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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O15229: Variant p.Arg452Cys

Kynurenine 3-monooxygenase
Gene: KMO
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Variant information Variant position: help 452 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Arginine (R) to Cysteine (C) at position 452 (R452C, p.Arg452Cys). 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 large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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

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


Sequence information Variant position: help 452 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 486 The length of the canonical sequence.
Location on the sequence: help LIAISSTYLLIHYMSPRSFL R LRRPWNWIAHFRNTTCFPAK 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                         LIAISSTYLLIHY--------------MSPRSFLRLRRP-WNWIAHFRNTTCFPAK

Mouse                         LIAIGGTYLLVHH--------------LSLRPLEFLRRPAW

Rat                           LVAIGSAYILVHH--------------LSPRPLELLRSA-W

Pig                           LVALSTTYLLTGP--------------TFRSSLGCLRRS-W

Xenopus tropicalis            TGSVGAAYLVIKYLPFNKYIEHVGNCLTHLKGNAYLSRL-W

Zebrafish                     VSAAGGTYVLVKN--------------SHKLPSISAEQL-W

Caenorhabditis elegans        LALIGAAAGIYVN-----------------RGKLGL-----

Drosophila                    IVTGGAIYAQRFL----------------------------

Slime mold                    LVKGNDDYNIEKI------------------DLVLADQL--

Baker's yeast                 LSIGG--YKLFKF--------------------LTRERS--

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 1 – 486 Kynurenine 3-monooxygenase
Glycosylation 465 – 465 N-linked (GlcNAc...) asparagine
Mutagenesis 465 – 465 N -> A. Not glycosylated. Reduces to 80% kynurenine 3-monooxygenase activity.



Literature citations
Cloning and functional expression of human kynurenine 3-monooxygenase.
Alberati-Giani D.; Cesura A.M.; Broger C.; Warren W.D.; Rover S.; Malherbe P.;
FEBS Lett. 410:407-412(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; VARIANT CYS-452; Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase.
Breton J.; Avanzi N.; Magagnin S.; Covini N.; Magistrelli G.; Cozzi L.; Isacchi A.;
Eur. J. Biochem. 267:1092-1099(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); CATALYTIC ACTIVITY; COFACTOR; BIOPHYSICOCHEMICAL PROPERTIES; VARIANT CYS-452;
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.