UniProtKB/SwissProt variant VAR

Variant information

Variant position:

279

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 Glycine (G) to Arginine (R) at position 279 (G279R, p.Gly279Arg).

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 glycine (G) to large size and basic (R)

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

BLOSUM score:

-2

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 HCP; a patient carrying also the L-12 mutation in ALAD.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs121917874 [ dbSNP | Ensembl ]

Sequence information

Variant position:

279

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

Protein sequence length:

454

The length of the canonical sequence.

Location on the sequence:

FNYRYFEVEEADGNKQWWFG G GCDLTPTYLNQEDAVHFHRT

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                         FNYRYFEVEEADGN-KQWWFGGGCDLTPTYLNQEDAVHFHRT

Mouse                         FNYRYFEVEEADGN-THWWFGGGCDLTPTYLNQEDAVHFHR

Rat                           FNYRYFEVEEADGK-MHWWFGGGCDLTPTYLNREDAVHFHR

Drosophila                    FNYRYFEVETAKGE-KQWWFGGGTDLTPYYLCEKDASHFHQ

Slime mold                    MNVRYFEAG------DVWWFGGGVDLTPVYPKLDQVVEFHS

Baker's yeast                 LNYRYFETWNQDGTPQTWWFGGGADLTPSYLYEEDGQLFHQ

Fission yeast                 LNYRYFELVNSDGK-KIWWFGGGADLTPSILFEEDGKHFHK

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	111 – 454	Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
Alternative sequence	272 – 287	NKQWWFGGGCDLTPTY -> KGLRSYGKYCRAKCAF. In isoform 2.
Beta strand	273 – 284

Literature citations

Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient.
Akagi R.; Inoue R.; Muranaka S.; Tahara T.; Taketani S.; Anderson K.E.; Phillips J.D.; Sassa S.;
Br. J. Haematol. 132:237-243(2006)
Cited for: VARIANT HCP ARG-279;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P36551: Variant p.Gly279Arg