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UniProtKB/Swiss-Prot P35520: Variant p.Arg379Gln

Cystathionine beta-synthase
Gene: CBS
Variant information

Variant position:  379
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 379 (R379Q, p.Arg379Gln).
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; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure.
Any additional useful information about the variant.

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



Sequence information

Variant position:  379
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:   KAAQELQEGQRCVVILPDSV  R NYMTKFLSDRWMLQKGFLKE
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                         KAAQ---ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKE

Mouse                         KAAR---ELQEGQRCVVILPDSVRNYMSKFLSDKWMLQKGF

Rat                           KAAQ---ELKEGQRCVVILPDSVRNYMSKFLSDKWMLQKGF

Rabbit                        KAAQ---ELQEGQRCVVILPDSVRNYMSKFLSDRWMLQKGF

Slime mold                    LAAK---QLKKGQRCVVLLADSIRNYMTKHLNDDWLVDNGF

Baker's yeast                 KYCEDHPELTEDDVIVAIFPDSIRSYLTKFVDDEWLKKNNL

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
Helix 378 – 381


Literature citations

Spectrum of CBS mutations in 16 homocystinuric patients from the iberian peninsula: high prevalence of T191M and absence of I278T or G307S.
Urreizti R.; Balcells S.; Rodes M.; Vilarinho L.; Baldellou A.; Couce M.L.; Munoz C.; Campistol J.; Pinto X.; Vilaseca M.A.; Grinberg D.;
Hum. Mutat. 22:103-103(2003)
Cited for: VARIANTS CBSD TRP-125; MET-191; TYR-275; CYS-336; PRO-338; ASN-349; GLN-379 AND PRO-456;

Functional assays testing pathogenicity of 14 cystathionine-beta synthase mutations.
Urreizti R.; Asteggiano C.; Cozar M.; Frank N.; Vilaseca M.A.; Grinberg D.; Balcells S.;
Hum. Mutat. 27:211-211(2006)
Cited for: CHARACTERIZATION OF VARIANTS CBSD TRP-125; ARG-148; VAL-173; MET-191; THR-226; TYR-275; CYS-336; HIS-336; PRO-338; ASN-349; GLN-379 AND PRO-456; CHARACTERIZATION OF VARIANT GLN-548;

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.