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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y2G2: Variant p.Val44Ile

Caspase recruitment domain-containing protein 8
Gene: CARD8
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Variant information Variant position: help 44 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help US 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 Valine (V) to Isoleucine (I) at position 44 (V44I, p.Val44Ile). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. 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 IBD30; uncertain significance. Any additional useful information about the variant.


Sequence information Variant position: help 44 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 537 The length of the canonical sequence.
Location on the sequence: help SSRNIDASKLIRLQGSRKLL V DNSIRELQYTKTGIFFQAEA 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.
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 – 537 Caspase recruitment domain-containing protein 8
Chain 1 – 296 Caspase recruitment domain-containing protein 8, N-terminus
Alternative sequence 1 – 130 MEKKECPEKSSSSEEELPRRDSGSSRNIDASKLIRLQGSRKLLVDNSIRELQYTKTGIFFQAEACVTNDTVYRELPCVSETLCDISHFFQEDDETEAEPLLFRAVPECQLSGGDIPSVSEEQESSEGQDS -> MMRQRQSHYCSVLFLSVNYLGGTFP. In isoform 1 and isoform 2.
Alternative sequence 1 – 116 MEKKECPEKSSSSEEELPRRDSGSSRNIDASKLIRLQGSRKLLVDNSIRELQYTKTGIFFQAEACVTNDTVYRELPCVSETLCDISHFFQEDDETEAEPLLFRAVPECQLSGGDIP -> MGIPTS. In isoform 7.
Alternative sequence 21 – 70 Missing. In isoform 4.
Mutagenesis 51 – 51 L -> A. Does not affect cleavage by HIV-1 protease.
Mutagenesis 52 – 52 Q -> A. Does not affect cleavage by HIV-1 protease.
Mutagenesis 53 – 53 Y -> A. Does not affect cleavage by HIV-1 protease.
Mutagenesis 54 – 54 T -> A. Does not affect cleavage by HIV-1 protease.
Mutagenesis 55 – 55 K -> A. Does not affect cleavage by HIV-1 protease.
Mutagenesis 56 – 56 T -> A. Does not affect cleavage by HIV-1 protease.
Mutagenesis 57 – 57 G -> A. Does not affect cleavage by HIV-1 protease.
Mutagenesis 58 – 58 I -> A. Does not affect cleavage by HIV-1 protease.
Mutagenesis 59 – 59 F -> A. Abolished cleavage by HIV-1 protease, leading to prevent formation of the CARD8 inflammasome and subsequent pyroptosis.
Mutagenesis 60 – 60 F -> A. Abolished cleavage by HIV-1 protease, leading to prevent formation of the CARD8 inflammasome and subsequent pyroptosis.



Literature citations
Loss-of-function CARD8 mutation causes NLRP3 inflammasome activation and Crohn's disease.
Mao L.; Kitani A.; Similuk M.; Oler A.J.; Albenberg L.; Kelsen J.; Aktay A.; Quezado M.; Yao M.; Montgomery-Recht K.; Fuss I.J.; Strober W.;
J. Clin. Invest. 128:1793-1806(2018)
Cited for: VARIANT IBD30 ILE-44;
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.