Sequence information
Variant position: 150 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:
DIVVWSELPPGAGLGSSAAY
S VCLAAALLTVCEEIPNPLKD
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 DIVVWSELPPGAGLGSSAAYS VCLAAALL-----TVCEEIPNPLKD
Mouse DMVVWSELPPGAGLGSSAAYS VCLAAALL-----TACEEVS
Rat DIMVWSELPPGAGLGSSAAYS VCVAAALL-----TACEEVT
Bovine DITVWSELPTGAGLGSSAAYS VCLAAALL-----TACEEIP
Slime mold NIKITSDLPIGAGLGSSASFC VSICAGLLKAFDTYICGGCK
Baker's yeast KFSLKSTLPIGAGLGSSASIS VSLALAMA-----YLGGLI-
Fission yeast TLTISSQVPLGAGLGSSATIS VVVATSLL-----LAFGNIE
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.
Helix
145 – 160
Literature citations
Molecular analysis of MVK mutations and enzymatic activity in hyper-IgD and periodic fever syndrome.
Cuisset L.; Drenth J.P.H.; Simon A.; Vincent M.-F.; van der Velde-Visser S.D.; van der Meer J.W.M.; Grateau G.; Delpech M.;
Eur. J. Hum. Genet. 9:260-266(2001)
Cited for: VARIANTS HIDS ASN-20; PRO-20; PRO-39; LEU-150; LEU-167; ARG-202; GLN-215; THR-268; SER-309; ARG-326 AND ILE-377; VARIANT MEVA THR-334; VARIANT ASN-52;
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.