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Reviewed, UniProtKB/Swiss-Prot Q8R4K2 (IRAK4_MOUSE)

Last modified January 19, 2010. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Interleukin-1 receptor-associated kinase 4
      Short name=IRAK-4
    EC=2.7.11.1
Gene names
Name: Irak4
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for the efficient recruitment of IRAK1 to the IL-1 receptor complex following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. Phosphorylates IRAK1 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Subunit structure

IL-1 stimulation leads to the formation of a signaling complex which dissociates from the IL-1 receptor following the binding of PELI1 By similarity. Interacts with IL1RL1 By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily.

Contains 1 death domain.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Interleukin-1 receptor-associated kinase 4
PRO_0000086036

Regions

Domain20 – 10485Death
Domain186 – 454269Protein kinase
Nucleotide binding192 – 2009ATP By similarity

Sites

Active site3111Proton acceptor By similarity
Binding site2131ATP By similarity

Amino acid modifications

Modified residue31N6-acetyllysine By similarity
Modified residue341N6-acetyllysine By similarity
Modified residue1521Phosphoserine By similarity

Experimental info

Sequence conflict3211K → R in AAH51676. Ref.3

Secondary structure

...................... 459
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8R4K2-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: FC11AD06983B7AEB

FASTA45950,872
        10         20         30         40         50         60 
MNKPLTPSTY IRNLNVGILR KLSDFIDPQE GWKKLAVAIK KPSGDDRYNQ FHIRRFEALL 

        70         80         90        100        110        120 
QTGKSPTCEL LFDWGTTNCT VGDLVDLLVQ IELFAPATLL LPDAVPQTVK SLPPREAATV 

       130        140        150        160        170        180 
AQTHGPCQEK DRTSVMPMPK LEHSCEPPDS SSPDNRSVES SDTRFHSFSF HELKSITNNF 

       190        200        210        220        230        240 
DEQPASAGGN RMGEGGFGVV YKGCVNNTIV AVKKLGAMVE ISTEELKQQF DQEIKVMATC 

       250        260        270        280        290        300 
QHENLVELLG FSSDSDNLCL VYAYMPNGSL LDRLSCLDGT PPLSWHTRCK VAQGTANGIR 

       310        320        330        340        350        360 
FLHENHHIHR DIKSANILLD KDFTAKISDF GLARASARLA QTVMTSRIVG TTAYMAPEAL 

       370        380        390        400        410        420 
RGEITPKSDI YSFGVVLLEL ITGLAAVDEN REPQLLLDIK EEIEDEEKTI EDYTDEKMSD 

       430        440        450 
ADPASVEAMY SAASQCLHEK KNRRPDIAKV QQLLQEMSA 

« Hide

References

« Hide 'large scale' references
[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: 11960013] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[4]"Molecular structure of the IL-1R-associated kinase-4 death domain and its implications for TLR signaling."
Lasker M.V., Gajjar M.M., Nair S.K.
J. Immunol. 175:4175-4179(2005) [PubMed: 16177054] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-113.
[5]"Solution structure of the death domain of interleukin-1 receptor-associated kinase 4 (IRAK4) from Mus musculus."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-114.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF445803 mRNA. Translation: AAM15773.1.
AK028837 mRNA. Translation: BAC26146.1.
BC051676 mRNA. Translation: AAH51676.1.
IPIIPI00153899.
RefSeqNP_084202.2.
UniGeneMm.422858

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WH4NMR-A1-114[»]
2A9IX-ray1.70A1-113[»]
SMRQ8R4K2. Positions 163-458.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8R4K2.

PTM databases

PhosphoSiteQ8R4K2.

Proteomic databases

PRIDEQ8R4K2.

Genome annotation databases

EnsemblENSMUST00000074936; ENSMUSP00000074471; ENSMUSG00000059883; Mus musculus. [Genome view]
GeneID266632.
KEGGmmu:266632.
UCSCuc007xjk.1. mouse.

Organism-specific databases

CTD266632.
MGIMGI:2182474. Irak4.

Phylogenomic databases

HOGENOMHBG713523.
HOVERGENQ8R4K2.
InParanoidQ8R4K2.
OMAMVEISTE.
PhylomeDBQ8R4K2.

Enzyme and pathway databases

BRENDA2.7.11.1. 244.

Gene expression databases

ArrayExpressQ8R4K2.
BgeeQ8R4K2.
CleanExMM_IRAK4.
GenevestigatorQ8R4K2.
GermOnlineENSMUSG00000059883. Mus musculus.

Family and domain databases

InterProIPR000488. Death.
IPR011029. DEATH-like.
IPR017428. Interleukin-1_rcpt-assoc_kin4.
IPR015787. Interleukin1_rcpt-assoc_kin4_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_prot_kinase-like_dom.
[Graphical view]
PANTHERPTHR23258:SF428. IRAK4. 1 hit.
PfamPF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF038189. IRAK4. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. False negative.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio392172.
SOURCESearch...

Entry information

Entry nameIRAK4_MOUSE
AccessionPrimary (citable) accession number: Q8R4K2
Secondary accession number(s): Q80WW1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2002
Last modified: January 19, 2010
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents