Home  |  Contact

UniProtKB/Swiss-Prot P35520: Variant p.Gly347Ser

Cystathionine beta-synthase
Gene: CBS
Variant information

Variant position:  347
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 Glycine (G) to Serine (S) at position 347 (G347S, p.Gly347Ser).
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 glycine (G) to small size and polar (S)
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 CBSD; protein expression is comparable to wild-type; loss of activity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  347
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:   NDEEAFTFARMLIAQEGLLC  G GSAGSTVAVAVKAAQELQEG
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                         NDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ---ELQEG

Mouse                         NDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAAR---EL

Rat                           NDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQ---EL

Rabbit                        TDKEAFAFARMLIAQEGLLCGGSAGSAVAVAVKAAQ---EL

Slime mold                    DDKESFIMARRLIKEEGLLCGGSSGSAMVGALLAAK---QL

Baker's yeast                 DDKPSFKYARQLISNEGVLVGGSSGSAFTAVVKYCEDHPEL

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
Binding site 349 – 349 Pyridoxal phosphate


Literature citations

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;

Identification and functional analysis of cystathionine beta-synthase gene mutations in patients with homocystinuria.
Lee S.-J.; Lee D.H.; Yoo H.-W.; Koo S.K.; Park E.-S.; Park J.-W.; Lim H.G.; Jung S.-C.;
J. Hum. Genet. 50:648-654(2005)
Cited for: VARIANTS CBSD GLN-154; VAL-155; ASP-234 DEL; MET-257; THR-288; CYS-336; SER-347 AND MET-353; VARIANT CYS-18; CHARACTERIZATION OF VARIANTS CBSD GLN-154; VAL-155; ASP-234 DEL; MET-257; THR-288; CYS-336; SER-347 AND MET-353; CHARACTERIZATION OF VARIANT CYS-18;

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.