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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O75923: Variant p.Arg2042Cys

Dysferlin
Gene: DYSF
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Variant information Variant position: help 2042 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 2042 (R2042C, p.Arg2042Cys). 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 MMD1, LGMDR2 and proximodistal myopathy. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 2042 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 2080 The length of the canonical sequence.
Location on the sequence: help DTSFLWFTSPYKTMKFILWR R FRWAIILFIILFILLLFLAI 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                         DTSFLWFTSPYKTMKFILWRRFRWAIILFIILFILLLFLAI

Mouse                         DTSFLWFTSPYKTMKFILWRRFRCAIILFIILFILLLFLGV

Bovine                        DTSFLWFTSPYKTMKFILWRRFRCAIIFFLILFIFLLFLGI

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 – 2080 Dysferlin
Topological domain 1 – 2046 Cytoplasmic
Alternative sequence 1969 – 2080 Missing. In isoform 15.



Literature citations
Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy.
Liu J.; Aoki M.; Illa I.; Wu C.; Fardeau M.; Angelini C.; Serrano C.; Urtizberea J.A.; Hentati F.; Hamida M.B.; Bohlega S.; Culper E.J.; Amato A.A.; Bossie K.; Oeltjen J.; Bejaoui K.; McKenna-Yasek D.; Hosler B.A.; Schurr E.; Arahata K.; de Jong P.J.; Brown R.H. Jr.;
Nat. Genet. 20:31-36(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS MMD1 VAL-1298; ARG-1857 AND CYS-2042; VARIANTS LGMDR2 VAL-1298 AND CYS-2042; Mutation finding in patients with dysferlin deficiency and role of the dysferlin interacting proteins annexin A1 and A2 in muscular dystrophies.
Cagliani R.; Magri F.; Toscano A.; Merlini L.; Fortunato F.; Lamperti C.; Rodolico C.; Prelle A.; Sironi M.; Aguennouz M.; Ciscato P.; Uncini A.; Moggio M.; Bresolin N.; Comi G.P.;
Hum. Mutat. 26:283-283(2005)
Cited for: VARIANTS MMD1 TRP-959; TRP-1693; ASN-1837 AND GLY-1942 AND CYS-2042; VARIANTS LGMDR2 ARG-621; TRP-959; GLN-1038; LYS-1335 AND CYS-2042; VARIANTS GLU-170; LEU-374 AND SER-1678; Mutation impact on dysferlin inferred from database analysis and computer-based structural predictions.
Therrien C.; Dodig D.; Karpati G.; Sinnreich M.;
J. Neurol. Sci. 250:71-78(2006)
Cited for: VARIANTS LGMDR2 ARG-791; CYS-930; TRP-1768 AND CYS-2042; VARIANT ALA-GLU-1065 INS; Analysis of the DYSF mutational spectrum in a large cohort of patients.
Krahn M.; Beroud C.; Labelle V.; Nguyen K.; Bernard R.; Bassez G.; Figarella-Branger D.; Fernandez C.; Bouvenot J.; Richard I.; Ollagnon-Roman E.; Bevilacqua J.A.; Salvo E.; Attarian S.; Chapon F.; Pellissier J.-F.; Pouget J.; Hammouda el H.; Laforet P.; Urtizberea J.A.; Eymard B.; Leturcq F.; Levy N.;
Hum. Mutat. 30:E345-E375(2009)
Cited for: VARIANTS LGMDR2 ARG-52; ARG-155; GLU-234; THR-284; TRP-555; ARG-618; ARG-731; CYS-930; PRO-1228; THR-1526; ASP-1543; TRP-1768; SER-1970 AND CYS-2042; VARIANTS MMD1 GLU-299; 386-PHE--ASP-390 DELINS TYR; ARG-426; TRP-456; TRP-555; LEU-1029; HIS-1046; HIS-1046; GLN-1693; 1938-THR-ALA-1939 DEL AND CYS-2042; VARIANTS GLU-170; TRP-253 AND TRP-555; VARIANTS PROXIMODISTAL MYOPATHY ARG-299; ARG-340; VAL-1748; TRP-1768 AND CYS-2042; VARIANT PSEUDOMETABOLIC MYOPATHY PRO-266; VARIANTS VAL-84; VAL-189; ALA-335; LEU-374; ASN-390; GLN-819; GLN-1022; GLN-1038; VAL-1276; VAL-1325; ASN-1837 AND SER-1967;
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.