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UniProtKB/Swiss-Prot P35914 : Variant p.Cys174Tyr
Hydroxymethylglutaryl-CoA lyase, mitochondrial
Gene: HMGCL
Variant information
Variant position: 174 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LP/P [Disclaimer : Variants classification is intended for research purposes only, not for clinical and diagnostic use . The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant. ]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: From Cysteine (C) to Tyrosine (Y) at position 174 (C174Y, p.Cys174Tyr).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: 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: -2The 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: In HMGCLD; activity lower than 5% respect to the wild-type.Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.
Sequence information
Variant position: 174 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 325 The length of the canonical sequence.
Location on the sequence:
LKAAQSANISVRGYVSCALG
C PYEGKISPAKVAEVTKKFYS
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 LKAAQSANISVRGYVSCALGC PYEGKISPAKVAEVTKKFYS
Mouse MQAAQAASISVRGYVSCALGC PYEGKVSPAKVAEVAKKLYS
Rat MQAARAASISVRGYVSCALGC PYEGKVSPAKVAEVAKKLYS
Bovine LKAARAAGISVRGYVSCVLGC PYEGKISPAKVAEVTKKLYS
Chicken MNAARAASIPVRGYVSCVLGC PYEGNISAAKVAEVSKKMYS
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
28 – 325
Hydroxymethylglutaryl-CoA lyase, mitochondrial
Domain
33 – 300
Pyruvate carboxyltransferase
Modified residue
179 – 179
N6-acetyllysine; alternate
Modified residue
179 – 179
N6-succinyllysine; alternate
Alternative sequence
117 – 187
Missing. In isoform 2 and isoform 3.
Literature citations
Ten novel HMGCL mutations in 24 patients of different origin with 3-hydroxy-3-methyl-glutaric aciduria.
Menao S.; Lopez-Vinas E.; Mir C.; Puisac B.; Gratacos E.; Arnedo M.; Carrasco P.; Moreno S.; Ramos M.; Gil M.C.; Pie A.; Ribes A.; Perez-Cerda C.; Ugarte M.; Clayton P.T.; Korman S.H.; Serra D.; Asins G.; Ramos F.J.; Gomez-Puertas P.; Hegardt F.G.; Casals N.; Pie J.;
Hum. Mutat. 30:E520-E529(2009)
Cited for: VARIANTS HMGCLD LYS-37; GLY-42; PHE-142; TYR-174; SER-192; PHE-200 AND ARG-233; CHARACTERIZATION OF VARIANTS HMGCLD LYS-37; PHE-142; TYR-174; SER-192 AND PHE-200;
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.