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UniProtKB/Swiss-Prot Q9NWZ3: Variant p.Gly298Asp

Interleukin-1 receptor-associated kinase 4
Gene: IRAK4
Variant information

Variant position:  298
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glycine (G) to Aspartate (D) at position 298 (G298D, p.Gly298Asp).
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:  Change from glycine (G) to medium size and acidic (D)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
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:  In IMD67; decreases inhibition of NF-kappa-B complex activation; impairs neutrophil migration and phagocytosis.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  298
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  460
The length of the canonical sequence.

Location on the sequence:   DGTPPLSWHMRCKIAQGAAN  G INFLHENHHIHRDIKSANIL
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         DGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANIL

Mouse                         DGTPPLSWHTRCKVAQGTANGIRFLHENHHIHRDIKSANIL

Bovine                        DGTPPLSWNMRCKIAQGAANGLSYLHENHHIHRDIKSANIL

Sequence annotation in neighborhood:  
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 – 460 Interleukin-1 receptor-associated kinase 4
Domain 186 – 454 Protein kinase
Active site 311 – 311 Proton acceptor
Helix 285 – 304


Literature citations

Impaired neutrophil migration and phagocytosis in IRAK-4 deficiency.
Bouma G.; Doffinger R.; Patel S.Y.; Peskett E.; Sinclair J.C.; Barcenas-Morales G.; Cerron-Gutierrez L.; Kumararatne D.S.; Davies E.G.; Thrasher A.J.; Burns S.O.;
Br. J. Haematol. 147:153-156(2009)
Cited for: VARIANT IMD67 ASP-298; CHARACTERIZATION OF VARIANT IMD67 ASP-298;

Clinical features and outcome of patients with IRAK-4 and MyD88 deficiency.
Picard C.; von Bernuth H.; Ghandil P.; Chrabieh M.; Levy O.; Arkwright P.D.; McDonald D.; Geha R.S.; Takada H.; Krause J.C.; Creech C.B.; Ku C.L.; Ehl S.; Marodi L.; Al-Muhsen S.; Al-Hajjar S.; Al-Ghonaium A.; Day-Good N.K.; Holland S.M.; Gallin J.I.; Chapel H.; Speert D.P.; Rodriguez-Gallego C.; Colino E.; Garty B.Z.; Roifman C.; Hara T.; Yoshikawa H.; Nonoyama S.; Domachowske J.; Issekutz A.C.; Tang M.; Smart J.; Zitnik S.E.; Hoarau C.; Kumararatne D.S.; Thrasher A.J.; Davies E.G.; Bethune C.; Sirvent N.; de Ricaud D.; Camcioglu Y.; Vasconcelos J.; Guedes M.; Vitor A.B.; Rodrigo C.; Almazan F.; Mendez M.; Arostegui J.I.; Alsina L.; Fortuny C.; Reichenbach J.; Verbsky J.W.; Bossuyt X.; Doffinger R.; Abel L.; Puel A.; Casanova J.L.;
Medicine (Baltimore) 89:403-425(2010)
Cited for: INVOLVEMENT IN IMD67; VARIANT IMD67 ASP-298;

Functional assessment of the mutational effects of human IRAK4 and MyD88 genes.
Yamamoto T.; Tsutsumi N.; Tochio H.; Ohnishi H.; Kubota K.; Kato Z.; Shirakawa M.; Kondo N.;
Mol. Immunol. 58:66-76(2014)
Cited for: CHARACTERIZATION OF VARIANTS VAL-5; TRP-20; THR-26; VAL-39 AND ARG-98; CHARACTERIZATION OF VARIANTS IMD67 CYS-12 AND ASP-298; FUNCTION; INTERACTION WITH MYD88;

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.