UniProtKB/SwissProt variant VAR

Variant information

Variant position:

205

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

Type of variant:

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:

From Serine (S) to Proline (P) at position 205 (S205P, p.Ser205Pro).

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 small size and polar (S) to medium size and hydrophobic (P)

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 HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs121908520 [ dbSNP | Ensembl ]

Sequence information

Variant position:

205

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

Protein sequence length:

392

The length of the canonical sequence.

Location on the sequence:

VASLGGTPLYMDRQGIDILY S GSQKALNAPPGTSLISFSDK

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                         VASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDK

Mouse                         VASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDK

Rat                           VASLGGVPIYMDQQGIDILYSGSQKVLNAPPGISLISFNDK

Rabbit                        VASLGGAPIYMDQQGIDVLYSGSQKALNAPPGTSLISFSDK

Cat                           VASLCGTPIYMDQQGIDVLYSGSQKVLNSPPGTSLISFSDK

Slime mold                    VAALGGVPVFVDDWKIDACYTGTQKCLSGPPGISPLTFSNA

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 – 392	Alanine--glyoxylate aminotransferase
Modified residue	209 – 209	N6-(pyridoxal phosphate)lysine
Modified residue	225 – 225	N6-acetyllysine; alternate
Modified residue	225 – 225	N6-succinyllysine; alternate
Mutagenesis	209 – 209	K -> R. Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
Beta strand	201 – 209

Literature citations

Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene.
Nishiyama K.; Funai T.; Katafuchi R.; Hattori F.; Onoyama K.; Ichiyama A.;
Biochem. Biophys. Res. Commun. 176:1093-1099(1991)
Cited for: VARIANT HP1 PRO-205;

Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations.
Coulter-Mackie M.B.; Lian Q.;
Mol. Genet. Metab. 89:349-359(2006)
Cited for: CHARACTERIZATION OF VARIANTS HP1 ARG-41; VAL-41; GLU-82; ARG-108; ASP-112; ARG-156; ARG-161; ARG-170; TYR-173; ASN-183; PHE-187; PRO-205 AND LEU-218; MUTAGENESIS OF LYS-209; SUBUNIT;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P21549: Variant p.Ser205Pro