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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9GZX7: Variant p.Phe15Leu

Single-stranded DNA cytosine deaminase
Gene: AICDA
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Variant information Variant position: help 15 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 Phenylalanine (F) to Leucine (L) at position 15 (F15L, p.Phe15Leu). 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 aromatic (F) to medium size and hydrophobic (L) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 HIGM2. Any additional useful information about the variant.


Sequence information Variant position: help 15 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 198 The length of the canonical sequence.
Location on the sequence: help MDSLLMNRRKFLYQ F KNVRWAKGRRETYLCYVVKR 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                         MDSLLMNRRKFLYQFKNVRWAKGRRETYLCYVVKR

                              MDSLLMKQRKFLYHFKNVRWAKGRHETYLCYVVKR

Mouse                         MDSLLMKQKKFLYHFKNVRWAKGRHETYLCYVVKR

Bovine                        MDSLLKKQRQFLYQFKNVRWAKGRHETYLCYVVKR
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 – 198 Single-stranded DNA cytosine deaminase
Region 2 – 26 Interaction with SUPT6H
Motif 1 – 30 Bipartite nuclear localization signal
Modified residue 27 – 27 Phosphothreonine; by PKA
Mutagenesis 10 – 10 K -> A. Little effect on nuclear import; when associated with A-193. No effect on CTNNBL1 binding.
Mutagenesis 18 – 18 V -> S. Greatly impaired nuclear import; when associated with V-19 and A-193. Reduced interaction with both CTNNBL1 and KPNA1, and abolishes immunoglobulin class switching; when associated with V-19.
Mutagenesis 19 – 19 R -> V. Greatly impaired nuclear import; when associated with S-18 and A-193. Reduced interaction with both CTNNBL1 and KPNA1, and abolishes immunoglobulin class switching; when associated with S-18.
Mutagenesis 20 – 20 W -> K. Impaired nuclear import; when associated with A-193. No effect on CTNNBL1 binding.
Mutagenesis 27 – 27 T -> A. Loss of phosphorylation. No effect on cytidine deaminase activity. Impaired class-switch recombination activity.
Mutagenesis 27 – 27 T -> E. Phosphomimetic mutant which shows loss of cytidine deaminase activity and impaired class-switch recombination activity.
Helix 8 – 15



Literature citations
A novel activation-induced cytidine deaminase (AID) mutation in Brazilian patients with hyper-IgM type 2 syndrome.
Caratao N.; Cortesao C.S.; Reis P.H.; Freitas R.F.; Jacob C.M.; Pastorino A.C.; Carneiro-Sampaio M.; Barreto V.M.;
Clin. Immunol. 148:279-286(2013)
Cited for: VARIANT HIGM2 LEU-15;
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.