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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y6K9: Variant p.Asp406Val

NF-kappa-B essential modulator
Gene: IKBKG
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Variant information Variant position: help 406 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 Aspartate (D) to Valine (V) at position 406 (D406V, p.Asp406Val). 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 medium size and acidic (D) to medium size and hydrophobic (V) 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 EDAID1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 406 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 419 The length of the canonical sequence.
Location on the sequence: help RSPPEEPPDFCCPKCQYQAP D MDTLQIHVMECIE 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                         RSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE--

Mouse                         RSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE

Rat                           RSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE

Pig                           RSPPEEPPNFCCPKCQYQAPDMDTLQIHVMECIE

Bovine                        RSPPDEPPKFCCPKCQYQAPDIDTLQIHVMECIE

Drosophila                    -SSRTSDTTLRCPICSKSFNALSVLQSHVNDCLD
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 – 419 NF-kappa-B essential modulator
Zinc finger 389 – 419 CCHC NOA-type
Region 251 – 419 Required for interaction with TNFAIP3
Region 382 – 419 Interaction with CYLD
Binding site 397 – 397
Binding site 400 – 400
Binding site 413 – 413
Binding site 417 – 417
Modified residue 387 – 387 Phosphoserine
Cross 399 – 399 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Mutagenesis 399 – 399 K -> R. Abolishes BCL10-mediated but not RIPK2-mediated ubiquitination. Important decrease in the ubiquitination level; when associated with R-285. No change in the ubiquitination level; when associated with R-115 or R-224.
Mutagenesis 414 – 414 V -> S. Abolishes binding to polyubiquitin.
Mutagenesis 415 – 415 M -> S. Impairs binding to polyubiquitin.
Beta strand 403 – 406



Literature citations
Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia.
Jain A.; Ma C.A.; Liu S.; Brown M.; Cohen J.; Strober W.;
Nat. Immunol. 2:223-228(2001)
Cited for: VARIANTS EDAID1 VAL-406 AND ARG-417;
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.