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:
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 QSIRALRDFLRKEYGGLDVL VNNAGIAFKVADPTPFHIQAE
Mouse QSIRALRDFLLKEYGGLDVL VNNAGIAFKVNDDTPFHIQAE
Rat QSIRALRDFLLQEYGGLNVL VNNAGIAFKVVDPTPFHIQAE
Pig QSIRALCDFLRKEYGGLDVL VNNAAIAFQLDNPTPFHIQAE
Bovine QSIRALRDFLRKEYGGLDVL VNNAGIAFKTADTTPFHIQAE
Rabbit QSIRALRDFLRRAYGGLNVL VNNAVIAFKMEDTTPFHIQAE
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
2 – 277 Carbonyl reductase [NADPH] 1
90 – 90 NADP; via carbonyl oxygen
106 – 106 Glutathione
82 – 89
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;
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.