Sequence information
Variant position: 158 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 427 The length of the canonical sequence.
Location on the sequence:
QSLMCGHQDVMVAGGMESMS
N VPYVMNRGSTPYGGVKLEDL
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 QSLMCGHQDVMVAGGMESMSN VPYVM--NRGSTPYGGVKLEDL
Mouse QSLMCGHQDVMVAGGMESMSN VPYVM--SRGATPYGGVKLE
Rat QSLMCGHQDVMVAGGMESMSN VPYVM--SRGATPYGGVKLE
Bovine QNLMCGHQDVMVAGGMESMSN VPYVM--NRGATPYGGVKLE
Xenopus tropicalis QSLMCGHQQVMVAGGMESMSN VPYCM--SRGATPYGGVKLE
Zebrafish QSLMCGHQDVMVAGGMESMSQ VPYIM--AREAPPYGGVKME
Baker's yeast QSIKCGNADVVVAGGCESMTN APYYMPAARAGAKFGQTVLV
Fission yeast QTIMTGNAEIVVAGGTESMSN APYYAPKNRFGAKYGNVELV
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
Chain
34 – 427
Acetyl-CoA acetyltransferase, mitochondrial
Modified residue
174 – 174
N6-acetyllysine; alternate
Modified residue
174 – 174
N6-succinyllysine; alternate
Alternative sequence
146 – 162
DVMVAGGMESMSNVPYV -> IKQETGSLAKICCHVRR. In isoform 2.
Helix
156 – 158
Literature citations
Molecular, biochemical, and clinical characterization of mitochondrial acetoacetyl-coenzyme A thiolase deficiency in two further patients.
Wakazono A.; Fukao T.; Yamaguchi S.; Hori T.; Orii T.; Lambert M.; Mitchell G.A.; Lee G.W.; Hashimoto T.;
Hum. Mutat. 5:34-42(1995)
Cited for: VARIANTS 3KTD ASP-158; MET-297 AND PRO-301; CHARACTERIZATION OF VARIANTS 3KTD ASP-158; MET-297 AND PRO-301; 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.