Variant position: 423 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 777 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 SSPPSSSSTATTGPPPKLCL VCSDEASGCHYGVLTCGSCKV
Mouse SSPPSSSSTAT-GPPPKLCL VCSDEASVCHYGVLTCGSCKV
Rat SSPPSSSSAAT-GPPPKLCL VCSDEASGCHYGVLTCGSCKV
Pig SSPPSSSSAAT-GPPPKLCL VCSDEASGCHYGVLTCGSCKV
Rabbit SSPPSNSTTAA-GPPPKLCL VCSDEASGCHYGVLTCGSCKV
Xenopus laevis SPSPSTSSTST-GPPPKLCL VCSDEASGCHYGVLTCGSCKV
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 – 777 Glucocorticoid receptor
418 – 493 Nuclear receptor
421 – 441 NR C4-type
404 – 404 Phosphoserine; by GSK3-beta
419 – 419 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
404 – 404 S -> A. Abolishes phosphorylation. Does not affect translocation to the nucleus following ligand stimulation. Increases protein half-life and transcriptional repressor activity. Alters repertoire of regulated genes. Increases cell death.
404 – 404 S -> D. Does not affect translocation to the nucleus following ligand stimulation.
422 – 424
A novel point mutation in the DNA-binding domain (DBD) of the human glucocorticoid receptor causes primary generalized glucocorticoid resistance by disrupting the hydrophobic structure of its DBD.
Roberts M.L.; Kino T.; Nicolaides N.C.; Hurt D.E.; Katsantoni E.; Sertedaki A.; Komianou F.; Kassiou K.; Chrousos G.P.; Charmandari E.;
J. Clin. Endocrinol. Metab. 98:E790-E795(2013)
Cited for: CHARACTERIZATION OF VARIANT GCCR ALA-423;
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