Sequence information
Variant position: 135 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 396 The length of the canonical sequence.
Location on the sequence:
LYLSICRKQRALPSLDIVVW
S ELPPGAGLGSSAAYSVCLAA
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 LYLSICRKQRALPSLDIVVWS ELPPGAGLGSSAAYSVCLAA
Mouse LYLAICRKQRTLPSLDMVVWS ELPPGAGLGSSAAYSVCLAA
Rat LYLAICRKQRTLPSLDIMVWS ELPPGAGLGSSAAYSVCVAA
Bovine LYLSICQSQRALPSLDITVWS ELPTGAGLGSSAAYSVCLAA
Slime mold LFCALTKCTK---AYNIKITS DLPIGAGLGSSASFCVSICA
Baker's yeast MFVCLCPHAK---NIKFSLKS TLPIGAGLGSSASISVSLAL
Fission yeast LFTSLSSPSQ---GCTLTISS QVPLGAGLGSSATISVVVAT
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
1 – 396
Mevalonate kinase
Active site
146 – 146
Proton donor
Metal binding
146 – 146
Magnesium
Binding site
135 – 135
ATP
Mutagenesis
145 – 145
S -> A. Modest changes in KM for ATP. 20-fold increase in KM for mevalonate. Approximately 2-fold decrease in Vmax.
Mutagenesis
146 – 146
S -> A. Modest changes in KM for ATP. 20-fold increase in KM for mevalonate. 4000-fold decrease in Vmax.
Mutagenesis
149 – 149
Y -> A. No effect on kinase activity. Approximately 4- and 8-fold decrease affinities for ATP and mevalonate, respectively.
Beta strand
129 – 137
Literature citations
Organization of the mevalonate kinase (MVK) gene and identification of novel mutations causing mevalonic aciduria and hyperimmunoglobulinaemia D and periodic fever syndrome.
Houten S.M.; Koster J.; Romeijn G.-J.; Frenkel J.; Di Rocco M.; Caruso U.; Landrieu P.; Kelley R.I.; Kuis W.; Poll-The B.T.; Gibson K.M.; Wanders R.J.A.; Waterham H.R.;
Eur. J. Hum. Genet. 9:253-259(2001)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS HIDS PRO-20; PRO-39; LEU-135; THR-148; THR-268 AND ILE-377; VARIANTS MEVA PRO-20; PHE-264; THR-268; MET-310 AND THR-334;
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.