Variant position: 394 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 KGLLNAIVIKETKDW--DAWKV CLRLRDNGLLAKPTHGDIIRF
Mouse KGLLNAIVIRETKDC--DAWKV CLRLRDNGLLAKPTHGDII
Rat KGLLNAIVIRETKDC--DAWKV CLRLRDNGLLAKPTHGDII
Bovine KGLLNAIVIRETKDC--DAWKV CLRLRDNGLLAKPTHGDII
Caenorhabditis elegans KGLFCAIVINKKY----DAWKV CLKLKENGLLAKNTHGDII
Drosophila KGLLNAIVINQKF----DAWEV CLRLKENGLLAKPTHGDII
Slime mold KGLLNAIVIDPNFTV--SAWDI CIKFAENGLLAKPTHDNII
Baker's yeast MGLLTAIVIDPSKANGKTAWDL CLLMKDHGLLAKPTHDHII
Fission yeast RGLLNAVVIDESKTNGRTAWDL CLIMRSRGVLAKPTHGNII
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
386 – 386 N6-acetyllysine
392 – 392 N6-acetyllysine
405 – 405 N6-acetyllysine; alternate
405 – 405 N6-succinyllysine; alternate
390 – 399
Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.
Michaud J.; Brody L.C.; Steel G.; Fontaine G.; Martin L.S.; Valle D.; Mitchell G.;
Cited for: VARIANTS HOGA THR-180; LEU-241; PRO-250; ASP-353 AND ARG-394;
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;
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.