Variant position: 260 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 335 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 MTLSQVKGFVRKNGVNEAKI DEIKNDNVQDTAEQKVQLLRN
Rhesus macaque MTLSQVKDFVRKNGVSEAKI DEIKNDNVQDTAEQKVQLLRN
Mouse MTIQEAKKFARENNIKEGKI DEIMHDSIQDTAEQKVQLLLC
Rat MKICDAKKFARQHKIPESKI DEIEHNSPQDAAEQKIQLLQC
Pig MKITEVKDFVRKNGIEETKI DEIMHDNPKDTAEQKVQLLRN
Bovine MRITEVKEFVRKNGMEEAKI DDIMHDNVHETAEQKVQLLRN
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
26 – 335 Tumor necrosis factor receptor superfamily member 6
191 – 335 Cytoplasmic
230 – 314 Death
212 – 317 Interaction with HIPK3
87 – 335 Missing. In isoform 3.
104 – 335 Missing. In isoform 2.
133 – 335 Missing. In isoform 5.
150 – 335 Missing. In isoform 4.
221 – 335 Missing. In isoform 7.
250 – 250 R -> E. Strongly decreased interaction with FADD.
261 – 261 E -> K. Loss of interaction with FADD.
256 – 265
Fas gene mutations in the Canale-Smith syndrome, an inherited lymphoproliferative disorder associated with autoimmunity.
Drappa J.; Vaishnaw A.K.; Sullivan K.E.; Chu J.-L.; Elkon K.B.;
N. Engl. J. Med. 335:1643-1649(1996)
Cited for: VARIANT ALPS1A TYR-260;
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;
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.