Variant position: 104 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 439 The length of the canonical sequence.
Location on the sequence:
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 SYSAVNQGHCHPKIVNALKS QVDKLTLTSRAFYNNVLGEYE
Mouse AYGAVSQGHCHPKIIDAMKS QVDKLTLTSRAFYNNVLGEYE
Rat AYGAVSQGHCHPKIIEAMKS QVDKLTLTSRAFYNNVLGEYE
Bovine AYSAVNQGHCHPKIVDALKS QVDKLTLTSRAFYNNVLGEYE
Caenorhabditis elegans AYSAVNQGHCHPKLLKVVQE QASTLTLTSRAFYNNVLGEYE
Drosophila AYSAVNQGHCHPKIVAALTA QASKLALTSRAFYSDVLGEYE
Slime mold AYSAVNQGHSHPKIVSALIT QAQKCALSSRAFYNEVFPQYA
Baker's yeast AYSAVNQGHCHPHIIKALTE QAQTLTLSSRAFHNDVYAQFA
Fission yeast AYSAVNQGHCHPKIIEALVE QAQRVTLSSRAFYNDKFGPFA
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.
Type Positions Description
26 – 439 Ornithine aminotransferase, hepatic form
36 – 439 Ornithine aminotransferase, renal form
102 – 102 N6-succinyllysine
107 – 107 N6-acetyllysine; alternate
107 – 107 N6-succinyllysine; alternate
1 – 138 Missing. In isoform 2.
95 – 104
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; SUBUNIT; SUBCELLULAR LOCATION;
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