Variant position: 167 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 624 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 MGEKCVLHVMNGAVMYQIDS VVRACSDFLVQQLDPSNAIGI
Mouse VGEKCVLHVMNGAVMYQIDS VVRACSDFLVQQLDPSNAIGI
Rat VGEKCVLHVMNGAVMYQIDS VVRACSDFLVQQLDPSNAIGI
Pig MGEKCVLHVMNGAVMYQIDS VVRACSDFLVQQLDPSNAIGI
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 – 624 Kelch-like ECH-associated protein 1
151 – 151 Sensor for electrophilic agents
151 – 151 S-(2,3-dicarboxypropyl)cysteine; alternate
151 – 151 S-(2-succinyl)cysteine; alternate
151 – 151 S-nitrosocysteine; alternate
151 – 151 N5-[4-(S-L-cysteinyl)-5-methyl-1H-imidazol-2-yl]-L-ornithine (Cys-Arg) (interchain with R-135 in KEAP1)
151 – 151 C -> SNDL. Substitution with a small side chain that prevents covalent modification by an electrophile; promotes constitutive ubiquitination of NFE2L2/NRF2 and subsequent repression of phase 2 detoxifying enzymes. Resistance of ubiquitination of PGAM5 to inhibition by oxidative stress and sulforaphane. Impaired interaction with CUL3. Reduced formation of a high-molecular mass KEAP1 molecule when methylglyoxal accumulates.
151 – 151 C -> WY. Substitution with a bulky side chain that mimicks covalent modification by an electrophile; prevents ubiquitination and degradation of NFE2L2/NRF2, leading to constitutive activation of NFE2L2/NRF2 and subsequent expression of phase 2 detoxifying enzymes.
165 – 177
Dysfunctional KEAP1-NRF2 interaction in non-small-cell lung cancer.
Singh A.; Misra V.; Thimmulappa R.K.; Lee H.; Ames S.; Hoque M.O.; Herman J.G.; Baylin S.B.; Sidransky D.; Gabrielson E.; Brock M.V.; Biswal S.;
PLoS Med. 3:1865-1876(2006)
Cited for: VARIANTS PHE-167; HIS-236; LEU-284; CYS-333 AND SER-350; CHARACTERIZATION OF VARIANTS HIS-236 AND CYS-333;
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.