Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9H257: Variant p.Arg70Trp

Caspase recruitment domain-containing protein 9
Gene: CARD9
Feedback?
Variant information Variant position: help 70 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 Tryptophan (W) at position 70 (R70W, p.Arg70Trp). 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 large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In IMD103; reduced cytokine production in response to C.albicans infection; impaired NF-kappa-B transcriptional activity; reduced production IgG antibodies in response to C.albicans infection. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 70 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 536 The length of the canonical sequence.
Location on the sequence: help SDPNLVIRKRKVGVLLDILQ R TGHKGYVAFLESLELYYPQL 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                         SDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQL

Mouse                         SDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQL

Rat                           SDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQL
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 – 536 Caspase recruitment domain-containing protein 9
Domain 6 – 98 CARD
Binding site 73 – 73
Mutagenesis 58 – 58 K -> D. Abolished homooligomerization and formation of BCL10-nucleating filaments.
Mutagenesis 66 – 66 D -> R. Abolished homooligomerization and formation of BCL10-nucleating filaments.
Mutagenesis 73 – 73 H -> A. Strongly reduced zinc-binding.
Turn 70 – 72



Literature citations
Inherited CARD9 deficiency in otherwise healthy children and adults with Candida species-induced meningoencephalitis, colitis, or both.
Lanternier F.; Mahdaviani S.A.; Barbati E.; Chaussade H.; Koumar Y.; Levy R.; Denis B.; Brunel A.S.; Martin S.; Loop M.; Peeters J.; de Selys A.; Vanclaire J.; Vermylen C.; Nassogne M.C.; Chatzis O.; Liu L.; Migaud M.; Pedergnana V.; Desoubeaux G.; Jouvion G.; Chretien F.; Darazam I.A.; Schaeffer A.A.; Netea M.G.; De Bruycker J.J.; Bernard L.; Reynes J.; Amazrine N.; Abel L.; Van der Linden D.; Harrison T.; Picard C.; Lortholary O.; Mansouri D.; Casanova J.L.; Puel A.;
J. Allergy Clin. Immunol. 135:1558-1568(2015)
Cited for: VARIANTS IMD103 GLN-35; TRP-70; 289-GLN--SER-536 DEL AND 295-GLN--SER-536 DEL; CHARACTERIZATION OF VARIANTS IMD103 GLN-35; TRP-70 AND 295-GLN--SER-536 DEL; FUNCTION; Chronic and invasive fungal infections in a family with CARD9 deficiency.
Alves de Medeiros A.K.; Lodewick E.; Bogaert D.J.; Haerynck F.; Van Daele S.; Lambrecht B.; Bosma S.; Vanderdonckt L.; Lortholary O.; Migaud M.; Casanova J.L.; Puel A.; Lanternier F.; Lambert J.; Brochez L.; Dullaers M.;
J. Clin. Immunol. 36:204-209(2016)
Cited for: VARIANT IMD103 TRP-70; CHARACTERIZATION OF VARIANT IMD103 TRP-70; FUNCTION; Human gut mycobiota tune immunity via CARD9-dependent induction of anti-fungal IgG antibodies.
Doron I.; Leonardi I.; Li X.V.; Fiers W.D.; Semon A.; Bialt-DeCelie M.; Migaud M.; Gao I.H.; Lin W.Y.; Kusakabe T.; Puel A.; Iliev I.D.;
Cell 0:0-0(2021)
Cited for: CHARACTERIZATION OF VARIANTS IMD103 GLN-35; TRP-70 AND 289-GLN--SER-536 DEL; FUNCTION; TISSUE SPECIFICITY; Inherited CARD9 deficiency in a child with invasive disease due to Exophiala dermatitidis and two older but asymptomatic siblings.
Imanaka Y.; Taniguchi M.; Doi T.; Tsumura M.; Nagaoka R.; Shimomura M.; Asano T.; Kagawa R.; Mizoguchi Y.; Karakawa S.; Arihiro K.; Imai K.; Morio T.; Casanova J.L.; Puel A.; Ohara O.; Kamei K.; Kobayashi M.; Okada S.;
J. Clin. Immunol. 41:975-986(2021)
Cited for: VARIANTS IMD103 GLU-196 AND PRO-373; CHARACTERIZATION OF VARIANTS IMD103 TRP-70; GLU-196 AND PRO-373; 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.