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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y6K9: Variant p.Ala288Gly

NF-kappa-B essential modulator
Gene: IKBKG
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Variant information Variant position: help 288 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 Alanine (A) to Glycine (G) at position 288 (A288G, p.Ala288Gly). 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 small size and hydrophobic (A) to glycine (G) 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 EDAID1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 288 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 QQAEEALVAKQEVIDKLKEE A EQHKIVMETVPVLKAQADIY 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                         QQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIY

Mouse                         QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIY

Rat                           QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIY

Pig                           QQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIY

Bovine                        QQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIY

Drosophila                    -------------INELKARDIQKQ---EVIKGLQIQNDIY
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
Region 242 – 350 Ubiquitin-binding (UBAN)
Region 246 – 365 Self-association
Region 251 – 419 Required for interaction with TNFAIP3
Coiled coil 49 – 356
Cross 277 – 277 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross 277 – 277 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross 283 – 283 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross 285 – 285 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross 292 – 292 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross 302 – 302 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence 257 – 304 Missing. In isoform 3.
Mutagenesis 277 – 277 K -> A. Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-309.
Mutagenesis 285 – 285 K -> R. Decreased ability to activate NF-kappa-B. Important decrease in the ubiquitination level; when associated with R-399.
Mutagenesis 296 – 296 E -> A. No effet on oligomerization,impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation.
Mutagenesis 300 – 300 V -> D. Greatly impairs tandem ubiquitin binding.
Mutagenesis 301 – 301 L -> A. Impairs tandem ubiquitin binding.
Mutagenesis 302 – 302 K -> R. No effect on MARCH2F-mediated K48-linked ubiquitination.
Mutagenesis 304 – 304 Q -> A. Complete loss of cleavage by HAV protease 3c.
Mutagenesis 304 – 304 Q -> A. Impairs tandem ubiquitin binding.
Mutagenesis 307 – 307 I -> N. Greatly impairs tandem ubiquitin binding.
Mutagenesis 308 – 308 Y -> A. Greatly impairs tandem ubiquitin binding.
Helix 271 – 295



Literature citations
X-linked anhidrotic ectodermal dysplasia with immunodeficiency is caused by impaired NF-kappa B signaling.
Doeffinger R.; Smahi A.; Bessia C.; Geissmann F.; Feinberg J.; Durandy A.; Bodemer C.; Kenwrick S.J.; Dupuis-Girod S.; Blanche S.; Wood P.; Rabia S.H.; Headon D.J.; Overbeek P.A.; Le Deist F.; Holland S.M.; Belani K.; Kumararatne D.S.; Fischer A.; Shapiro R.; Conley M.E.; Reimund E.; Kalhoff H.; Abinun M.; Munnich A.; Israael A.; Courtois G.; Casanova J.-L.;
Nat. Genet. 27:277-285(2001)
Cited for: INVOLVEMENT IN EDAID1; VARIANTS EDAID1 PRO-175; PRO-227; GLY-288; ASN-311; ARG-417 AND PHE-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.