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UniProtKB/Swiss-Prot P00387: Variant p.Arg58Gln

NADH-cytochrome b5 reductase 3
Gene: CYB5R3
Variant information

Variant position:  58
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Arginine (R) to Glutamine (Q) at position 58 (R58Q, p.Arg58Gln).
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 large size and basic (R) to medium size and polar (Q)
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 METHB-CYB5R3; type 1; 62% of activity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  58
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  301
The length of the canonical sequence.

Location on the sequence:   SPDIKYPLRLIDREIISHDT  R RFRFALPSPQHILGLPVGQH
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         SPDIKYPLRLIDREIISHDTRRFRFALPSPQHILGLPVGQH

                              SPDIKYPLRLIDKEVINHDTRRFRFALPSPQHILGLPVGQH

Mouse                         NPDIKYPLRLIDKEVISPDTRRFRFALPSPQHILGLPIGQH

Rat                           NPDIKYPLRLIDKEIISHDTRRFRFALPSPQHILGLPIGQH

Bovine                        NPDIKYPLRLIDKEVISHDTRRFRFALPSPEHILGLPVGQH

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 – 301 NADH-cytochrome b5 reductase 3 membrane-bound form
Chain 27 – 301 NADH-cytochrome b5 reductase 3 soluble form
Domain 40 – 152 FAD-binding FR-type
Modified residue 42 – 42 N6-acetyllysine
Modified residue 43 – 43 Phosphotyrosine
Beta strand 54 – 63


Literature citations

Submission
Lan F.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT PRO-66; VARIANTS HM GLN-58; PRO-73 AND TYR-204;

Exonic point mutations in NADH-cytochrome B5 reductase genes of homozygotes for hereditary methemoglobinemia, types I and III: putative mechanisms of tissue-dependent enzyme deficiency.
Katsube T.; Sakamoto N.; Kobayashi Y.; Seki R.; Hirano M.; Tanishima K.; Tomoda A.; Takazakura E.; Yubisui T.; Takeshita M.; Sakaki Y.; Fukumaki Y.;
Am. J. Hum. Genet. 48:799-808(1991)
Cited for: VARIANTS METHB-CYB5R3 GLN-58 AND PRO-149;

Arginine-glutamine replacement at residue 57 of NADH-cytochrome b5 reductase in Chinese hereditary methemoglobinemia.
Huang C.-H.; Xie Y.; Wang Y.; Wu Y.-S.;
Zhonghua Xue Ye Xue Za Zhi 18:200-203(1997)
Cited for: VARIANT METHB-CYB5R3 GLN-58;

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.