Variant position: 373 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 431 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 APEKQRTLNEIYHWFTRMFA FFRNHPATWKNAIRHNLSLHK
Mouse APERQRTLNEIYHWFTRMFA YFRNHPATWKNAIRHNLSLHK
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 – 431 Forkhead box protein P3
1 – 417 Forkhead box protein P3, C-terminally processed
52 – 417 Forkhead box protein P3 41 kDa form
337 – 423 Fork-head
393 – 393 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
382 – 382 K -> KVSSSEVAVTGMASSAIAAQSGQAWVWAHRHIGEERDVGCWWWLLASEVDAHLLPVPGLPQ. In isoform 3.
370 – 370 M -> T. Disrupts dimerization but does not affect DNA-binding; when associated with Q-348. Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with Q-348 and P-372.
372 – 372 A -> P. Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with Q-348 and T-370.
372 – 375
Structure of a domain-swapped FOXP3 dimer on DNA and its function in regulatory T cells.
Bandukwala H.S.; Wu Y.; Feuerer M.; Chen Y.; Barboza B.; Ghosh S.; Stroud J.C.; Benoist C.; Mathis D.; Rao A.; Chen L.;
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 336-417 IN COMPLEX WITH DNA AND NFATC2; FUNCTION; SUBUNIT; DOMAIN FORK-HEAD; INTERACTION WITH NFATC2; CHARACTERIZATION OF VARIANTS IPEX GLU-251 DEL; HIS-347; CYS-371 AND ALA-373; MUTAGENESIS OF TRP-348; MET-370 AND ALA-372;
Clinical and molecular profile of a new series of patients with immune dysregulation, polyendocrinopathy, enteropathy, X-linked syndrome: inconsistent correlation between forkhead box protein 3 expression and disease severity.
Gambineri E.; Perroni L.; Passerini L.; Bianchi L.; Doglioni C.; Meschi F.; Bonfanti R.; Sznajer Y.; Tommasini A.; Lawitschka A.; Junker A.; Dunstheimer D.; Heidemann P.H.; Cazzola G.; Cipolli M.; Friedrich W.; Janic D.; Azzi N.; Richmond E.; Vignola S.; Barabino A.; Chiumello G.; Azzari C.; Roncarolo M.G.; Bacchetta R.;
J. Allergy Clin. Immunol. 122:1105-1112(2008)
Cited for: VARIANTS IPEX PRO-242; LEU-324; ALA-339; HIS-347; ALA-373; CYS-374 AND THR-384; CHARACTERIZATION OF VARIANTS IPEX PRO-242; LEU-324; ALA-339; HIS-347; ALA-373; CYS-374 AND THR-384;
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.