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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8WXG6: Variant p.Ser257Phe

MAP kinase-activating death domain protein
Gene: MADD
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Variant information Variant position: help 257 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 Serine (S) to Phenylalanine (F) at position 257 (S257F, p.Ser257Phe). 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 small size and polar (S) to large size and aromatic (F) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 DEEAH; impaired TNFA-induced activation of the MAP kinases ERK1/2; enhanced susceptibility to TNFA-induced apoptosis; decreased EGF internalization. Any additional useful information about the variant.


Sequence information Variant position: help 257 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1647 The length of the canonical sequence.
Location on the sequence: help SSALLHDLREIEAWIYRLLR S PVPVSGQKRVDIEVLPQELQ 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                         SSALLHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQELQ

Mouse                         SSALLQDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQELQ

Rat                           SSALLHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQEVQ

Caenorhabditis elegans        VPEVMKEIKEIETWILMLLSSPVPVPGKTKVQIEVMPMDLS

Drosophila                    PSIVLHDVREIETWILRLLSTPVPVPGSTRVEVEVLSPTVH
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 1 – 1647 MAP kinase-activating death domain protein
Domain 14 – 268 uDENN



Literature citations
Biallelic MADD variants cause a phenotypic spectrum ranging from developmental delay to a multisystem disorder.
Schneeberger P.E.; Kortuem F.; Korenke G.C.; Alawi M.; Santer R.; Woidy M.; Buhas D.; Fox S.; Juusola J.; Alfadhel M.; Webb B.D.; Coci E.G.; Abou Jamra R.; Siekmeyer M.; Biskup S.; Heller C.; Maier E.M.; Javaher-Haghighi P.; Bedeschi M.F.; Ajmone P.F.; Iascone M.; Peeters H.; Ballon K.; Jaeken J.; Rodriguez Alonso A.; Palomares-Bralo M.; Santos-Simarro F.; Meuwissen M.E.C.; Beysen D.; Kooy R.F.; Houlden H.; Murphy D.; Doosti M.; Karimiani E.G.; Mojarrad M.; Maroofian R.; Noskova L.; Kmoch S.; Honzik T.; Cope H.; Sanchez-Valle A.; Gelb B.D.; Kurth I.; Hempel M.; Kutsche K.;
Brain 143:2437-2453(2020)
Cited for: INVOLVEMENT IN DEEAH; VARIANTS DEEAH 216-ARG--SER-1647 DEL; PHE-257; VAL-305; 327-ARG--SER-1647 DEL; LEU-372; ARG-1040 AND 1431-TRP--SER-1647 DEL; VARIANTS NEDDISH PRO-346; LEU-354; PRO-945; 1213-SER--SER-1647 DEL; SER-1283; ARG-1318 AND 1532-ARG--SER-1647 DEL; CHARACTERIZATION OF VARIANTS DEEAH VAL-305; ARG-1040; FUNCTION;
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.