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UniProtKB/Swiss-Prot P35520: Variant p.Arg125Gln

Cystathionine beta-synthase
Gene: CBS
Variant information

Variant position:  125
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 Arginine (R) to Glutamine (Q) at position 125 (R125Q, p.Arg125Gln).
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 (R) to medium size and polar (Q)
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 CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  125
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  551
The length of the canonical sequence.

Location on the sequence:   LLAKCEFFNAGGSVKDRISL  R MIEDAERDGTLKPGDTIIEP
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                         LLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPG-DTIIEP

Mouse                         LLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPG-DTIIE

Rat                           LLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPG-DTIIE

Rabbit                        LLAKCEFFNAGGSVKDRISLRMIEDAERAGTLRPG-DTIIE

Slime mold                    LVAKCEFFNAGGSVKDRIGHRMIVDAEESGRIKKG-DTLIE

Baker's yeast                 IYAKLELYNPGGSIKDRIAKSMVEEAEASGRIHPSRSTLIE

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.

TypePositionsDescription
Chain 1 – 551 Cystathionine beta-synthase
Modified residue 119 – 119 N6-(pyridoxal phosphate)lysine
Helix 119 – 132


Literature citations

Cystathionine beta-synthase mutations: effect of mutation topology on folding and activity.
Kozich V.; Sokolova J.; Klatovska V.; Krijt J.; Janosik M.; Jelinek K.; Kraus J.P.;
Hum. Mutat. 31:809-819(2010)
Cited for: CHARACTERIZATION OF VARIANTS CBSD LEU-49; ARG-65; ARG-78; ASN-102; VAL-114; GLN-125; LYS-144; ARG-148; TYR-165; LYS-176; ALA-180; MET-191; LYS-228; ARG-262; LYS-266; THR-278; LYS-302; ARG-305; SER-307; CYS-369; LEU-422; THR-435; GLN-439; ASN-444; LEU-466 AND SER-539; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; ACTIVITY REGULATION; SUBUNIT;

Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria.
Marble M.; Geraghty M.T.; de Franchis R.; Kraus J.P.; Valle D.;
Hum. Mol. Genet. 3:1883-1886(1994)
Cited for: VARIANTS CBSD GLN-125 AND ASP-131;

The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations.
Sebastio G.; Sperandeo M.P.; Panico M.; de Franchis R.; Kraus J.P.; Andria G.;
Am. J. Hum. Genet. 56:1324-1333(1995)
Cited for: VARIANTS CBSD SER-88; GLN-125 AND MET-257;

The molecular basis of cystathionine beta-synthase deficiency in Australian patients: genotype-phenotype correlations and response to treatment.
Gaustadnes M.; Wilcken B.; Oliveriusova J.; McGill J.; Fletcher J.; Kraus J.P.; Wilcken D.E.;
Hum. Mutat. 20:117-126(2002)
Cited for: VARIANTS CBSD LEU-49; PRO-101; ARG-109; GLN-125; LYS-144; TYR-165; LYS-228; THR-278; LYS-302; SER-307; GLU-331; CYS-336; SER-347; MET-353; CYS-369; MET-371 AND GLN-439; CHARACTERIZATION OF VARIANTS CBSD PRO-101; ARG-109; LYS-228 AND SER-347;

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.