Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P35520: Variant p.Arg336Cys

Cystathionine beta-synthase
Gene: CBS
Feedback?
Variant information Variant position: help 336 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 336 (R336C, p.Arg336Cys). 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 CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 336 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 551 The length of the canonical sequence.
Location on the sequence: help DRTVVDKWFKSNDEEAFTFA R MLIAQEGLLCGGSAGSTVAV 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         DRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAV

Mouse                         DRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAV

Rat                           DRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAV

Rabbit                        DRTVVDRWFKSTDKEAFAFARMLIAQEGLLCGGSAGSAVAV

Slime mold                    ERKLVDQWIKTDDKESFIMARRLIKEEGLLCGGSSGSAMVG

Baker's yeast                 DRKLIDVWYKTDDKPSFKYARQLISNEGVLVGGSSGSAFTA
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 1 – 551 Cystathionine beta-synthase
Binding site 349 – 349
Helix 328 – 342



Literature citations
Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype.
de Franchis R.; Kraus E.; Kozich V.; Sebastio G.; Kraus J.P.;
Hum. Mutat. 13:453-457(1999)
Cited for: VARIANTS CBSD TRP-58; VAL-126; LYS-302 AND CYS-336; 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; 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; 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; 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; CBS gene mutations found in a Chinese pyridoxine-responsive homocystinuria patient.
Kwok J.S.; Fung S.L.; Lui G.C.; Law E.L.; Chan M.H.; Leung C.B.; Tang N.L.;
Pathology 43:81-83(2011)
Cited for: VARIANTS CBSD THR-278 AND CYS-336;
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.