Sequence information
Variant position: 211 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:
QGERMIHGNPSGVDNAVSTW
G GALRYHQGKISSLKRSPALQ
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 QGERMIHGNPSGVDNAVSTWG GALRYHQ----GKISS------L--KRSPALQ
Mouse EGERVIHGNPSGVDNAVSTWG GALRFQQ----GTMSS----
Rat EGERVIHGNPSGVDNSVSTWG GALRYQQ----GKMSS----
Bovine QGERVIHGNPSGVDNAVSTWG GALRYQQ----GKISS----
Slime mold QGEKIMHGTPSGIDNAVATFG KALTFTR----KNGYK----
Baker's yeast IGEKCIHGTPSGIDNAVATYG NALLFEKDSHNGTINT-NNF
Fission yeast LGECCIHGTPSGIDNAVATNG GLIAFRK----ATAHQSAMK
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
204 – 204
Proton acceptor
Metal binding
193 – 193
Magnesium
Mutagenesis
193 – 193
E -> Q. No change in protein stability. Decreased kinase activity. Approximately 50-fold decrease in Vmax. Approximately 20- and 40-fold decrease affinities for ATP and mevalonate, respectively.
Mutagenesis
196 – 196
I -> A. No effect on kinase activity. Approximately 2- and 3-fold decrease affinities for ATP and mevalonate, respectively.
Mutagenesis
201 – 201
S -> A. Modest changes in KM for ATP. 100-fold increase in KM for mevalonate. Approximately 2-fold increase in Vmax.
Mutagenesis
204 – 204
D -> A. No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate.
Mutagenesis
204 – 204
D -> N. No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate.
Literature citations
MVK mutations and associated clinical features in Italian patients affected with autoinflammatory disorders and recurrent fever.
D'Osualdo A.; Picco P.; Caroli F.; Gattorno M.; Giacchino R.; Fortini P.; Corona F.; Tommasini A.; Salvi G.; Specchia F.; Obici L.; Meini A.; Ricci A.; Seri M.; Ravazzolo R.; Martini A.; Ceccherini I.;
Eur. J. Hum. Genet. 13:314-320(2005)
Cited for: VARIANTS HIDS GLN-20; ILE-132; THR-148; ARG-171; GLU-211; GLN-215; ILE-250; ARG-265; THR-268; MET-310; VAL-376 AND ILE-377; VARIANTS ASN-52 AND MET-356;
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.