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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P35520: Variant p.Gly148Arg

Cystathionine beta-synthase
Gene: CBS
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Variant information Variant position: help 148 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 Glycine (G) to Arginine (R) at position 148 (G148R, p.Gly148Arg). 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 glycine (G) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 148 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 EDAERDGTLKPGDTIIEPTS G NTGIGLALAAAVRGYRCIIV 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                         EDAERDGTLKPG-DTIIEPTSGNTGIGLALAAAVRGYRCIIV

Mouse                         EDAERAGNLKPG-DTIIEPTSGNTGIGLALAAAVKGYRCII

Rat                           EDAERAGTLKPG-DTIIEPTSGNTGIGLALAAAVKGYRCII

Rabbit                        EDAERAGTLRPG-DTIIEPTSGNTGIGLALAAAVKGYRCII

Slime mold                    VDAEESGRIKKG-DTLIEPTSGNTGIGLALTAAIKGYKMII

Baker's yeast                 EEAEASGRIHPSRSTLIEPTSGNTGIGLALIGAIKGYRTII
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 149 – 149



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; Identification and functional analysis of two novel mutations in the CBS gene in Polish patients with homocystinuria.
Orendac M.; Pronicka E.; Kubalska J.; Janosik M.; Sokolova J.; Linnebank M.; Koch H.G.; Kozich V.;
Hum. Mutat. 23:631-631(2004)
Cited for: VARIANTS CBSD MET-143; ARG-148; LYS-228 AND THR-278; CHARACTERIZATION OF VARIANTS CBSD MET-143 AND ARG-148; 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.