Home  |  Contact

UniProtKB/Swiss-Prot P00441: Variant p.Thr55Arg

Superoxide dismutase [Cu-Zn]
Gene: SOD1
Variant information

Variant position:  55
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 Threonine (T) to Arginine (R) at position 55 (T55R, p.Thr55Arg).
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 medium size and polar (T) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In ALS1; reduces tendency to form fibrillar aggregates.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  55
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  154
The length of the canonical sequence.

Location on the sequence:   SIKGLTEGLHGFHVHEFGDN  T AGCTSAGPHFNPLSRKHGGP
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.

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.

TypePositionsDescription
Chain 2 – 154 Superoxide dismutase [Cu-Zn]
Metal binding 47 – 47 Copper; catalytic
Metal binding 49 – 49 Copper; catalytic
Metal binding 64 – 64 Copper; catalytic
Metal binding 64 – 64 Zinc; via pros nitrogen
Metal binding 72 – 72 Zinc; via pros nitrogen
Mutagenesis 58 – 58 C -> A. Exhibits very slow copper acquisition.
Mutagenesis 58 – 58 C -> S. Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147.
Turn 55 – 57


Literature citations

Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes.
Andersen P.M.; Sims K.B.; Xin W.W.; Kiely R.; O'Neill G.; Ravits J.; Pioro E.; Harati Y.; Brower R.D.; Levine J.S.; Heinicke H.U.; Seltzer W.; Boss M.; Brown R.H. Jr.;
Amyotroph. Lateral Scler. 4:62-73(2003)
Cited for: VARIANTS ALS1 VAL-9; CYS-21; LEU-23; ARG-49; ARG-55; ALA-88; THR-90; MET-98; LEU-119; GLY-125 AND ARG-148;

SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization.
Banci L.; Bertini I.; Boca M.; Girotto S.; Martinelli M.; Valentine J.S.; Vieru M.;
PLoS ONE 3:E1677-E1677(2008)
Cited for: CHARACTERIZATION OF VARIANTS ALS1 ARG-55; ALA-91; ALA-94; ASP-94; MET-98 AND PHE-145;

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.