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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04181: Variant p.Asn89Lys

Ornithine aminotransferase, mitochondrial
Gene: OAT
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Variant information Variant position: help 89 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 Asparagine (N) to Lysine (K) at position 89 (N89K, p.Asn89Lys). 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 (N) to large size and basic (K) 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 HOGA; no effect on protein abundance. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 89 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 439 The length of the canonical sequence.
Location on the sequence: help YLWDVEGRKYFDFLSSYSAV N QGHCHPKIVNALKSQVDKLT 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                         YLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLT

Mouse                         YMWDVEGRQYFDFLSAYGAVSQGHCHPKIIDAMKSQVDKLT

Rat                           YMWDVEGRQYFDFLSAYGAVSQGHCHPKIIEAMKSQVDKLT

Bovine                        YVWDVEGRKYFDFLSAYSAVNQGHCHPKIVDALKSQVDKLT

Caenorhabditis elegans        FVWDVEGKKYFDFLAAYSAVNQGHCHPKLLKVVQEQASTLT

Drosophila                    FVWDVEGKRYFDYLSAYSAVNQGHCHPKIVAALTAQASKLA

Slime mold                    HVWDVEEKQYFDFLSAYSAVNQGHSHPKIVSALITQAQKCA

Baker's yeast                 HVWDPEGKLYLDFLSAYSAVNQGHCHPHIIKALTEQAQTLT

Fission yeast                 KVWDPEGREYLDFLSAYSAVNQGHCHPKIIEALVEQAQRVT
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 26 – 439 Ornithine aminotransferase, hepatic form
Chain 36 – 439 Ornithine aminotransferase, renal form
Modified residue 102 – 102 N6-succinyllysine
Modified residue 107 – 107 N6-acetyllysine; alternate
Modified residue 107 – 107 N6-succinyllysine; alternate
Alternative sequence 1 – 138 Missing. In isoform 2.
Turn 87 – 90



Literature citations
Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences.
Brody L.C.; Mitchell G.A.; Obie C.; Michaud J.; Steel G.; Fontaine G.; Robert M.-F.; Sipila I.; Kaiser-Kupfer M.; Valle D.;
J. Biol. Chem. 267:3302-3307(1992)
Cited for: VARIANTS HOGA HIS-55; LYS-89; PHE-93; LEU-154; THR-180; ALA-184 DEL; LEU-241; CYS-245; PRO-250; ILE-267; LYS-271; ASP-353; ALA-375; ARG-394; PRO-402 AND LEU-417; VARIANT PHE-437; CHARACTERIZATION OF VARIANTS HOGA HIS-55; LYS-89; PHE-93; LEU-154; THR-180; ALA-184 DEL; LEU-241; CYS-245; PRO-250; ILE-267; LYS-271; ASP-353; ALA-375; ARG-394; PRO-402 AND LEU-417; CHARACTERIZATION OF VARIANT PRO-270; FUNCTION; CATALYTIC ACTIVITY; PATHWAY;
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.