Sequence information
Variant position: 88 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 277 The length of the canonical sequence.
Location on the sequence:
QSIRALRDFLRKEYGGLDVL
V NNAGIAFKVADPTPFHIQAE
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 QSIRALRDFLRKEYGGLDVLV NNAGIAFKVADPTPFHIQAE
Mouse QSIRALRDFLLKEYGGLDVLV NNAGIAFKVNDDTPFHIQAE
Rat QSIRALRDFLLQEYGGLNVLV NNAGIAFKVVDPTPFHIQAE
Pig QSIRALCDFLRKEYGGLDVLV NNAAIAFQLDNPTPFHIQAE
Bovine QSIRALRDFLRKEYGGLDVLV NNAGIAFKTADTTPFHIQAE
Rabbit QSIRALRDFLRRAYGGLNVLV NNAVIAFKMEDTTPFHIQAE
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
Chain
2 – 277
Carbonyl reductase [NADPH] 1
Binding site
90 – 90
NADP; via carbonyl oxygen
Binding site
106 – 106
Glutathione
Beta strand
82 – 89
Literature citations
Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER).
Gonzalez-Covarrubias V.; Kalabus J.L.; Blanco J.G.;
Pharm. Res. 25:1730-1734(2008)
Cited for: ACTIVITY REGULATION; FUNCTION; CHARACTERIZATION OF VARIANT ILE-88;
A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity.
Gonzalez-Covarrubias V.; Ghosh D.; Lakhman S.S.; Pendyala L.; Blanco J.G.;
Drug Metab. Dispos. 35:973-980(2007)
Cited for: VARIANT ILE-88; CHARACTERIZATION OF VARIANT ILE-88; BIOPHYSICOCHEMICAL PROPERTIES; ACTIVITY REGULATION; CATALYTIC ACTIVITY;
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.