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UniProtKB/Swiss-Prot Q9H257: Variant p.Arg101Cys

Caspase recruitment domain-containing protein 9
Gene: CARD9
Variant information

Variant position:  101
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 Arginine (R) to Cysteine (C) at position 101 (R101C, p.Arg101Cys).
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 large size and basic (R) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
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 CANDF2.
Any additional useful information about the variant.

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



Sequence information

Variant position:  101
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  536
The length of the canonical sequence.

Location on the sequence:   ESLELYYPQLYKKVTGKEPA  R VFSMIIDASGESGLTQLLMT
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                         ESLELYYPQLYKKVTGKEPARVFSMIIDASGESGLTQLLMT

Mouse                         ESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMT

Rat                           ESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMT

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 – 536 Caspase recruitment domain-containing protein 9
Region 99 – 116 Linker
Mutagenesis 101 – 101 R -> Q. Disruption of the linker region, relieving autoinhibition and leading to activation of NF-kappa-B.
Mutagenesis 103 – 103 F -> L. Disruption of the linker region, relieving autoinhibition and leading to activation of NF-kappa-B.
Mutagenesis 107 – 107 I -> E. Disruption of the linker region, relieving autoinhibition and leading to activation of NF-kappa-B. Constitutively forms BCL10-nucleating filaments.
Mutagenesis 111 – 111 G -> S. Disruption of the linker region, relieving autoinhibition and leading to activation of NF-kappa-B.
Mutagenesis 114 – 114 G -> D. Disruption of the linker region, relieving autoinhibition and leading to activation of NF-kappa-B.
Mutagenesis 115 – 115 L -> I. Disruption of the linker region, relieving autoinhibition and leading to activation of NF-kappa-B. Constitutively forms BCL10-nucleating filaments.


Literature citations

Deep dermatophytosis and inherited CARD9 deficiency.
Lanternier F.; Pathan S.; Vincent Q.B.; Liu L.; Cypowyj S.; Prando C.; Migaud M.; Taibi L.; Ammar-Khodja A.; Boudghene Stambouli O.; Guellil B.; Jacobs F.; Goffard J.C.; Schepers K.; del Marmol V.; Boussofara L.; Denguezli M.; Larif M.; Bachelez H.; Michel L.; Lefranc G.; Hay R.; Jouvion G.; Chretien F.; Fraitag S.; Bougnoux M.E.; Boudia M.; Abel L.; Lortholary O.; Casanova J.L.; Picard C.; Grimbacher B.; Puel A.;
N. Engl. J. Med. 369:1704-1714(2013)
Cited for: VARIANTS CANDF2 CYS-101 AND 289-GLN--SER-536 DEL;

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.