Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P35520: Variant p.Asp444Asn

Cystathionine beta-synthase
Gene: CBS
Feedback?
Variant information Variant position: help 444 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 Aspartate (D) to Asparagine (N) at position 444 (D444N, p.Asp444Asn). 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 medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased 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 444 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 TVLPTITCGHTIEILREKGF D QAPVVDEAGVILGMVTLGNM 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                         TVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNM

Mouse                         TVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNM

Rat                           TVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNM

Rabbit                        TVLPGVTCSDTIDILRGKGFDQAPVVDETGEILGMVTLGNM

Slime mold                    TISATTTCAAAVQLLQQYGFDQLPVVSESKKVLGQLTLGNL

Baker's yeast                 SVKETAKVTDVIKILKDNGFDQLPVLTEDGKLSGLVTLSEL
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
Domain 418 – 476 CBS
Beta strand 444 – 449



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; Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient.
Kluijtmans L.A.J.; Boers G.H.J.; Stevens E.M.B.; Renier W.O.; Kraus J.P.; Trijbels F.J.M.; van den Heuvel L.P.W.J.; Blom H.J.;
J. Clin. Invest. 98:285-289(1996)
Cited for: VARIANT CBSD ASN-444; CHARACTERIZATION OF VARIANT CBSD ASN-444; High homocysteine and thrombosis without connective tissue disorders are associated with a novel class of cystathionine beta-synthase (CBS) mutations.
Maclean K.N.; Gaustadnes M.; Oliveriusova J.; Janosik M.; Kraus E.; Kozich V.; Kery V.; Skovby F.; Ruediger N.; Ingerslev J.; Stabler S.P.; Allen R.H.; Kraus J.P.;
Hum. Mutat. 19:641-655(2002)
Cited for: VARIANTS CBSD ARG-85; THR-278; LEU-422; THR-435; ASN-444 AND LEU-466; CHARACTERIZATION OF VARIANTS CBSD ARG-85; LEU-422; THR-435 AND LEU-466; Insights into the regulatory domain of cystathionine Beta-synthase: characterization of six variant proteins.
Mendes M.I.; Santos A.S.; Smith D.E.; Lino P.R.; Colaco H.G.; de Almeida I.T.; Vicente J.B.; Salomons G.S.; Rivera I.; Blom H.J.; Leandro P.;
Hum. Mutat. 35:1195-1202(2014)
Cited for: VARIANT CBSD GLY-449; CHARACTERIZATION OF VARIANTS CBSD LEU-427; ASN-444; GLY-449; LEU-500 AND GLN-540; CATALYTIC ACTIVITY; Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): Identification and functional analysis of CBS gene mutations in Homocystinuria patients.
Mendes M.I.; Colaco H.G.; Smith D.E.; Ramos R.J.; Pop A.; van Dooren S.J.; Tavares de Almeida I.; Kluijtmans L.A.; Janssen M.C.; Rivera I.; Salomons G.S.; Leandro P.; Blom H.J.;
J. Inherit. Metab. Dis. 37:245-254(2014)
Cited for: VARIANTS CBSD LEU-49; LYS-269 DEL; THR-278; HIS-336; LEU-427; ASN-444; LEU-500 AND GLN-540; CHARACTERIZATION OF VARIANTS CBSD LEU-49; LYS-269 DEL; THR-278; HIS-336; LEU-427; ASN-444; LEU-500 AND GLN-540; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; ACTIVITY REGULATION;
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.