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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9H257: Variant p.Arg35Gln

Caspase recruitment domain-containing protein 9
Gene: CARD9
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Variant information Variant position: help 35 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 35 (R35Q, p.Arg35Gln). 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 IMD103; abolished homooligomerization and formation of BCL10-nucleating filaments; reduced cytokine production in response to C.albicans infection; 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 35 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 EGFRVTLTSVIDPSRITPYL R QCKVLNPDDEEQVLSDPNLV 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                         EGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLV

Mouse                         ESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLV

Rat                           ESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLV
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
Mutagenesis 15 – 15 E -> R. Abolished homooligomerization and formation of BCL10-nucleating filaments.
Mutagenesis 35 – 35 R -> E. Abolished homooligomerization and formation of BCL10-nucleating filaments.
Mutagenesis 37 – 37 C -> A. Does not affect zinc-binbing.
Mutagenesis 43 – 43 D -> R. Abolished homooligomerization and formation of BCL10-nucleating filaments.
Helix 31 – 36



Literature citations
Structures of autoinhibited and polymerized forms of CARD9 reveal mechanisms of CARD9 and CARD11 activation.
Holliday M.J.; Witt A.; Rodriguez Gama A.; Walters B.T.; Arthur C.P.; Halfmann R.; Rohou A.; Dueber E.C.; Fairbrother W.J.;
Nat. Commun. 10:3070-3070(2019)
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) OF 2-152 IN COMPLEX WITH ZINC; FUNCTION; ACTIVITY REGULATION; INTERACTION WITH BCL10; UBIQUITINATION AT LYS-125; SUBUNIT; DOMAIN; MUTAGENESIS OF GLU-15; ARG-35; ASP-43; LYS-58; ASP-66; ARG-101; PHE-103; ILE-107; GLY-111; GLY-114 AND LEU-115; CHARACTERIZATION OF VARIANT IMD103 GLN-35; 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; 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;
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.