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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P05166: Variant p.Arg512Cys

Propionyl-CoA carboxylase beta chain, mitochondrial
Gene: PCCB
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Variant information Variant position: help 512 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 Cysteine (C) at position 512 (R512C, p.Arg512Cys). 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 (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 PA-2; affects heteromeric and homomeric assembly. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 512 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 539 The length of the canonical sequence.
Location on the sequence: help NPFPAAVRGFVDDIIQPSST R ARICCDLDVLASKKVQRPWR 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: 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 29 – 539 Propionyl-CoA carboxylase beta chain, mitochondrial
Domain 294 – 533 CoA carboxyltransferase C-terminal
Region 32 – 533 Carboxyltransferase
Helix 511 – 521



Literature citations
Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients.
Rodriguez-Pombo P.; Hoenicka J.; Muro S.; Perez B.; Perez-Cerda C.; Richard E.; Desviat L.R.; Ugarte M.;
Am. J. Hum. Genet. 63:360-369(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS PA-2; VARIANTS PA-2 PRO-44; ARG-106; ARG-131; TRP-165; LYS-168; ASP-198; TRP-410; VAL-497; CYS-512 AND PRO-519; Effect of PCCB gene mutations on the heteromeric and homomeric assembly of propionyl-CoA carboxylase.
Muro S.; Perez B.; Desviat L.R.; Rodriguez-Pombo P.; Perez-Cerda C.; Clavero S.; Ugarte M.;
Mol. Genet. Metab. 74:476-483(2001)
Cited for: CHARACTERIZATION OF VARIANTS PA-2 GLN-165; VAL-497; CYS-512; PRO-519 AND ASP-536; CHARACTERIZATION OF VARIANT VAL-497; Mutation spectrum of the PCCA and PCCB genes in Japanese patients with propionic acidemia.
Yang X.; Sakamoto O.; Matsubara Y.; Kure S.; Suzuki Y.; Aoki Y.; Yamaguchi S.; Takahashi Y.; Nishikubo T.; Kawaguchi C.; Yoshioka A.; Kimura T.; Hayasaka K.; Kohno Y.; Iinuma K.; Ohura T.;
Mol. Genet. Metab. 81:335-342(2004)
Cited for: VARIANTS PA-2 PRO-153; TRP-165; TRP-410; ILE-428 AND CYS-512; Characterization of four variant forms of human propionyl-CoA carboxylase expressed in Escherichia coli.
Jiang H.; Rao K.S.; Yee V.C.; Kraus J.P.;
J. Biol. Chem. 280:27719-27727(2005)
Cited for: CHARACTERIZATION OF VARIANTS PA-2 TRP-165; LYS-168 AND TRP-410 AND CYS-512; CHARACTERIZATION OF VARIANT VAL-497; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; PATHWAY;
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.