Variant position: 810 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 984 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 FKNLPLEDQITLIQYSWMCL SSFALSWRSYKHTNSQFLYFA
Mouse FKNLPLEDQITLIQYSWMCL SSFALSWRSYKHTNSQFLYFA
Rat FKNLPLEDQITLIQYSWMCL SSFALSWRSYKHTNSQLLYFA
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 – 984 Mineralocorticoid receptor
733 – 984 Steroid-binding
817 – 817 Steroid
707 – 984 Missing. In isoform 2.
796 – 796 E -> R. Decreased coactivator binding.
808 – 808 C -> S. Increases aldosterone-binding.
810 – 810 S -> M. Alters receptor specificity.
817 – 817 R -> A. Reduces aldosterone binding and transcription transactivation.
795 – 822
A ligand-mediated hydrogen bond network required for the activation of the mineralocorticoid receptor.
Bledsoe R.K.; Madauss K.P.; Holt J.A.; Apolito C.J.; Lambert M.H.; Pearce K.H.; Stanley T.B.; Stewart E.L.; Trump R.P.; Willson T.M.; Williams S.P.;
J. Biol. Chem. 280:31283-31293(2005)
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 712-984 OF MUTANT SER-808 IN COMPLEXES WITH AGONIST AND ANTAGONISTS; CHARACTERIZATION OF VARIANT EOHSEP LEU-810; MUTAGENESIS OF SER-767; ASN-770 AND THR-945;
Crystal structure of a mutant mineralocorticoid receptor responsible for hypertension.
Fagart J.; Huyet J.; Pinon G.M.; Rochel M.; Mayer C.; Rafestin-Oblin M.-E.;
Nat. Struct. Mol. Biol. 12:554-555(2005)
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 731-984 OF MUTANT LEU-810 IN COMPLEXES WITH STEROID AGONISTS; CHARACTERIZATION OF VARIANT EOHSEP LEU-810; MUTAGENESIS OF GLN-776 AND ARG-817;
Activating mineralocorticoid receptor mutation in hypertension exacerbated by pregnancy.
Geller D.S.; Farhi A.; Pinkerton N.; Fradley M.; Moritz M.; Spitzer A.; Meinke G.; Tsai F.T.F.; Sigler P.B.; Lifton R.P.;
Cited for: VARIANT EOHSEP LEU-810; MUTAGENESIS OF SER-810;
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