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Protein Page:
IRAK1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
IRAK1 a TKL kinase of the IRAK family. Involved in Toll/IL-1 signaling. One of two putative serine/threonine kinases that become associated with the interleukin-1 receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. Extensively phosphorylated after its association with IL1-R-1. Polyubiquitinated; after cell stimulation with IL-1-beta. Polyubiquitination occurs with polyubiquitin chains linked through 'Lys-63'. Partially responsible for IL1-induced upregulation of the transcription factor NF-kappa B. Three isoforms of the human protein and produced by alternative splicing. Isoform 1 binds rapidly but is then degraded allowing isoform 2 to mediate a slower, more sustained response to the cytokine. Isoform 2 is inactive suggesting that the kinase activity of this enzyme is not required for IL-1 signaling. Once phosphorylated, IRAK1 recruits the adapter protein PELI1. Isoform 1 and isoform 2 are ubiquitously expressed in all tissues examined, with isoform 1 being more strongly expressed than isoform 2. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; EC 2.7.11.1; Protein kinase, TKL; Protein kinase, Ser/Thr (non-receptor); TKL group; IRAK family
Chromosomal Location of Human Ortholog: Xq28
Cellular Component: interleukin-1 receptor complex; cytoplasm; plasma membrane; endosome membrane; lipid particle; cytosol; nucleus
Molecular Function: NF-kappaB-inducing kinase activity; protein serine/threonine kinase activity; protein binding; interleukin-1 receptor binding; protein homodimerization activity; protein heterodimerization activity; ubiquitin-protein ligase activity; kinase activity; ATP binding; protein kinase activity
Biological Process: nerve growth factor receptor signaling pathway; activation of MAPK activity; protein amino acid autophosphorylation; positive regulation of smooth muscle cell proliferation; positive regulation of transcription, DNA-dependent; stress-activated MAPK cascade; protein ubiquitination; response to lipopolysaccharide; toll-like receptor 3 signaling pathway; signal transduction; protein amino acid phosphorylation; toll-like receptor 10 signaling pathway; activation of NF-kappaB transcription factor; toll-like receptor 5 signaling pathway; response to peptidoglycan; transmembrane receptor protein serine/threonine kinase signaling pathway; lipopolysaccharide-mediated signaling pathway; JNK cascade; toll-like receptor 4 signaling pathway; positive regulation of I-kappaB kinase/NF-kappaB cascade; MyD88-independent toll-like receptor signaling pathway; activation of NF-kappaB-inducing kinase; protein oligomerization; toll-like receptor 2 signaling pathway; MyD88-dependent toll-like receptor signaling pathway; inhibition of NF-kappaB transcription factor; toll-like receptor signaling pathway; regulation of cytokine and chemokine mediated signaling pathway; innate immune response; positive regulation of transcription from RNA polymerase II promoter; toll-like receptor 9 signaling pathway; negative regulation of apoptosis
Reference #:  P51617 (UniProtKB)
Alt. Names/Synonyms: Interleukin-1 receptor-associated kinase 1; IRAK; IRAK-1; IRAK1; pelle; Pelle homolog
Gene Symbols: IRAK1
Molecular weight: 76,537 Da
Basal Isoelectric point: 6.18  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

IRAK1

Protein Structure Not Found.

Substrate Sequence Logo
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Sites Implicated In
transcription, inhibited: T100‑p
enzymatic activity, induced: T209‑p, T387‑p
protein conformation: T66‑p, T209‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
3 0 T66-p CERSGQRtASVLWPW
1 0 T100-p LRARDIItAWHPPAP
1 2 S131-p PAEAEAWsPRkLPSS
2 0 K134-ub AEAWsPRkLPSSAST
1 0 S144-p SSASTFLsPAFPGSQ
1 0 S173-p SLWPPPPsPAPSSTk
1 0 K180-ub sPAPSSTkPGPESSV
1 0 T209-p LCEISRGtHNFSEEL
0 2 K239-ac RNTVYAVkRLKENAD
0 2 K253-ub DLEWTAVkQSFLTEV
0 3 K342-ub SLIHGDIkSSNVLLD
2 1 K355-ub LDERLTPkLGDFGLA
0 4 S371-p FSRFAGSsPsQssMV
0 1 S371 FSRFAGSSPsQssMV
0 1 S373-p RFAGSsPsQssMVAR
0 1 S375-p AGSsPsQssMVARTQ
2 1 S376-p GSsPsQssMVARTQT
3 0 T387-p RTQTVRGtLAYLPEE
2 4 K397-ub YLPEEYIkTGRLAVD
0 1 T431 VKTHGARTKYLKDLV
0 2 Y515-p RPPMTQVyERLEKLQ
0 2 S556-p SSTGRAHsGAAPWQP
0 1 S568-p WQPLAAPsGASAQAA
0 3 S601-p GLSAALRsWHLtPSC
0 1 T605-p ALRsWHLtPSCPLDP
0 1 S650-p EGLALGSsASsSSEP
0 1 S653-p ALGSsASsSSEPPQI
12756 : Phospho-IRAK1 (Thr209) Antibody
  IRAK1 iso4  
T66 CERSGQRTASVLWPW
T100 LRARDIITAWHPPAP
S131 PAEAEAWSPRKLPSS
K134 AEAWSPRKLPSSAST
S144 SSASTFLSPAFPGSQ
S173 SLWPPPPSPAPSSTK
K180 SPAPSSTKPGPESSV
T209 LCEISRGTHNFSEEL
K239 RNTVYAVKRLKENAD
K253 DLEWTAVKQSFLTEV
K342 SLIHGDIKSSNVLLD
K355 LDERLTPKLGDFGLA
S371 FSRFAGSSPSQSSMV
S371 FSRFAGSSPSQSSMV
S373 RFAGSSPSQSSMVAR
S375 AGSSPSQSSMVARTQ
S376 GSSPSQSSMVARTQT
T387 RTQTVRGTLAYLPEE
K397 YLPEEYIKTGRLAVD
T431-p VKTHGARtKYLVYER
Y436 ARtKYLVYERLEKLQ
S477 SSTGRAHSGAAPWQP
S489 WQPLAAPSGASAQAA
S522 GLSAALRSWHLTPSC
T526 ALRSWHLTPSCPLDP
S571 EGLALGSSASSSSEP
S574 ALGSSASSSSEPPQI
12756 : Phospho-IRAK1 (Thr209) Antibody
  mouse

 
T66-p CERSEQRtASVLWPW
T100 LRARDIITAWHPPAP
S131 GSEAGDWSPRKLQSS
K134 AGDWSPRKLQSSAST
S144 SSASTFLSPAFPGSQ
S173 SLGPPLPSSAPSSTK
K180 SSAPSSTKSSPESPV
T209 FCEISQGTCNFSEEL
K239 RNTTYAVKRLKEEAD
K253 DLEWTMVKQSFLTEV
K342 SLIHGDIKSSNVLLD
K355 LDERLMPKLGDFGLA
K371 FSRFAGAKASQSSTV
K371-ub FSRFAGAkASQSSTV
S373 RFAGAkASQSSTVAR
S375 AGAkASQSSTVARTS
S376 GAkASQSSTVARTST
T387 RTSTVRGTLAYLPEE
K397 YLPEEYIKTGRLAVD
T431 VRTQGAKTKYLKDLI
Y515 RPPMTQVYKRLEGLQ
S553 STTGSAQSGDEPWQP
T565 WQPLVVTTRAPAQAA
S598 GLSATLHSWHLTPGS
T602 TLHSWHLTPGSHPSP
S647 EGSPTGSSSLLSSEP
L650 PTGSSSLLSSEPPQI
  rat

 
T66 CERSEQRTASVLWPW
T100 LRARDIITAWHPPAS
S131 GSETEDWSPRKLQSS
K134 TEDWSPRKLQSSAST
S144 SSASTFLSPAFPGSQ
S173 SLGPPLQSSAPSSIK
K180 SSAPSSIKPSPESPV
T209 FCEISQGTCNFSEEL
K239 RNTTYAVKRLKEEAD
K253 DLEWTVVKQSFLTEV
K342 SLIHGDIKSSNVLLD
K355-ub LDERLMPkLGDFGLA
N371 FSRFAGANPSQSSTV
N371 FSRFAGANPSQSSTV
S373 RFAGANPSQSSTVAR
S375 AGANPSQSSTVARTC
S376 GANPSQSSTVARTCT
T387 RTCTVRGTLAYLPEE
K397-ub YLPEEYIkTGRLAVD
T431 VRTQGAKTKYLKDLI
Y515 RPPMTQVYKRLEGLQ
S553 STTGSAQSGDEPWQP
T565 WQPLVVTTRAPAQAA
S598 GLSATLHSWHLTPDS
T602 TLHSWHLTPDSHPSP
S647 EGSSMGSSSLLSSEP
L650 SMGSSSLLSSEPPQI
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