UniProtKB/SwissProt variant VAR

Mineralocorticoid receptor
Gene: NR3C2
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Variant information Variant position:

776 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Glutamine (Q) to Arginine (R) at position 776 (Q776R, p.Gln776Arg). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Change from medium size and polar (Q) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Variant description:

In PHA1A; reduces aldosterone binding. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs121912565 [ dbSNP | Ensembl ]

Sequence information Variant position:

776 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:

SSKPDTAENLLSTLNRLAGK Q MIQVVKWAKVLPGFKNLPLE 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                         SSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLE

Mouse                         NSKPDTAESLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLE

Rat                           NSKPDTAESLLSTLNRLAAKQMIQVVKWAKVLPGFKNLPLE

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	1 – 984	Mineralocorticoid receptor
Domain	726 – 964	NR LBD
Binding site	770 – 770
Binding site	770 – 770
Binding site	770 – 770
Binding site	776 – 776
Binding site	776 – 776
Binding site	776 – 776
Alternative sequence	672 – 788	Missing. In isoform 4.
Alternative sequence	707 – 984	Missing. In isoform 2.
Mutagenesis	767 – 767	S -> N. Loss of transcription transactivation.
Mutagenesis	767 – 767	S -> Q. Strong decrease of transcription transactivation.
Mutagenesis	770 – 770	N -> ADHQST. Abolishes aldosterone binding and transcription transactivation.
Mutagenesis	776 – 776	Q -> A. Reduces aldosterone binding and transcription transactivation.
Mutagenesis	782 – 782	K -> E. Decreased coactivator binding.
Mutagenesis	785 – 785	K -> E. Loss of coactivator binding.
Mutagenesis	796 – 796	E -> R. Decreased coactivator binding.
Helix	762 – 785

Literature citations
Different inactivating mutations of the mineralocorticoid receptor in fourteen families affected by type I pseudohypoaldosteronism.
Sartorato P.; Lapeyraque A.-L.; Armanini D.; Kuhnle U.; Khaldi Y.; Salomon R.; Abadie V.; Di Battista E.; Naselli A.; Racine A.; Bosio M.; Caprio M.; Poulet-Young V.; Chabrolle J.-P.; Niaudet P.; De Gennes C.; Lecornec M.-H.; Poisson E.; Fusco A.M.; Loli P.; Lombes M.; Zennaro M.-C.;
J. Clin. Endocrinol. Metab. 88:2508-2517(2003)
Cited for: CHARACTERIZATION OF VARIANTS PHA1A ARG-633; ARG-776; PRO-924 AND PRO-979;

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.

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08235: Variant p.Gln776Arg