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UniProtKB/Swiss-Prot P35520: Variant p.Gly307Ser

Cystathionine beta-synthase
Gene: CBS
Variant information

Variant position:  307
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 307 (G307S, p.Gly307Ser).
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; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation.
Any additional useful information about the variant.

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



Sequence information

Variant position:  307
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:   LAEPEELNQTEQTTYEVEGI  G YDFIPTVLDRTVVDKWFKSN
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                         LAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSN

Mouse                         LAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKSN

Rat                           LAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVDRWFKSN

Rabbit                        LAEPEELNQTEVTAYEVEGIGYDFIPTVLDRTVVDRWFKST

Slime mold                    LAQPESLNNTNKS-YKIEGIGYDFIPNVLERKLVDQWIKTD

Baker's yeast                 LAQPENLNKTDITDYKVEGIGYDFVPQVLDRKLIDVWYKTD

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


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;

Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria.
Hu F.L.; Gu Z.; Kozich V.; Kraus J.P.; Ramesh V.; Shih V.E.;
Hum. Mol. Genet. 2:1857-1860(1993)
Cited for: VARIANTS CBSD THR-278 AND SER-307;

A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene.
Kruger W.D.; Cox D.R.;
Hum. Mol. Genet. 4:1155-1161(1995)
Cited for: VARIANTS CBSD MET-168; HIS-224; THR-278; SER-307; VAL-331 AND GLU-454;

Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria.
Kim C.E.; Gallagher P.M.; Guttormsen A.B.; Refsum H.; Ueland P.M.; Ose L.; Foelling I.; Whitehead A.S.; Tsai M.Y.; Kruger W.D.;
Hum. Mol. Genet. 6:2213-2221(1997)
Cited for: VARIANTS CBSD MET-262; LYS-266; THR-278; SER-307; ALA-320 AND CYS-369;

Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99.
Kozich V.; Janosik M.; Sokolova J.; Oliveriusova J.; Orendac M.; Kraus J.P.; Elleder D.;
J. Inherit. Metab. Dis. 20:363-366(1997)
Cited for: VARIANTS CBSD LYS-176; THR-278 AND SER-307;

Characterization of mutations in the cystathionine beta-synthase gene in Irish patients with homocystinuria.
Gallagher P.M.; Naughten E.; Hanson N.Q.; Schwichtenberg K.; Bignell M.; Yuan M.; Ward P.; Yap S.; Whitehead A.S.; Tsai M.Y.;
Mol. Genet. Metab. 65:298-302(1998)
Cited for: VARIANTS CBSD PRO-101; LYS-228; MET-262; THR-278; SER-307 AND PRO-355;

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;

Cystathionine beta-synthase deficiency in Georgia (USA): correlation of clinical and biochemical phenotype with genotype.
Kruger W.D.; Wang L.; Jhee K.H.; Singh R.H.; Elsas L.J. II;
Hum. Mutat. 22:434-441(2003)
Cited for: VARIANTS CBSD PRO-101; THR-226; SER-228; PRO-231; THR-278; SER-307; ALA-320; MET-353; ASN-376 AND LYS-526; CHARACTERIZATION OF VARIANTS CBSD PRO-101; THR-226; SER-228; PRO-231; THR-278; SER-307; ALA-320; MET-353; ASN-376 AND LYS-526;

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.