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Q8K4B2

- IRAK3_MOUSE

UniProt

Q8K4B2 - IRAK3_MOUSE

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Protein
Interleukin-1 receptor-associated kinase 3
Gene
Irak3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Inhibits dissociation of IRAK1 and IRAK4 from the Toll-like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei205 – 2051ATP By similarityBy similarity
Binding sitei324 – 3241ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi184 – 1929ATP By similarityBy similarity
Nucleotide bindingi308 – 3114ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. protein kinase activity Source: MGI
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: UniProtKB
  2. interleukin-1-mediated signaling pathway Source: MGI
  3. negative regulation of MAP kinase activity Source: BHF-UCL
  4. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
  5. negative regulation of cytokine-mediated signaling pathway Source: BHF-UCL
  6. negative regulation of innate immune response Source: BHF-UCL
  7. negative regulation of interleukin-12 production Source: BHF-UCL
  8. negative regulation of interleukin-6 production Source: BHF-UCL
  9. negative regulation of macrophage cytokine production Source: BHF-UCL
  10. negative regulation of protein catabolic process Source: BHF-UCL
  11. negative regulation of protein complex disassembly Source: Ensembl
  12. negative regulation of toll-like receptor signaling pathway Source: BHF-UCL
  13. negative regulation of tumor necrosis factor production Source: BHF-UCL
  14. positive regulation of NF-kappaB transcription factor activity Source: MGI
  15. positive regulation of macrophage tolerance induction Source: BHF-UCL
  16. protein autophosphorylation Source: MGI
  17. protein phosphorylation Source: UniProtKB
  18. regulation of protein complex disassembly Source: UniProtKB
  19. response to exogenous dsRNA Source: BHF-UCL
  20. response to lipopolysaccharide Source: BHF-UCL
  21. response to peptidoglycan Source: BHF-UCL
  22. response to virus Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_224208. Interleukin-1 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-1 receptor-associated kinase 3 (EC:2.7.11.1)
Short name:
IRAK-3
Alternative name(s):
IL-1 receptor-associated kinase M
Short name:
IRAK-M
Gene namesi
Name:Irak3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1921164. Irak3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. nucleus Source: BHF-UCL
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 609609Interleukin-1 receptor-associated kinase 3
PRO_0000086034Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei480 – 4801Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ8K4B2.

PTM databases

PhosphoSiteiQ8K4B2.

Expressioni

Tissue specificityi

Highly expressed in liver and thymus and at lower levels in heart, brain, spleen and kidney.1 Publication

Gene expression databases

ArrayExpressiQ8K4B2.
BgeeiQ8K4B2.
CleanExiMM_IRAK3.
GenevestigatoriQ8K4B2.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
IRAK4Q9NWZ34EBI-646179,EBI-448378From a different organism.
Irak4Q8R4K27EBI-646179,EBI-3842721
Traf6P701963EBI-646179,EBI-448028

Protein-protein interaction databases

BioGridi216351. 2 interactions.
IntActiQ8K4B2. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8K4B2.
SMRiQ8K4B2. Positions 184-457.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 10666Death
Add
BLAST
Domaini178 – 463286Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 death domain.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063073.
HOGENOMiHOG000060319.
HOVERGENiHBG052146.
InParanoidiQ8K4B2.
KOiK04732.
OMAiFKQEKKM.
OrthoDBiEOG7KQ21F.
PhylomeDBiQ8K4B2.
TreeFamiTF328924.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K4B2-1 [UniParc]FASTAAdd to Basket

« Hide

MAGRCGARGA LSPQLLLFDL PPALLGELCG ILDSCDGPLG WRGLAERLSN    50
SWLDVRHIEK YVNQGKSGTR ELLWSWAQKN KTIGDLLEVL QDMGHQRAIH 100
LIINYGVSWT PSVQTHHELP FPSFPPEVKH ACRENDPGPL EPANVTVDNV 150
LVPEHNEKGT LQKTPISFQS ILEGTKHFHK DFLIGEGEIF EVYRVDIRNQ 200
AYAVKLFKQE KKMQLKKHWK RFLSELEVLL LFRHPHILEL AAYFTETEKL 250
CLVYPYMSNG TLFDRLQCTN GTTPLSWHVR ISVLIGIAKA IQYLHNTQPC 300
AVICGNVSSA NILLDDQLQP KLTDFAAAHF RPNLEQQSST INMTGGGRKH 350
LWYMPEEYIR QGRLSVKTDV YSFGIVIMEV LTGCKVVLDD PKHVQLRDLL 400
MELMEKRGLD SCLSFLDRKI PPCPRNFSAK LFSLAGRCVA TKAKLRPTMD 450
EVLSSLESTQ PSLYFAEDPP TSLKSFRCPS PLFLDNVPSI PVEDDENQNN 500
HSVPPKEVLG TDRVTQKTPF ECSQSEVTFL GLDRNRGNRG SEADCNVPSS 550
SHEECWSPEL VAPSQDLSPT VISLGSSWEV PGHSYGSKPM EKRCSSGLFC 600
SEHEQSKKQ 609
Length:609
Mass (Da):68,455
Last modified:October 25, 2004 - v2
Checksum:iA63E010C9F29D856
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351C → W in AAM83393. 1 Publication
Sequence conflicti42 – 421R → W in AAM83393. 1 Publication
Sequence conflicti62 – 621V → L in AAM83393. 1 Publication
Sequence conflicti126 – 1261P → L in AAM83393. 1 Publication
Sequence conflicti147 – 1471V → M in AAM83393. 1 Publication
Sequence conflicti282 – 2821S → G in BAC33612. 1 Publication
Sequence conflicti282 – 2821S → N in AAM83393. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF461763 mRNA. Translation: AAM83393.1.
AJ440757 mRNA. Translation: CAD29448.2.
AK029057 mRNA. Translation: BAC26270.1.
AK049210 mRNA. Translation: BAC33612.1.
CCDSiCCDS24204.1.
RefSeqiNP_082955.2. NM_028679.3.
UniGeneiMm.146194.

Genome annotation databases

EnsembliENSMUST00000020448; ENSMUSP00000020448; ENSMUSG00000020227.
GeneIDi73914.
KEGGimmu:73914.
UCSCiuc007het.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF461763 mRNA. Translation: AAM83393.1 .
AJ440757 mRNA. Translation: CAD29448.2 .
AK029057 mRNA. Translation: BAC26270.1 .
AK049210 mRNA. Translation: BAC33612.1 .
CCDSi CCDS24204.1.
RefSeqi NP_082955.2. NM_028679.3.
UniGenei Mm.146194.

3D structure databases

ProteinModelPortali Q8K4B2.
SMRi Q8K4B2. Positions 184-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 216351. 2 interactions.
IntActi Q8K4B2. 6 interactions.

PTM databases

PhosphoSitei Q8K4B2.

Proteomic databases

PRIDEi Q8K4B2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020448 ; ENSMUSP00000020448 ; ENSMUSG00000020227 .
GeneIDi 73914.
KEGGi mmu:73914.
UCSCi uc007het.1. mouse.

Organism-specific databases

CTDi 11213.
MGIi MGI:1921164. Irak3.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063073.
HOGENOMi HOG000060319.
HOVERGENi HBG052146.
InParanoidi Q8K4B2.
KOi K04732.
OMAi FKQEKKM.
OrthoDBi EOG7KQ21F.
PhylomeDBi Q8K4B2.
TreeFami TF328924.

Enzyme and pathway databases

Reactomei REACT_224208. Interleukin-1 signaling.

Miscellaneous databases

NextBioi 339332.
PROi Q8K4B2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8K4B2.
Bgeei Q8K4B2.
CleanExi MM_IRAK3.
Genevestigatori Q8K4B2.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
InterProi IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
[Graphical view ]
Pfami PF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "IRAK-M is a negative regulator of Toll-like receptor signaling."
    Kobayashi K., Hernandez L.D., Galan J.E., Janeway C.A. Jr., Medzhitov R., Flavell R.A.
    Cell 110:191-202(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: C57BL/6.
    Tissue: Macrophage.
  2. "Identification and characterization of murine IRAK-M."
    Rosati O., Martin M.U.
    Biochem. Biophys. Res. Commun. 293:1472-1477(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Macrophage.
  3. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.

Entry informationi

Entry nameiIRAK3_MOUSE
AccessioniPrimary (citable) accession number: Q8K4B2
Secondary accession number(s): Q8C7U8, Q8CE40, Q8K1S8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: October 25, 2004
Last modified: September 3, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Asn-306 is present instead of the conserved Asp which is expected to be an active site residue. Low level autophosphorylation activity has been reported in 1 Publication, while other authors describe this as an inactive kinase.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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