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UniProtKB/Swiss-Prot Q9BZS1: Variant p.Ala384Thr

Forkhead box protein P3
Gene: FOXP3
Variant information

Variant position:  384
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 Alanine (A) to Threonine (T) at position 384 (A384T, p.Ala384Thr).
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 small size and hydrophobic (A) to medium size and polar (T)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
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 IPEX; no loss of protein expression.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  384
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:   YHWFTRMFAFFRNHPATWKN  A IRHNLSLHKCFVRVESEKGA
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                         YHWFTRMFAFFRNHPATWKNAIRHNLSLHKCFVRVESEKGA

Mouse                         YHWFTRMFAYFRNHPATWKNAIRHNLSLHKCFVRVESEKGA

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.

TypePositionsDescription
Chain 1 – 431 Forkhead box protein P3
Chain 1 – 417 Forkhead box protein P3, C-terminally processed
Chain 52 – 417 Forkhead box protein P3 41 kDa form
DNA binding 337 – 423 Fork-head
Cross 393 – 393 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence 382 – 382 K -> KVSSSEVAVTGMASSAIAAQSGQAWVWAHRHIGEERDVGCWWWLLASEVDAHLLPVPGLPQ. In isoform 3.
Mutagenesis 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.
Mutagenesis 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.
Helix 381 – 391


Literature citations

X-linked neonatal diabetes mellitus, enteropathy and endocrinopathy syndrome is the human equivalent of mouse scurfy.
Wildin R.S.; Ramsdell F.; Peake J.; Faravelli F.; Casanova J.-L.; Buist N.; Levy-Lahad E.; Mazzella M.; Goulet O.; Perroni L.; Bricarelli F.D.; Byrne G.; McEuen M.; Proll S.; Appleby M.; Brunkow M.E.;
Nat. Genet. 27:18-20(2001)
Cited for: VARIANTS IPEX CYS-371; THR-384 AND TRP-397;

The immune dysregulation, polyendocrinopathy, enteropathy, X-linked syndrome (IPEX) is caused by mutations of FOXP3.
Bennett C.L.; Christie J.; Ramsdell F.; Brunkow M.E.; Ferguson P.J.; Whitesell L.; Kelly T.E.; Saulsbury F.T.; Chance P.F.; Ochs H.D.;
Nat. Genet. 27:20-21(2001)
Cited for: VARIANT IPEX THR-384;

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;

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.