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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04181: Variant p.Cys394Tyr

Ornithine aminotransferase, mitochondrial
Gene: OAT
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Variant information Variant position: help 394 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 Tyrosine (Y) at position 394 (C394Y, p.Cys394Tyr). 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 (Y) 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 HOGA; loss of protein stability; loss of ornithine aminotransferase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 394 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 KGLLNAIVIKETKDWDAWKV C LRLRDNGLLAKPTHGDIIRF 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                         KGLLNAIVIKETKDW--DAWKVCLRLRDNGLLAKPTHGDIIRF

Mouse                         KGLLNAIVIRETKDC--DAWKVCLRLRDNGLLAKPTHGDII

Rat                           KGLLNAIVIRETKDC--DAWKVCLRLRDNGLLAKPTHGDII

Bovine                        KGLLNAIVIRETKDC--DAWKVCLRLRDNGLLAKPTHGDII

Caenorhabditis elegans        KGLFCAIVINKKY----DAWKVCLKLKENGLLAKNTHGDII

Drosophila                    KGLLNAIVINQKF----DAWEVCLRLKENGLLAKPTHGDII

Slime mold                    KGLLNAIVIDPNFTV--SAWDICIKFAENGLLAKPTHDNII

Baker's yeast                 MGLLTAIVIDPSKANGKTAWDLCLLMKDHGLLAKPTHDHII

Fission yeast                 RGLLNAVVIDESKTNGRTAWDLCLIMRSRGVLAKPTHGNII
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 386 – 386 N6-acetyllysine
Modified residue 392 – 392 N6-acetyllysine
Modified residue 405 – 405 N6-acetyllysine; alternate
Modified residue 405 – 405 N6-succinyllysine; alternate
Helix 390 – 399



Literature citations
Functional analysis of missense mutations of OAT, causing gyrate atrophy of choroid and retina.
Doimo M.; Desbats M.A.; Baldoin M.C.; Lenzini E.; Basso G.; Murphy E.; Graziano C.; Seri M.; Burlina A.; Sartori G.; Trevisson E.; Salviati L.;
Hum. Mutat. 34:229-236(2013)
Cited for: VARIANTS HOGA ASP-51; ARG-104; GLN-199; LYS-318; MET-332; TYR-394; LEU-417; ASN-436 AND PHE-437; CHARACTERIZATION OF ASP-51; ARG-104; GLN-199; VAL-226; LYS-318; MET-332; TYR-394; LEU-402; LEU-417; ASN-436 AND PHE-437; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; SUBUNIT; SUBCELLULAR LOCATION;
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.