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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y6K9: Variant p.His413Tyr

NF-kappa-B essential modulator
Gene: IKBKG
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Variant information Variant position: help 413 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 Histidine (H) to Tyrosine (Y) at position 413 (H413Y, p.His413Tyr). 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 polar (H) to large size and aromatic (Y) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 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 IP. Any additional useful information about the variant.


Sequence information Variant position: help 413 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 PDFCCPKCQYQAPDMDTLQI H VMECIE 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                         PDFCCPKCQYQAPDMDTLQIHVMECIE--

Mouse                         PDFCCPKCQYQAPDMDTLQIHVMECIE

Rat                           PDFCCPKCQYQAPDMDTLQIHVMECIE

Pig                           PNFCCPKCQYQAPDMDTLQIHVMECIE

Bovine                        PKFCCPKCQYQAPDIDTLQIHVMECIE

Drosophila                    TTLRCPICSKSFNALSVLQSHVNDCLD
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
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.
Helix 407 – 416



Literature citations
Insight into IKBKG/NEMO locus: report of new mutations and complex genomic rearrangements leading to incontinentia pigmenti disease.
Conte M.I.; Pescatore A.; Paciolla M.; Esposito E.; Miano M.G.; Lioi M.B.; McAleer M.A.; Giardino G.; Pignata C.; Irvine A.D.; Scheuerle A.E.; Royer G.; Hadj-Rabia S.; Bodemer C.; Bonnefont J.P.; Munnich A.; Smahi A.; Steffann J.; Fusco F.; Ursini M.V.;
Hum. Mutat. 35:165-177(2014)
Cited for: VARIANTS IP PRO-170; GLN-173; PRO-314; PRO-322 AND TYR-413;
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.