Variant position: 427 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 PW---WWHLRVQELGLSAPLTVL PTITCGHTIEILREKGFDQAP
Mouse PW---WWRLRVQELSLSAPLTVL PTVTCEDTIAILREKGFD
Rat PW---WWHLRVQELSLSAPLTVL PTVTCEHTIAILREKGFD
Rabbit PW---WWHLRVQELSLSVPLTVL PGVTCSDTIDILRGKGFD
Slime mold QEEEKYHGATVKDLTLPKPITIS ATTTCAAAVQLLQQYGFD
Baker's yeast KYADVFGNATVKDLHLKPVVSVK ETAKVTDVIKILKDNGFD
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
418 – 476 CBS
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;
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.