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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00441: Variant p.His44Arg

Superoxide dismutase [Cu-Zn]
Gene: SOD1
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Variant information Variant position: help 44 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 Histidine (H) to Arginine (R) at position 44 (H44R, p.His44Arg). 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 polar (H) to large size and basic (R) 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 ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 44 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 154 The length of the canonical sequence.
Location on the sequence: help KESNGPVKVWGSIKGLTEGL H GFHVHEFGDNTAGCTSAGPH 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: 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 2 – 154 Superoxide dismutase [Cu-Zn]
Binding site 47 – 47
Binding site 49 – 49
Binding site 64 – 64
Binding site 64 – 64
Cross 33 – 33 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)
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.
Beta strand 41 – 50



Literature citations
ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization.
DiDonato M.; Craig L.; Huff M.E.; Thayer M.M.; Cardoso R.M.; Kassmann C.J.; Lo T.P.; Bruns C.K.; Powers E.T.; Kelly J.W.; Getzoff E.D.; Tainer J.A.;
J. Mol. Biol. 332:601-615(2003)
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS; DISULFIDE BOND; SUBUNIT; CHARACTERIZATION OF VARIANTS ALS1 VAL-5 AND ARG-44; Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis.
Rosen D.R.; Siddique T.; Patterson D.; Figlewicz D.A.; Sapp P.; Hentati A.; Donaldson D.; Goto J.; O'Regan J.P.; Deng H.-X.; Rahmani Z.; Krizus A.; McKenna-Yasek D.; Cayabyab A.; Gaston S.M.; Berger R.; Tanzi R.E.; Halperin J.J.; Herzfeldt B.; van den Bergh R.; Hung W.-Y.; Bird T.; Deng G.; Mulder D.W.; Smyth C.; Laing N.G.; Soriano E.; Pericak-Vance M.A.; Haines J.; Rouleau G.A.; Gusella J.S.; Horvitz H.R.; Brown R.H. Jr.;
Nature 362:59-62(1993)
Cited for: VARIANTS ALS1 ARG-38; VAL-39; ASP-42; SER-42; ARG-44; ARG-86; ALA-94; CYS-94; GLY-101; VAL-107 AND THR-114; Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.
Deng H.-X.; Hentati A.; Tainer J.A.; Iqbal Z.; Cayabyab A.; Hung W.-Y.; Getzoff E.D.; Hu P.; Herzfeldt B.; Roos R.P.; Warner C.; Deng G.; Soriano E.; Smyth C.; Parge H.E.; Ahmed A.; Roses A.D.; Hallewell R.A.; Pericak-Vance M.A.; Siddique T.;
Science 261:1047-1051(1993)
Cited for: VARIANTS ALS1 VAL-5; ARG-38; VAL-39; ASP-42; SER-42; ARG-44; ARG-86; ALA-94; CYS-94; GLY-101; VAL-107; THR-114; PHE-145 AND GLY-149;
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.