRVYI

Rat                           QDMSKSGP----RLPGESAITDKEVIYICPFSGPVKGRLYI

Bovine                        RDVGETLP----RLPGEIRITDKEVIYICPFNGPIKGRVYI

Xenopus laevis                HEQNDEIS----RLPGETLITDKEVIYMCPFYGPVKGRIYV

Xenopus tropicalis            HEQNDEIP----CLPGEALITDKDVIYMCPFYGPVKGRIHV

Baker's yeast                 SLILTPMDVVRIRLQQQQMIPD------CSCDG--------
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; 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 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.