UniProtKB/Swiss-Prot P52815: Variant p.Ala181Val

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 181 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LP/P [Disclaimer: Variants classification is intended for research purposes only, not for clinical and diagnostic use. The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant.] 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 Alanine (A) to Valine (V) at position 181 (A181V, p.Ala181Val). 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 hydrophobic (A) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: 0 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 COXPD45; MRPL12 steady state level are reduced in patient fibroblasts; results in defective mt-LSU assembly; reduced mitochondrial translation with a significant decrease of synthesis of COXI, COXII and COXIII subunits. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs577290119 [ dbSNP | Ensembl ]

Sequence information

Variant position: 181 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 198 The length of the canonical sequence.
Location on the sequence: AKKLVESLPQEIKANVAKAE A EKIKAALEAVGGTVVLE 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.
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	37 – 198	Large ribosomal subunit protein bL12m, long mature form
Chain	45 – 198	Large ribosomal subunit protein bL12m, short mature form
Modified residue	162 – 162	N6-succinyllysine
Modified residue	163 – 163	N6-acetyllysine
Modified residue	173 – 173	N6-acetyllysine
Modified residue	178 – 178	N6-acetyllysine; alternate
Modified residue	178 – 178	N6-succinyllysine; alternate
Modified residue	185 – 185	N6-acetyllysine
Mutagenesis	163 – 163	K -> QR. No effect on promoter binding activity of POLRMT.
Mutagenesis	173 – 173	K -> Q. No effect on promoter binding activity of POLRMT.
Mutagenesis	173 – 173	K -> R. Reduced promoter binding activity of POLRMT.

Literature citations

Mutations in mitochondrial ribosomal protein MRPL12 leads to growth retardation, neurological deterioration and mitochondrial translation deficiency.
Serre V.; Rozanska A.; Beinat M.; Chretien D.; Boddaert N.; Munnich A.; Roetig A.; Chrzanowska-Lightowlers Z.M.;
Biochim. Biophys. Acta 1832:1304-1312(2013)
Cited for: FUNCTION; INVOLVEMENT IN COXPD45; VARIANT COXPD45 VAL-181; CHARACTERIZATION OF VARIANT COXPD45 VAL-181;