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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P25445: Variant p.Arg250Gln

Tumor necrosis factor receptor superfamily member 6
Gene: FAS
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Variant information Variant position: help 250 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Arginine (R) to Glutamine (Q) at position 250 (R250Q, p.Arg250Gln). 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: help Change from large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In ALPS1A; no effect on interaction with FADD. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 250 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 335 The length of the canonical sequence.
Location on the sequence: help SKYITTIAGVMTLSQVKGFV R KNGVNEAKIDEIKNDNVQDT 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         SKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDT

Rhesus macaque                SKYITTIAGAMTLSQVKDFVRKNGVSEAKIDEIKNDNVQDT

Mouse                         SKYIPRIAEDMTIQEAKKFARENNIKEGKIDEIMHDSIQDT

Rat                           NKYIWRTAEKMKICDAKKFARQHKIPESKIDEIEHNSPQDA

Pig                           GKYITRIAEQMKITEVKDFVRKNGIEETKIDEIMHDNPKDT

Bovine                        GKYIPSIAEQMRITEVKEFVRKNGMEEAKIDDIMHDNVHET
Sequence annotation in neighborhood: help 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 26 – 335 Tumor necrosis factor receptor superfamily member 6
Topological domain 191 – 335 Cytoplasmic
Domain 230 – 314 Death
Region 212 – 317 Interaction with HIPK3
Region 230 – 254 Interaction with CALM
Glycosylation 250 – 250 (Microbial infection) N-beta-linked (GlcNAc) arginine
Alternative sequence 87 – 335 Missing. In isoform 3.
Alternative sequence 104 – 335 Missing. In isoform 2.
Alternative sequence 133 – 335 Missing. In isoform 5.
Alternative sequence 150 – 335 Missing. In isoform 4.
Alternative sequence 221 – 335 Missing. In isoform 7.
Mutagenesis 250 – 250 R -> A. Abolished GlcNAcylation by E.coli NleB1.
Mutagenesis 250 – 250 R -> E. Strongly decreased interaction with FADD.
Mutagenesis 261 – 261 E -> K. Loss of interaction with FADD.



Literature citations
Autoimmune lymphoproliferative syndrome with defective Fas: genotype influences penetrance.
Jackson C.E.; Fischer R.E.; Hsu A.P.; Anderson S.M.; Choi Y.; Wang J.; Dale J.K.; Fleisher T.A.; Middelton L.A.; Sneller M.C.; Lenardo M.J.; Straus S.E.; Puck J.M.;
Am. J. Hum. Genet. 64:1002-1014(1999)
Cited for: VARIANTS ALPS1A LYS-241 AND GLN-250; The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations.
Wang L.; Yang J.K.; Kabaleeswaran V.; Rice A.J.; Cruz A.C.; Park A.Y.; Yin Q.; Damko E.; Jang S.B.; Raunser S.; Robinson C.V.; Siegel R.M.; Walz T.; Wu H.;
Nat. Struct. Mol. Biol. 17:1324-1329(2010)
Cited for: CHARACTERIZATION OF VARIANTS ALPS1A CYS-232; GLN-250; ASP-257; TYR-260; VAL-260; LYS-270 AND LYS-272; MUTAGENESIS OF ARG-250; GLU-261; GLN-283 AND LYS-287;
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.