Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UMS0: Variant p.Cys210Phe

NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
Gene: NFU1
Feedback?
Variant information Variant position: help 210 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 Cysteine (C) to Phenylalanine (F) at position 210 (C210F, p.Cys210Phe). 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 (C) to large size and aromatic (F) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 MMDS1 and SPG93; likely pathogenic. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 210 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 254 The length of the canonical sequence.
Location on the sequence: help GDVIYKGFEDGIVQLKLQGS C TSCPSSIITLKNGIQNMLQF 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                         GDVIYKGFE--DGIVQLKLQGSCTSCPSSIITLKNGIQNMLQF

Mouse                         GDVIYRGFE--DGIVRLKLQGSCTSCPSSIITLKSGIQNML

Drosophila                    GDIVFMGYE--GGVVKLKMQGSCSSCPSSIVTLKNGVQNML

Baker's yeast                 GDIDYRGWDPKTGTVYLRLQGACTSCSSSEVTLKYGIESML
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 10 – 254 NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
Region 173 – 241 NifU
Binding site 210 – 210
Binding site 213 – 213
Turn 208 – 212



Literature citations
Cavitating leukoencephalopathy with multiple mitochondrial dysfunction syndrome and NFU1 mutations.
Invernizzi F.; Ardissone A.; Lamantea E.; Garavaglia B.; Zeviani M.; Farina L.; Ghezzi D.; Moroni I.;
Front. Genet. 5:412-412(2014)
Cited for: VARIANTS MMDS1 ARG-189 AND PHE-210;
Phenotypic continuum of NFU1-related disorders.
Kaiyrzhanov R.; Zaki M.S.; Lau T.; Sen S.; Azizimalamiri R.; Zamani M.; Sayin G.Y.; Hilander T.; Efthymiou S.; Chelban V.; Brown R.; Thompson K.; Scarano M.I.; Ganesh J.; Koneev K.; Guelacar I.M.; Person R.; Sadykova D.; Maidyrov Y.; Seifi T.; Zadagali A.; Bernard G.; Allis K.; Elloumi H.Z.; Lindy A.; Taghiabadi E.; Verma S.; Logan R.; Kirmse B.; Bai R.; Khalaf S.M.; Abdel-Hamid M.S.; Sedaghat A.; Shariati G.; Issa M.; Zeighami J.; Elbendary H.M.; Brown G.; Taylor R.W.; Galehdari H.; Gleeson J.J.; Carroll C.J.; Cowan J.A.; Moreno-De-Luca A.; Houlden H.; Maroofian R.;
Ann. Clin. Transl. Neurol. 9:2025-2035(2022)
Cited for: VARIANTS SPG93 SER-88; VAL-99; PRO-100; GLY-101; ALA-121; PRO-133; ARG-183; ARG-189; PHE-210 AND LEU-241; INVOLVEMENT IN SPG93;
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.