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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00387: Variant p.Gly292Asp

NADH-cytochrome b5 reductase 3
Gene: CYB5R3
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Variant information Variant position: help 292 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 Glycine (G) to Aspartate (D) at position 292 (G292D, p.Gly292Asp). 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 glycine (G) to medium size and acidic (D) 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 METHB-CYB5R3; type 1; retains approximately 58% of residual NADH-cytochrome b5 reductase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 292 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 301 The length of the canonical sequence.
Location on the sequence: help LMCGPPPMIQYACLPNLDHV G HPTERCFVF 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                         LMCGPPPMIQYACLPNLDHVGHPTERCFVF

                              LMCGPPPMIQYACLPNLDRVGHPKERCFAF

Mouse                         LMCGPPPMIQFACLPNLERVGHPKERCFTF

Rat                           LMCGPPPMIQFACLPNLERVGHPKERCFTF

Bovine                        LMCGPPPMIQYACLPNLDRVGHPKERCFAF
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 – 301 NADH-cytochrome b5 reductase 3
Mutagenesis 274 – 274 C -> A. Loss of 30% of NADH-cytochrome b5 reductase activity.
Mutagenesis 274 – 274 C -> A. Loss of 80% of NADH-cytochrome b5 reductase activity.
Mutagenesis 274 – 274 C -> S. No effect on NADH-cytochrome b5 reductase activity.
Mutagenesis 284 – 284 C -> S. No effect on NADH-cytochrome b5 reductase activity.
Mutagenesis 298 – 298 C -> S. No effect on NADH-cytochrome b5 reductase activity.
Mutagenesis 299 – 299 F -> A. Decreases protein stability and slightly decreases NADH-cytochrome b5 reductase activity.
Mutagenesis 299 – 299 F -> L. No effect on protein stability and NADH-cytochrome b5 reductase activity.
Mutagenesis 301 – 301 F -> A. Decreases protein stability and slightly decreases NADH-cytochrome b5 reductase activity.
Mutagenesis 301 – 301 F -> L. No effect on protein stability and NADH-cytochrome b5 reductase activity.



Literature citations
Familial idiopathic methemoglobinemia revisited: original cases reveal 2 novel mutations in NADH-cytochrome b5 reductase.
Percy M.J.; Gillespie M.J.S.; Savage G.; Hughes A.E.; McMullin M.F.; Lappin T.R.J.;
Blood 100:3447-3449(2002)
Cited for: VARIANTS METHB-CYB5R3 GLU-256 DEL AND ASP-292; Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase.
Percy M.J.; Crowley L.J.; Davis C.A.; McMullin M.F.; Savage G.; Hughes J.; McMahon C.; Quinn R.J.M.; Smith O.; Barber M.J.; Lappin T.R.J.;
Br. J. Haematol. 129:847-853(2005)
Cited for: CHARACTERIZATION OF VARIANTS METHB-CYB5R3 GLU-256 DEL AND ASP-292; CATALYTIC ACTIVITY; COFACTOR; FUNCTION; BIOPHYSICOCHEMICAL PROPERTIES;
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.