Variant position: 165 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:
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 PTSGNTGIGLALAAAVRGYR CIIVMPEKMSSEKVDVLRALG
Mouse PTSGNTGIGLALAAAVKGYR CIIVMPEKMSMEKVDVLRALG
Rat PTSGNTGIGLALAAAVKGYR CIIVMPEKMSMEKVDVLRALG
Rabbit PTSGNTGIGLALAAAVKGYR CIIVMPEKMSLEKVDVLRALG
Slime mold PTSGNTGIGLALTAAIKGYK MIITLPEKMSQEKVDVLKALG
Baker's yeast PTSGNTGIGLALIGAIKGYR TIITLPEKMSNEKVSVLKALG
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.
Type Positions Description
1 – 551 Cystathionine beta-synthase
149 – 149 Pyridoxal phosphate
164 – 170
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;
Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients.
Kluijtmans L.A.J.; Blom H.J.; Boers G.H.J.; van Oost B.A.; Trijbels F.J.M.; van den Heuvel L.P.W.J.;
Hum. Genet. 96:249-250(1995)
Cited for: VARIANTS CBSD TYR-165 AND MET-371;
Mutational analysis of the cystathionine beta-synthase gene: a splicing mutation, two missense mutations and an insertion in patients with homocystinuria.
Gordon R.B.; Cox A.J.; Dawson P.A.; Emmerson B.T.; Kraus J.P.; Dudman N.P.;
Hum. Mutat. 11:332-332(1998)
Cited for: VARIANTS CBSD LYS-144 AND TYR-165;
Impaired heme binding and aggregation of mutant cystathionine beta-synthase subunits in homocystinuria.
Janosik M.; Oliveriusova J.; Janosikova B.; Sokolova J.; Kraus E.; Kraus J.P.; Kozich V.;
Am. J. Hum. Genet. 68:1506-1513(2001)
Cited for: VARIANTS CBSD ARG-65; VAL-114; LYS-144; THR-155; TYR-165; LYS-176 AND THR-278; CHARACTERIZATION OF VARIANTS CBSD VAL-114; LYS-144; THR-155; TYR-165; LYS-176 AND THR-278;
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;
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.