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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P53602: Variant p.Arg161Gln

Diphosphomevalonate decarboxylase
Gene: MVD
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Variant information Variant position: help 161 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 Arginine (R) to Glutamine (Q) at position 161 (R161Q, p.Arg161Gln). 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 large size and basic (R) to medium size and polar (Q) 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 POROK7; 1000-fold diminution in diphosphomevalonate decarboxylase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 161 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 400 The length of the canonical sequence.
Location on the sequence: help VYGVESDLSEVARRGSGSAC R SLYGGFVEWQMGEQADGKDS 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                         VYGV---ESDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKDS

Mouse                         VYGV---EGDLSEVARRGSGSACRSLYGGFVEWQMGEQADG

Rat                           VYGV---EGDLSEVARRGSGSACRSLYGGFVEWQMGEQADG

Bovine                        VYGV---DSDLSEVARRGSGSACRSLYGGFVEWQMGERPDG

Zebrafish                     LFNV---EGELSGVARQGSGSACRSLYGGFVQWKLGEQSDG

Slime mold                    MYGV---DGDISGIARLGSGSACRSMYGGFVKWEMGTKDDG

Baker's yeast                 LYQLPQSTSEISRIARKGSGSACRSLFGGYVAWEMGKAEDG

Fission yeast                 LYDLPWTPTQLSRIARQGSGSACRSLFGGYVAWEMGELHSG
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 2 – 400 Diphosphomevalonate decarboxylase
Binding site 156 – 161
Helix 157 – 163



Literature citations
Genomic variations of the mevalonate pathway in porokeratosis.
Zhang Z.; Li C.; Wu F.; Ma R.; Luan J.; Yang F.; Liu W.; Wang L.; Zhang S.; Liu Y.; Gu J.; Hua W.; Fan M.; Peng H.; Meng X.; Song N.; Bi X.; Gu C.; Zhang Z.; Huang Q.; Chen L.; Xiang L.; Xu J.; Zheng Z.; Jiang Z.;
Elife 4:E06322-E06322(2015)
Cited for: INVOLVEMENT IN POROK7; VARIANTS POROK7 ARG-101; VAL-128; GLN-161; LEU-161; GLN-228; TRP-228; SER-249; SER-292; ILE-371 DEL AND ARG-376; Human mevalonate diphosphate decarboxylase: characterization, investigation of the mevalonate diphosphate binding site, and crystal structure.
Voynova N.E.; Fu Z.; Battaile K.P.; Herdendorf T.J.; Kim J.J.; Miziorko H.M.;
Arch. Biochem. Biophys. 480:58-67(2008)
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS); MUTAGENESIS OF ASN-17; CHARACTERIZATION OF VARIANT POROK7 GLN-161; FUNCTION; CATALYTIC ACTIVITY; 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.