UniProtKB/SwissProt variant VAR

Variant information

Variant position:

329

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

Disease [Disclaimer]

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

From Lysine (K) to Glutamate (E) at position 329 (K329E, p.Lys329Glu).

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 large size and basic (K) to medium size and acidic (E)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

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:

In ACADMD; most common variant.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs77931234 [ dbSNP | Ensembl ]

Sequence information

Variant position:

329

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:

421

The length of the canonical sequence.

Location on the sequence:

FGKLLVEHQAISFMLAEMAM K VELARMSYQRAAWEVDSGRR

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                         FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR

Chimpanzee                    FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR

Mouse                         FGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRR

Rat                           FGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRR

Pig                           FGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRR

Bovine                        FGKLLIEHQGISFLLAEMAMKVELARLSYQRAAWEVDSGRR

Caenorhabditis elegans        FGTVIANHQAVQFMLADMAVNLELARLITYKSANDVDNKVR

Drosophila                    FGVPIAYHQAVQFMLADMAIGVETSRLAWRLSAWEIDQGRR

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	26 – 421	Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Helix	317 – 345

Literature citations

Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency.
Matsubara Y.; Narisawa K.; Miyabayashi S.; Tada K.; Coates P.M.; Bachmann C.; Elsas L.J. II; Pollitt R.J.; Rhead W.J.; Roe C.R.;
Biochem. Biophys. Res. Commun. 171:498-505(1990)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342; VARIANT ACADMD GLU-329;

Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation.
Yokota I.; Indo Y.; Coates P.M.; Tanaka K.;
J. Clin. Invest. 86:1000-1003(1990)
Cited for: VARIANT ACADMD GLU-329;

Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency.
Kelly D.P.; Whelan A.J.; Ogden M.L.; Alpers R.; Zhang Z.F.; Bellus G.; Gregersen N.; Dorland L.; Strauss A.W.;
Proc. Natl. Acad. Sci. U.S.A. 87:9236-9240(1990)
Cited for: VARIANT ACADMD GLU-329;

Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli.
Gregersen N.; Andresen B.S.; Bross P.; Winter V.; Ruediger N.; Engst S.; Christensen E.; Kelly D.; Strauss A.W.; Koelvraa S.; Bolund L.; Ghisla S.;
Hum. Genet. 86:545-551(1991)
Cited for: VARIANT ACADMD GLU-329;

Frequency of the G985 MCAD mutation in the general population.
Blakemore A.I.; Singleton H.; Pollitt R.J.; Engel P.C.; Kolvraa S.; Gregersen N.; Curtis D.;
Lancet 337:298-299(1991)
Cited for: VARIANT ACADMD GLU-329 FREQUENCY;

Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency.
Yang B.-Z.; Ding J.-H.; Zhou C.; Dimachkie M.M.; Sweetman L.; Dasouki M.J.; Wilkinson J.; Roe C.R.;
Mol. Genet. Metab. 69:259-262(2000)
Cited for: VARIANTS ACADMD LEU-206 AND GLU-329;

Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency.
Albers S.; Levy H.L.; Irons M.; Strauss A.W.; Marsden D.;
J. Inherit. Metab. Dis. 24:417-418(2001)
Cited for: VARIANTS ACADMD THR-281 AND GLU-329;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P11310: Variant p.Lys329Glu