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Protein

Interleukin-1 receptor-associated kinase 4

Gene

IRAK4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways (PubMed:17878374). Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Kineticsi

  1. KM=650 µM for ATP (at pH 7.5)1 Publication
  2. KM=1100 µM for substrate (at pH 7.5)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei213 – 2131ATP
    Active sitei311 – 3111Proton acceptorPROSITE-ProRule annotation
    Binding sitei329 – 3291ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi192 – 2009ATPPROSITE-ProRule annotation
    Nucleotide bindingi313 – 3164ATP

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_22442. Interleukin-1 signaling.
    REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25222. MyD88 dependent cascade initiated on endosome.
    REACT_27215. MyD88 cascade initiated on plasma membrane.
    REACT_355210. MyD88 deficiency (TLR2/4).
    REACT_355363. MyD88 deficiency (TLR5).
    REACT_355387. IRAK4 deficiency (TLR5).
    REACT_355462. IRAK4 deficiency (TLR2/4).
    REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
    SignaLinkiQ9NWZ3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-1 receptor-associated kinase 4 (EC:2.7.11.1)
    Short name:
    IRAK-4
    Alternative name(s):
    Renal carcinoma antigen NY-REN-64
    Gene namesi
    Name:IRAK4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:17967. IRAK4.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Recurrent isolated invasive pneumococcal disease 1 (IPD1)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionRecurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.

    See also OMIM:610799
    IRAK4 deficiency (IRAK4D)6 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionCauses extracellular pyogenic bacterial and fungal infections in otherwise healthy children.

    See also OMIM:607676
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121R → C in IRAK4D; no effect on inhibition of NF-kappa-B complex activation; loss of interaction with MYD88; decreases protein stability. 2 Publications
    VAR_072888
    Natural varianti298 – 2981G → D in IRAK4D; decreases inhibition of NF-kappa-B complex activation; impairs neutrophil migration and phagocytosis. 3 Publications
    VAR_072892
    Natural varianti391 – 3911R → H Found in a patient with IRAK4D in association with C-12; probable neutral polymorphism. 2 Publications
    Corresponds to variant rs55944915 [ dbSNP | Ensembl ].
    VAR_040590

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131K → A: Loss of kinase activity. 1 Publication

    Organism-specific databases

    MIMi607676. phenotype.
    610799. phenotype.
    Orphaneti70592. Immunodeficiency due to interleukin-1 receptor-associated kinase-4 deficiency.
    PharmGKBiPA134914577.

    Polymorphism and mutation databases

    BioMutaiIRAK4.
    DMDMi50401181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 460460Interleukin-1 receptor-associated kinase 4PRO_0000086035Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei34 – 341N6-acetyllysine1 Publication
    Modified residuei342 – 3421Phosphothreonine2 Publications
    Modified residuei345 – 3451Phosphothreonine3 Publications
    Modified residuei346 – 3461Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NWZ3.
    PaxDbiQ9NWZ3.
    PRIDEiQ9NWZ3.

    Expressioni

    Gene expression databases

    BgeeiQ9NWZ3.
    CleanExiHS_IRAK4.
    ExpressionAtlasiQ9NWZ3. baseline and differential.
    GenevisibleiQ9NWZ3. HS.

    Organism-specific databases

    HPAiCAB016685.
    CAB022077.
    HPA000924.

    Interactioni

    Subunit structurei

    Associates with MYD88 and IRAK2 to form a ternary complex called the Myddosome. Once phosphorylated, IRAK4 dissociates from the receptor complex and then associates with the TNF receptor-associated factor 6 (TRAF6), IRAK1, and PELI1; this intermediate complex is required for subsequent NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression. Interacts with IL1RL1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Irak3Q8K4B24EBI-448378,EBI-646179From a different organism.
    PELI2Q9HAT83EBI-448378,EBI-448407
    TIRAPP587532EBI-448378,EBI-528644

    Protein-protein interaction databases

    BioGridi119322. 26 interactions.
    DIPiDIP-31351N.
    IntActiQ9NWZ3. 11 interactions.
    MINTiMINT-1383671.
    STRINGi9606.ENSP00000390651.

    Structurei

    Secondary structure

    1
    460
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 133Combined sources
    Helixi16 – 2611Combined sources
    Helixi31 – 388Combined sources
    Beta strandi42 – 487Combined sources
    Helixi50 – 578Combined sources
    Helixi58 – 603Combined sources
    Turni61 – 633Combined sources
    Helixi66 – 738Combined sources
    Turni74 – 774Combined sources
    Helixi81 – 899Combined sources
    Turni90 – 923Combined sources
    Helixi94 – 1007Combined sources
    Beta strandi102 – 1043Combined sources
    Beta strandi166 – 1683Combined sources
    Helixi170 – 1767Combined sources
    Turni177 – 1804Combined sources
    Turni185 – 1884Combined sources
    Beta strandi191 – 1944Combined sources
    Beta strandi196 – 20712Combined sources
    Beta strandi209 – 2157Combined sources
    Turni223 – 2253Combined sources
    Helixi226 – 23914Combined sources
    Beta strandi248 – 2525Combined sources
    Beta strandi254 – 2574Combined sources
    Beta strandi259 – 2635Combined sources
    Helixi270 – 2756Combined sources
    Helixi277 – 2793Combined sources
    Helixi285 – 30420Combined sources
    Helixi314 – 3163Combined sources
    Beta strandi317 – 3193Combined sources
    Beta strandi325 – 3273Combined sources
    Beta strandi349 – 3513Combined sources
    Helixi352 – 3543Combined sources
    Helixi357 – 3604Combined sources
    Helixi367 – 38216Combined sources
    Beta strandi391 – 3955Combined sources
    Helixi398 – 4047Combined sources
    Helixi410 – 4134Combined sources
    Helixi423 – 43614Combined sources
    Turni441 – 4433Combined sources
    Helixi447 – 45711Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NRUX-ray2.00A/B/C/D154-460[»]
    2NRYX-ray2.15A/B/C/D154-460[»]
    2O8YX-ray2.40A/B163-460[»]
    2OIBX-ray2.00A/B/C/D160-460[»]
    2OICX-ray2.40A/B/C/D160-460[»]
    2OIDX-ray2.30A/B/C/D160-460[»]
    3MOPX-ray3.40G/H/I/J4-106[»]
    4U97X-ray2.65A/B154-460[»]
    4U9AX-ray2.80A/B154-460[»]
    4XS2X-ray2.73A/B/C/D160-460[»]
    ProteinModelPortaliQ9NWZ3.
    SMRiQ9NWZ3. Positions 4-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NWZ3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 10485DeathAdd
    BLAST
    Domaini186 – 454269Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 death domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000063073.
    HOGENOMiHOG000116550.
    HOVERGENiHBG066836.
    InParanoidiQ9NWZ3.
    KOiK04733.
    OMAiFCDKDRT.
    OrthoDBiEOG7MD4Q1.
    PhylomeDBiQ9NWZ3.
    TreeFamiTF351380.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR011029. DEATH-like_dom.
    IPR017428. IL-1_rcpt-assoc_kin4.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038189. IRAK4. 1 hit.
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9NWZ3-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MNKPITPSTY VRCLNVGLIR KLSDFIDPQE GWKKLAVAIK KPSGDDRYNQ
    60 70 80 90 100
    FHIRRFEALL QTGKSPTSEL LFDWGTTNCT VGDLVDLLIQ NEFFAPASLL
    110 120 130 140 150
    LPDAVPKTAN TLPSKEAITV QQKQMPFCDK DRTLMTPVQN LEQSYMPPDS
    160 170 180 190 200
    SSPENKSLEV SDTRFHSFSF YELKNVTNNF DERPISVGGN KMGEGGFGVV
    210 220 230 240 250
    YKGYVNNTTV AVKKLAAMVD ITTEELKQQF DQEIKVMAKC QHENLVELLG
    260 270 280 290 300
    FSSDGDDLCL VYVYMPNGSL LDRLSCLDGT PPLSWHMRCK IAQGAANGIN
    310 320 330 340 350
    FLHENHHIHR DIKSANILLD EAFTAKISDF GLARASEKFA QTVMTSRIVG
    360 370 380 390 400
    TTAYMAPEAL RGEITPKSDI YSFGVVLLEI ITGLPAVDEH REPQLLLDIK
    410 420 430 440 450
    EEIEDEEKTI EDYIDKKMND ADSTSVEAMY SVASQCLHEK KNKRPDIKKV
    460
    QQLLQEMTAS
    Length:460
    Mass (Da):51,530
    Last modified:October 1, 2000 - v1
    Checksum:i6C8156ADF25FF81E
    GO
    Isoform 2 (identifier: Q9NWZ3-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-124: Missing.

    Show »
    Length:336
    Mass (Da):37,674
    Checksum:i6608D68A2EE4138C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 811V → A in AAM15772 (PubMed:11960013).Curated
    Sequence conflicti432 – 4321V → G in AAD42884 (PubMed:10508479).Curated
    Sequence conflicti437 – 4371L → R in AAD42884 (PubMed:10508479).Curated
    Sequence conflicti444 – 4441R → S in AAD42884 (PubMed:10508479).Curated
    Sequence conflicti451 – 4511Q → H in AAD42884 (PubMed:10508479).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51I → V Polymorphism; no effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88. 2 Publications
    Corresponds to variant rs56312115 [ dbSNP | Ensembl ].
    VAR_040588
    Natural varianti12 – 121R → C in IRAK4D; no effect on inhibition of NF-kappa-B complex activation; loss of interaction with MYD88; decreases protein stability. 2 Publications
    VAR_072888
    Natural varianti20 – 201R → W Polymorphism; increases inhibition of NF-kappa-B complex activation; decreases interaction with MYD88; decreases protein stability. 1 Publication
    VAR_072889
    Natural varianti26 – 261I → T Polymorphism; no effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88. 1 Publication
    VAR_072890
    Natural varianti39 – 391I → V Polymorphism; no effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88. 1 Publication
    VAR_072891
    Natural varianti98 – 981S → R Polymorphism; no effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88. 2 Publications
    Corresponds to variant rs4251469 [ dbSNP | Ensembl ].
    VAR_019354
    Natural varianti298 – 2981G → D in IRAK4D; decreases inhibition of NF-kappa-B complex activation; impairs neutrophil migration and phagocytosis. 3 Publications
    VAR_072892
    Natural varianti355 – 3551M → V.1 Publication
    VAR_040589
    Natural varianti390 – 3901H → R.1 Publication
    Corresponds to variant rs4251583 [ dbSNP | Ensembl ].
    VAR_019355
    Natural varianti391 – 3911R → H Found in a patient with IRAK4D in association with C-12; probable neutral polymorphism. 2 Publications
    Corresponds to variant rs55944915 [ dbSNP | Ensembl ].
    VAR_040590
    Natural varianti428 – 4281A → T.2 Publications
    Corresponds to variant rs4251545 [ dbSNP | Ensembl ].
    VAR_019356

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 124124Missing in isoform 2. 2 PublicationsVSP_041556Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF445802 mRNA. Translation: AAM15772.1.
    AF155118 mRNA. Translation: AAD42884.1.
    AY340964 mRNA. Translation: AAR02360.1.
    AY340965 mRNA. Translation: AAR02361.1.
    AY340966 mRNA. Translation: AAR02362.1.
    AY340967 mRNA. Translation: AAR02363.1.
    AK000528 mRNA. Translation: BAA91232.1.
    AK299944 mRNA. Translation: BAG61774.1.
    AY186092 Genomic DNA. Translation: AAN75440.1.
    AC093012 Genomic DNA. No translation available.
    BC013316 mRNA. Translation: AAH13316.1.
    CCDSiCCDS44862.1. [Q9NWZ3-2]
    CCDS8744.1. [Q9NWZ3-1]
    RefSeqiNP_001107654.1. NM_001114182.2. [Q9NWZ3-1]
    NP_001138728.1. NM_001145256.1. [Q9NWZ3-2]
    NP_001138729.1. NM_001145257.1. [Q9NWZ3-2]
    NP_001138730.1. NM_001145258.1. [Q9NWZ3-2]
    NP_057207.2. NM_016123.3. [Q9NWZ3-1]
    XP_005269000.1. XM_005268943.3. [Q9NWZ3-1]
    XP_005269001.1. XM_005268944.3. [Q9NWZ3-1]
    XP_005269002.1. XM_005268945.3. [Q9NWZ3-1]
    XP_005269003.1. XM_005268946.3. [Q9NWZ3-1]
    XP_005269004.1. XM_005268947.3. [Q9NWZ3-2]
    XP_005269005.1. XM_005268948.2. [Q9NWZ3-2]
    XP_005269006.1. XM_005268949.2. [Q9NWZ3-2]
    XP_006719501.1. XM_006719438.2. [Q9NWZ3-1]
    XP_006719502.1. XM_006719439.2. [Q9NWZ3-2]
    UniGeneiHs.138499.

    Genome annotation databases

    EnsembliENST00000431837; ENSP00000390327; ENSG00000198001. [Q9NWZ3-2]
    ENST00000440781; ENSP00000408734; ENSG00000198001. [Q9NWZ3-2]
    ENST00000551736; ENSP00000446490; ENSG00000198001. [Q9NWZ3-1]
    ENST00000613694; ENSP00000479889; ENSG00000198001. [Q9NWZ3-1]
    GeneIDi51135.
    KEGGihsa:51135.
    UCSCiuc001rnt.3. human. [Q9NWZ3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    IRAK4base

    IRAK4 mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF445802 mRNA. Translation: AAM15772.1.
    AF155118 mRNA. Translation: AAD42884.1.
    AY340964 mRNA. Translation: AAR02360.1.
    AY340965 mRNA. Translation: AAR02361.1.
    AY340966 mRNA. Translation: AAR02362.1.
    AY340967 mRNA. Translation: AAR02363.1.
    AK000528 mRNA. Translation: BAA91232.1.
    AK299944 mRNA. Translation: BAG61774.1.
    AY186092 Genomic DNA. Translation: AAN75440.1.
    AC093012 Genomic DNA. No translation available.
    BC013316 mRNA. Translation: AAH13316.1.
    CCDSiCCDS44862.1. [Q9NWZ3-2]
    CCDS8744.1. [Q9NWZ3-1]
    RefSeqiNP_001107654.1. NM_001114182.2. [Q9NWZ3-1]
    NP_001138728.1. NM_001145256.1. [Q9NWZ3-2]
    NP_001138729.1. NM_001145257.1. [Q9NWZ3-2]
    NP_001138730.1. NM_001145258.1. [Q9NWZ3-2]
    NP_057207.2. NM_016123.3. [Q9NWZ3-1]
    XP_005269000.1. XM_005268943.3. [Q9NWZ3-1]
    XP_005269001.1. XM_005268944.3. [Q9NWZ3-1]
    XP_005269002.1. XM_005268945.3. [Q9NWZ3-1]
    XP_005269003.1. XM_005268946.3. [Q9NWZ3-1]
    XP_005269004.1. XM_005268947.3. [Q9NWZ3-2]
    XP_005269005.1. XM_005268948.2. [Q9NWZ3-2]
    XP_005269006.1. XM_005268949.2. [Q9NWZ3-2]
    XP_006719501.1. XM_006719438.2. [Q9NWZ3-1]
    XP_006719502.1. XM_006719439.2. [Q9NWZ3-2]
    UniGeneiHs.138499.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NRUX-ray2.00A/B/C/D154-460[»]
    2NRYX-ray2.15A/B/C/D154-460[»]
    2O8YX-ray2.40A/B163-460[»]
    2OIBX-ray2.00A/B/C/D160-460[»]
    2OICX-ray2.40A/B/C/D160-460[»]
    2OIDX-ray2.30A/B/C/D160-460[»]
    3MOPX-ray3.40G/H/I/J4-106[»]
    4U97X-ray2.65A/B154-460[»]
    4U9AX-ray2.80A/B154-460[»]
    4XS2X-ray2.73A/B/C/D160-460[»]
    ProteinModelPortaliQ9NWZ3.
    SMRiQ9NWZ3. Positions 4-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119322. 26 interactions.
    DIPiDIP-31351N.
    IntActiQ9NWZ3. 11 interactions.
    MINTiMINT-1383671.
    STRINGi9606.ENSP00000390651.

    Chemistry

    BindingDBiQ9NWZ3.
    ChEMBLiCHEMBL3778.
    GuidetoPHARMACOLOGYi2045.

    Polymorphism and mutation databases

    BioMutaiIRAK4.
    DMDMi50401181.

    Proteomic databases

    MaxQBiQ9NWZ3.
    PaxDbiQ9NWZ3.
    PRIDEiQ9NWZ3.

    Protocols and materials databases

    DNASUi51135.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000431837; ENSP00000390327; ENSG00000198001. [Q9NWZ3-2]
    ENST00000440781; ENSP00000408734; ENSG00000198001. [Q9NWZ3-2]
    ENST00000551736; ENSP00000446490; ENSG00000198001. [Q9NWZ3-1]
    ENST00000613694; ENSP00000479889; ENSG00000198001. [Q9NWZ3-1]
    GeneIDi51135.
    KEGGihsa:51135.
    UCSCiuc001rnt.3. human. [Q9NWZ3-1]

    Organism-specific databases

    CTDi51135.
    GeneCardsiGC12P044152.
    HGNCiHGNC:17967. IRAK4.
    HPAiCAB016685.
    CAB022077.
    HPA000924.
    MIMi606883. gene.
    607676. phenotype.
    610799. phenotype.
    neXtProtiNX_Q9NWZ3.
    Orphaneti70592. Immunodeficiency due to interleukin-1 receptor-associated kinase-4 deficiency.
    PharmGKBiPA134914577.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000063073.
    HOGENOMiHOG000116550.
    HOVERGENiHBG066836.
    InParanoidiQ9NWZ3.
    KOiK04733.
    OMAiFCDKDRT.
    OrthoDBiEOG7MD4Q1.
    PhylomeDBiQ9NWZ3.
    TreeFamiTF351380.

    Enzyme and pathway databases

    ReactomeiREACT_22442. Interleukin-1 signaling.
    REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25222. MyD88 dependent cascade initiated on endosome.
    REACT_27215. MyD88 cascade initiated on plasma membrane.
    REACT_355210. MyD88 deficiency (TLR2/4).
    REACT_355363. MyD88 deficiency (TLR5).
    REACT_355387. IRAK4 deficiency (TLR5).
    REACT_355462. IRAK4 deficiency (TLR2/4).
    REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
    SignaLinkiQ9NWZ3.

    Miscellaneous databases

    ChiTaRSiIRAK4. human.
    EvolutionaryTraceiQ9NWZ3.
    GenomeRNAii51135.
    NextBioi53983.
    PROiQ9NWZ3.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NWZ3.
    CleanExiHS_IRAK4.
    ExpressionAtlasiQ9NWZ3. baseline and differential.
    GenevisibleiQ9NWZ3. HS.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR011029. DEATH-like_dom.
    IPR017428. IL-1_rcpt-assoc_kin4.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038189. IRAK4. 1 hit.
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "IRAK4: a novel member of the IRAK family with the properties of an IRAK-kinase."
      Li S., Strelow A., Fontana E.J., Wesche H.
      Proc. Natl. Acad. Sci. U.S.A. 99:5567-5572(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH IRAK1 AND TRAF6.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    3. "Human interleukin-1 receptor associated kinase 4 cDNA sequences."
      Chuang T.H., Ulevitch R.J.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Spleen.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    5. SeattleSNPs variation discovery resource
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-98; ARG-390 AND THR-428.
    6. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    8. "Pellino 1 is required for interleukin-1 (IL-1)-mediated signaling through its interaction with the IL-1 receptor-associated kinase 4 (IRAK4)-IRAK-tumor necrosis factor receptor-associated factor 6 (TRAF6) complex."
      Jiang Z., Johnson H.J., Nie H., Qin J., Bird T.A., Li X.
      J. Biol. Chem. 278:10952-10956(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRAK1; PELI1 AND TRAF6.
    9. "Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4."
      Burns K., Janssens S., Brissoni B., Olivos N., Beyaert R., Tschopp J.
      J. Exp. Med. 197:263-268(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF IRAK1.
    10. "Distinct mutations in IRAK-4 confer hyporesponsiveness to lipopolysaccharide and interleukin-1 in a patient with recurrent bacterial infections."
      Medvedev A.E., Lentschat A., Kuhns D.B., Blanco J.C.G., Salkowski C., Zhang S., Arditi M., Gallin J.I., Vogel S.N.
      J. Exp. Med. 198:521-531(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN IRAK4D.
    11. "IRAK4 kinase activity is redundant for interleukin-1 (IL-1) receptor-associated kinase phosphorylation and IL-1 responsiveness."
      Qin J., Jiang Z., Qian Y., Casanova J.-L., Li X.
      J. Biol. Chem. 279:26748-26753(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-213.
    12. Cited for: INVOLVEMENT IN IRAK4D.
    13. "IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST 2 and induces T helper type 2-associated cytokines."
      Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K., Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F., Kastelein R.A.
      Immunity 23:479-490(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IL1RL1.
    14. "Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor signaling through direct interaction with the adaptor Pellino-1."
      Choi K.C., Lee Y.S., Lim S., Choi H.K., Lee C.H., Lee E.K., Hong S., Kim I.H., Kim S.J., Park S.H.
      Nat. Immunol. 7:1057-1065(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH IRAK1; MYD88; PELI1 AND TRAF6.
    15. Cited for: FUNCTION IN PHOSPHORYLATION OF NCF1.
    16. "IRAK-4 kinase activity is required for interleukin-1 (IL-1) receptor- and toll-like receptor 7-mediated signaling and gene expression."
      Koziczak-Holbro M., Joyce C., Gluck A., Kinzel B., Muller M., Tschopp C., Mathison J.C., Davis C.N., Gram H.
      J. Biol. Chem. 282:13552-13560(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TLR7 SIGNALING PATHWAY.
    17. "IRAK4 and NEMO mutations in otherwise healthy children with recurrent invasive pneumococcal disease."
      Ku C.-L., Picard C., Erdos M., Jeurissen A., Bustamante J., Puel A., von Bernuth H., Filipe-Santos O., Chang H.-H., Lawrence T., Raes M., Marodi L., Bossuyt X., Casanova J.-L.
      J. Med. Genet. 44:16-23(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN IPD1.
    18. "The IRAK-catalysed activation of the E3 ligase function of Pellino isoforms induces the Lys63-linked polyubiquitination of IRAK1."
      Ordureau A., Smith H., Windheim M., Peggie M., Carrick E., Morrice N., Cohen P.
      Biochem. J. 409:43-52(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PELI1.
    19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "IRAK1 and IRAK4 promote phosphorylation, ubiquitination, and degradation of MyD88 adaptor-like (Mal)."
      Dunne A., Carpenter S., Brikos C., Gray P., Strelow A., Wesche H., Morrice N., O'Neill L.A.
      J. Biol. Chem. 285:18276-18282(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TIRAP.
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Natural loss-of-function mutation of myeloid differentiation protein 88 disrupts its ability to form Myddosomes."
      Nagpal K., Plantinga T.S., Sirois C.M., Monks B.G., Latz E., Netea M.G., Golenbock D.T.
      J. Biol. Chem. 286:11875-11882(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    27. "What the Myddosome structure tells us about the initiation of innate immunity."
      Gay N.J., Gangloff M., O'Neill L.A.
      Trends Immunol. 32:104-109(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON MYDDOSOME.
    28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Crystal structures of IRAK-4 kinase in complex with inhibitors: a serine/threonine kinase with tyrosine as a gatekeeper."
      Wang Z., Liu J., Sudom A., Ayres M., Li S., Wesche H., Powers J.P., Walker N.P.C.
      Structure 14:1835-1844(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 154-460 IN COMPLEX WITH INHIBITORS, PHOSPHORYLATION AT THR-345 AND SER-346.
    30. "Crystal structures of the apo and inhibited IRAK4 kinase domain."
      Mol C.D., Arduini R.M., Baker D.P., Chien E.Y., Dougan D.R., Friedman J., Gibaja V., Hession C.A., Horne A.
      Submitted (DEC-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 163-460, PHOSPHORYLATION AT THR-342 AND THR-345.
    31. "Cutting Edge: IL-1 receptor-associated kinase 4 structures reveal novel features and multiple conformations."
      Kuglstatter A., Villasenor A.G., Shaw D., Lee S.W., Tsing S., Niu L., Song K.W., Barnett J.W., Browner M.F.
      J. Immunol. 178:2641-2645(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 160-460 IN COMPLEX WITH ATP ANALOGS, PHOSPHORYLATION AT THR-342; THR-345 AND SER-346, BIOPHYSICOCHEMICAL PROPERTIES.
    32. "Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling."
      Lin S.-C., Lo Y.-C., Wu H.
      Nature 465:885-890(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 4-106.
    33. "TLR9 activation induces normal neutrophil responses in a child with IRAK-4 deficiency: involvement of the direct PI3K pathway."
      Hoarau C., Gerard B., Lescanne E., Henry D., Francois S., Lacapere J.J., El Benna J., Dang P.M., Grandchamp B., Lebranchu Y., Gougerot-Pocidalo M.A., Elbim C.
      J. Immunol. 179:4754-4765(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IRAK4D CYS-12, CHARACTERIZATION OF VARIANT IRAK4D CYS-12, VARIANT HIS-391, FUNCTION.
    34. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-5; VAL-355; HIS-391 AND THR-428.
    35. Cited for: VARIANT IRAK4D ASP-298, CHARACTERIZATION OF VARIANT IRAK4D ASP-298.
    36. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN IRAK4D, VARIANT IRAK4D ASP-298.
    37. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS VAL-5; TRP-20; THR-26; VAL-39 AND ARG-98, CHARACTERIZATION OF VARIANTS IRAK4D CYS-12 AND ASP-298, FUNCTION, INTERACTION WITH MYD88.

    Entry informationi

    Entry nameiIRAK4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NWZ3
    Secondary accession number(s): Q69FE1, Q8TDF7, Q9Y589
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 1, 2000
    Last modified: June 24, 2015
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.