Sequence information
Variant position: 298 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 545 The length of the canonical sequence.
Location on the sequence:
SVPAPLALPSDPQLHQKNED
E CAVCRDGGELICCDGCPRAF
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 SVPAPLALPSDPQLHQKNEDE CAVCRDGGELICCDGCPRAF
Mouse GVPPLPSLPSEPQVNQKNEDE CAVCHDGGELICCDGCPRAF
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 – 545
Autoimmune regulator
Zinc finger
296 – 343
PHD-type 1
Region
295 – 298
Interaction with histone H3 not methylated at 'Lys-4'
Alternative sequence
293 – 293
Q -> PVCMGVSCLCQ. In isoform 4.
Mutagenesis
295 – 295
N -> A. Abolishes interaction with histone H3.
Mutagenesis
297 – 297
D -> A. Strongly reduces interaction with unmethylated histone H3 and abolishes interaction with histone H3 trimethylated at 'Lys-4'. No effect on doted nuclear localization. Dominant-negative effect on target gene transcription.
Mutagenesis
298 – 298
E -> A. Reduces interaction with histone H3.
Mutagenesis
302 – 302
C -> P. Reduces transcriptional activation.
Mutagenesis
303 – 303
R -> P. Alters protein folding and abolishes interaction with histone H3. No effect on doted nuclear localization. Dominant-negative effect on target gene transcription.
Mutagenesis
304 – 304
D -> A. Strongly reduces interaction with histone H3.
Mutagenesis
307 – 307
E -> A. Reduces interaction with histone H3.
Mutagenesis
312 – 312
D -> A. Abolishes interaction with histone H3.
Mutagenesis
312 – 312
D -> N. No effect on doted nuclear localization. Dominant-negative effect on target gene transcription.
Beta strand
298 – 303
Literature citations
Dominant mutations in the autoimmune regulator AIRE are associated with common organ-specific autoimmune diseases.
Oftedal B.E.; Hellesen A.; Erichsen M.M.; Bratland E.; Vardi A.; Perheentupa J.; Kemp E.H.; Fiskerstrand T.; Viken M.K.; Weetman A.P.; Fleishman S.J.; Banka S.; Newman W.G.; Sewell W.A.; Sozaeva L.S.; Zayats T.; Haugarvoll K.; Orlova E.M.; Haavik J.; Johansson S.; Knappskog P.M.; Loevaas K.; Wolff A.S.; Abramson J.; Husebye E.S.;
Immunity 42:1185-1196(2015)
Cited for: INVOLVEMENT IN APS1; FUNCTION; SUBCELLULAR LOCATION; VARIANTS APS1 PRO-28; CYS-90; MET-301; TYR-311 AND LEU-326; CHARACTERIZATION OF VARIANTS PRO-28; CYS-90; MET-301; TYR-311 AND LEU-326; MUTAGENESIS OF 28-LEU-LEU-29; LEU-97; ASP-297; ARG-303; ASP-312; CYS-446 AND ARG-471; VARIANTS LYS-298; TRP-299; TYR-302; GLN-303; TRP-303; SER-305; ARG-306; MET-309; GLN-316; TRP-316; PRO-319; GLN-328; TRP-328; ARG-332 AND ALA-484; CHARACTERIZATION OF VARIANTS LYS-298; TYR-302; SER-305 AND GLN-328;
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.