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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P54868: Variant p.Met307Thr

Hydroxymethylglutaryl-CoA synthase, mitochondrial
Gene: HMGCS2
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Variant information Variant position: help 307 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 Methionine (M) to Threonine (T) at position 307 (M307T, p.Met307Thr). 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 hydrophobic (M) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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 HMGCS2D; abolished enzymatic activity. Any additional useful information about the variant.


Sequence information Variant position: help 307 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 508 The length of the canonical sequence.
Location on the sequence: help DRPFTLDDLQYMIFHTPFCK M VQKSLARLMFNDFLSASSDT 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                         DRPFTLDDLQYMIFHTPFCKMVQKSLARLMFNDFLSASSDT

Mouse                         NQPFTLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDK

Rat                           NQPFTLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDK

Pig                           ERHFTLDDLQFMIFHTPFCKLVQKSLARLMFSDFLLADSDT

Bovine                        DRPFTLDDVQYMIFHTPFCKLVQKSLARLMFNDFLLASGDT
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 38 – 508 Hydroxymethylglutaryl-CoA synthase, mitochondrial
Active site 301 – 301 Proton donor/acceptor
Modified residue 306 – 306 N6-acetyllysine
Modified residue 310 – 310 N6-acetyllysine; alternate
Modified residue 310 – 310 N6-succinyllysine; alternate
Helix 305 – 322



Literature citations
Refining the diagnosis of mitochondrial HMG-CoA synthase deficiency.
Aledo R.; Mir C.; Dalton R.N.; Turner C.; Pie J.; Hegardt F.G.; Casals N.; Champion M.P.;
J. Inherit. Metab. Dis. 29:207-211(2006)
Cited for: VARIANTS HMGCS2D HIS-188 AND THR-307; New case of mitochondrial HMG-CoA synthase deficiency. Functional analysis of eight mutations.
Ramos M.; Menao S.; Arnedo M.; Puisac B.; Gil-Rodriguez M.C.; Teresa-Rodrigo M.E.; Hernandez-Marcos M.; Pierre G.; Ramaswami U.; Baquero-Montoya C.; Bueno G.; Casale C.; Hegardt F.G.; Gomez-Puertas P.; Pie J.;
Eur. J. Med. Genet. 56:411-415(2013)
Cited for: CATALYTIC ACTIVITY; FUNCTION; VARIANTS HMGCS2D MET-54; CYS-167; LEU-174; HIS-188; ARG-212; THR-307; ARG-388; 424-ARG--VAL-508 DEL AND HIS-500; CHARACTERIZATION OF VARIANTS HMGCS2D MET-54; CYS-167; LEU-174; HIS-188; ARG-212; THR-307; ARG-388 AND HIS-500; BIOPHYSICOCHEMICAL PROPERTIES;
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.