+ |
CHUK | up-regulates activity
phosphorylation
|
AMBRA1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272974 |
Ser1043 |
CRPEALNsGVEYYWD |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
30217973 |
Furthermore, we show that mitophagy function of AMBRA1 is post-translationally controlled, upon HUWE1 activity, by a positive phosphorylation on its serine 1014. This modification is mediated by the IKKα kinase and induces structural changes in AMBRA1, thus promoting its interaction with LC3/GABARAP (mATG8) proteins and its mitophagic activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates
phosphorylation
|
FOXA2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195312 |
Ser107 |
AGMGPHLsPSLSPLG |
Homo sapiens |
|
pmid |
sentence |
22196886 |
Here, we show that ikk_, an important downstream kinase of tnf_, interacts with and phosphorylates foxa2 at s107/s111, thereby suppressing foxa2 transactivation activity and leading to decreased numb expression |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195316 |
Ser111 |
PHLSPSLsPLGGQAA |
Homo sapiens |
|
pmid |
sentence |
22196886 |
Here, we show that ikk_, an important downstream kinase of tnf_, interacts with and phosphorylates foxa2 at s107/s111, thereby suppressing foxa2 transactivation activity and leading to decreased numb expression |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CHUK | up-regulates activity
phosphorylation
|
BCL3 |
0.439 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277362 |
Ser122 |
CPMEHPLsADIAMAT |
in vitro |
|
pmid |
sentence |
28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277363 |
Ser454 |
PSPAPGGs |
in vitro |
|
pmid |
sentence |
28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CHUK | up-regulates
phosphorylation, binding
|
CREBBP |
0.533 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154329 |
Ser1382 |
MKSRFVDsGEMSESF |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
17434128 |
Phosphorylation of cbp by ikkalpha promotes cell growth by switching the binding preference of cbp from p53 to nf-kappabhere, we show that ikkalpha phosphorylates cbp at serine 1382 and serine 1386 and consequently increases cbp's hat and transcriptional activities |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154333 |
Ser1386 |
FVDSGEMsESFPYRT |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
17434128 |
Phosphorylation of cbp by ikkalpha promotes cell growth by switching the binding preference of cbp from p53 to nf-kappabhere, we show that ikkalpha phosphorylates cbp at serine 1382 and serine 1386 and consequently increases cbp's hat and transcriptional activities |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-101539 |
|
|
Homo sapiens |
|
pmid |
sentence |
12789342 |
Ikk-alpha interacts with creb-binding protein and in conjunction with rel a is recruited to nf-kappab-responsive promoters and mediates the cytokine-induced phosphorylation and subsequent acetylation of specific residues in histone h3. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CHUK | up-regulates activity
phosphorylation
|
MTOR |
0.523 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276646 |
Ser1415 |
PTPAILEsLISINNK |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
24990947 |
Importantly, IKKα is shown to phosphorylate mTOR at serine 1415 in a manner dependent on Akt to promote mTORC1 activity. These results demonstrate that IKKα is an effector of Akt in promoting mTORC1 activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP3K14 | up-regulates activity
phosphorylation
|
CHUK |
0.684 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-55942 |
Ser176 |
AKDVDQGsLCTSFVG |
Homo sapiens |
|
pmid |
sentence |
9520446 |
Nf-kappab-inducing kinase activates ikk-alpha by phosphorylation of ser-176. Nik preferentially phosphorylates ikk-alpha over ikk-beta, leading to the activation of ikk-alpha kinase activity; the accumulated nik phosphorylates ikkalfa. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-55946 |
Ser180 |
DQGSLCTsFVGTLQY |
Homo sapiens |
|
pmid |
sentence |
9520446 |
NIK preferentially phosphorylates ikk-alpha over ikk-beta, leading to the activation of ikk-alpha kinase activity; the accumulated nik phosphorylates ikkalfa. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167060 |
|
|
Homo sapiens |
|
pmid |
sentence |
20651737 |
Once activated by autophosphorylation, nik activates ikkalpha, which in turn phosphorylates nf-kb2. This stimulates limited proteasome-mediated proteolysis of nf-kb2 to p52. Removal of the carboxy-terminal ankyrin repeats from nf-kb2 releases the p52/RELB heterodimer, allowing its translocation to the nucleus where it instigates the expression of nf-kb target genes. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
Pathways: | NF-KB Non Canonical |
+ |
CHUK | up-regulates activity
phosphorylation
|
IKBKB |
0.653 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250771 |
Ser177 |
AKELDQGsLCTSFVG |
in vitro |
|
pmid |
sentence |
10022904 |
Our data indicate that IKKα stimulates IKKβ kinase activity for the IκBα substrate. Finally, we demonstrate that IKKα can phosphorylate IKKβ in in vitro kinase assays. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250772 |
Ser181 |
DQGSLCTsFVGTLQY |
in vitro |
|
pmid |
sentence |
10022904 |
Our data indicate that IKKα stimulates IKKβ kinase activity for the IκBα substrate. Finally, we demonstrate that IKKα can phosphorylate IKKβ in in vitro kinase assays. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CHUK | down-regulates activity
phosphorylation
|
COPS5 |
0.329 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275507 |
Ser201 |
KPPDEGPsEYQTIPL |
in vitro |
|
pmid |
sentence |
31950832 |
Overexpression of IKKalpha or IKKbeta leads to enhanced phosphorylation of CSN5, the catalytic subunit for CSN deneddylase activity. Mutational analyses have revealed that phosphorylation at serine 201 and threonine 205 of CSN5 impairs CSN-mediated deneddylation activity in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275508 |
Thr205 |
EGPSEYQtIPLNKIE |
in vitro |
|
pmid |
sentence |
31950832 |
Overexpression of IKKalpha or IKKbeta leads to enhanced phosphorylation of CSN5, the catalytic subunit for CSN deneddylase activity. Mutational analyses have revealed that phosphorylation at serine 201 and threonine 205 of CSN5 impairs CSN-mediated deneddylation activity in vitro. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CHUK | down-regulates
phosphorylation
|
NCOR2 |
0.426 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-129956 |
Ser2407 |
AKVSGRPsSRKAKSP |
Homo sapiens |
|
pmid |
sentence |
15494311 |
Nf-kappab transcription requires ikkalpha to phosphorylate smrt on chromatin, stimulating the exchange of corepressor for coactivator complexes. Ikk directly phosphorylates smrt to stimulate nuclear export. Ikkalpha orchestrates smrt derepression, a prerequisite for nf-kappab transcription and survival. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates quantity by destabilization
phosphorylation
|
ELAVL1 |
0.328 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276422 |
Ser304 |
EAAMAIAsLNGYRLG |
Homo sapiens |
LNCaP Cell |
pmid |
sentence |
23115237 |
Furthermore, mutational analysis indicates that IKKα-dependent phosphorylation at Ser-304 is crucial to the binding of HuR to β-TrCP1. Mechanistically, this HuR degradation pathway differs from that reported for heat shock and hypoxia, which underlies the complexity in the regulation of HuR turnover under different stress stimuli. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates quantity by destabilization
phosphorylation
|
NFKBIA |
0.893 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-52875 |
Ser32 |
LLDDRHDsGLDSMKD |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
9346241 |
We described the purification of a 900 kda protein kinase complex, the ikb kinase (ikk), that phosphorylates ikbalfa and ikbbeta at the sites that mediate their ubiquitination and degradation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-52879 |
Ser36 |
RHDSGLDsMKDEEYE |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
9346241 |
We described the purification of a 900 kda protein kinase complex, the ikb kinase (ikk), that phosphorylates ikbalfa and ikbbeta at the sites that mediate their ubiquitination and degradation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates activity
phosphorylation
|
CYLD |
0.524 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204688 |
Ser418 |
TTENRFHsLPFSLTK |
Homo sapiens |
Neuron |
pmid |
sentence |
24614225 |
Thus, serine 418 is phosphorylated in vivo. Cyld phosphorylation may serve as a mechanism to inactivate its traf2 deubiquitination activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204696 |
Ser432 |
KMPNTNGsIGHSPLS |
Homo sapiens |
Neuron |
pmid |
sentence |
24614225 |
The phosphorylation of cyld was completely abolished by the combined mutations of the entire serine cluster (m4, lane 5). Similar results were obtained with the ikk holoenzyme (fig. 4c, panel 1), recombinant ikk_ (panel 2), and recombinant ikk_cyld phosphorylation may serve as a mechanism to inactivate its traf2 deubiquitination activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204700 |
Ser436 |
TNGSIGHsPLSLSAQ |
Homo sapiens |
Neuron |
pmid |
sentence |
24614225 |
The phosphorylation of cyld was completely abolished by the combined mutations of the entire serine cluster (m4, lane 5). Similar results were obtained with the ikk holoenzyme (fig. 4c, panel 1), recombinant ikk_ (panel 2), and recombinant ikk_cyld phosphorylation may serve as a mechanism to inactivate its traf2 deubiquitination activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204704 |
Ser439 |
SIGHSPLsLSAQSVM |
Homo sapiens |
Neuron |
pmid |
sentence |
24614225 |
The phosphorylation of cyld was completely abolished by the combined mutations of the entire serine cluster (m4, lane 5). Similar results were obtained with the ikk holoenzyme (fig. 4c, panel 1), recombinant ikk_ (panel 2), and recombinant ikk_cyld phosphorylation may serve as a mechanism to inactivate its traf2 deubiquitination activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204712 |
Ser444 |
PLSLSAQsVMEELNT |
Homo sapiens |
Neuron |
pmid |
sentence |
24614225 |
The phosphorylation of cyld was completely abolished by the combined mutations of the entire serine cluster (m4, lane 5). Similar results were obtained with the ikk holoenzyme (fig. 4c, panel 1), recombinant ikk_ (panel 2), and recombinant ikk_cyld phosphorylation may serve as a mechanism to inactivate its traf2 deubiquitination activity. |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
CHUK | up-regulates activity
phosphorylation
|
CYLD |
0.524 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204692 |
Ser422 |
RFHSLPFsLTKMPNT |
Homo sapiens |
Neuron |
pmid |
sentence |
24614225 |
The phosphorylation of cyld was completely abolished by the combined mutations of the entire serine cluster (m4, lane 5). Similar results were obtained with the ikk holoenzyme (fig. 4c, panel 1), recombinant ikk_ (panel 2), and recombinant ikk_cyld phosphorylation may serve as a mechanism to inactivate its traf2 deubiquitination activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204708 |
Ser441 |
GHSPLSLsAQSVMEE |
Homo sapiens |
Neuron |
pmid |
sentence |
24614225 |
The phosphorylation of cyld was completely abolished by the combined mutations of the entire serine cluster (m4, lane 5). Similar results were obtained with the ikk holoenzyme (fig. 4c, panel 1), recombinant ikk_ (panel 2), and recombinant ikk_cyld phosphorylation may serve as a mechanism to inactivate its traf2 deubiquitination activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates
phosphorylation
|
TRAF4 |
0.392 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197253 |
Ser426 |
KPGTWRGsLDESSLG |
Homo sapiens |
|
pmid |
sentence |
22547678 |
Traf4 is atypical within its family because it is the only traf family member to negatively regulate innate immune signaling. Ikk_'s phosphorylation of serine-426 on traf4 was required for this negative regulation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | up-regulates activity
phosphorylation
|
RELA |
0.841 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-71270 |
Ser536 |
SGDEDFSsIADMDFS |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10521409 |
Our data suggest that the stimulation of nfkb by akt is dependent on the phosphorylation of p65 at s534, mediated by ikk (ikb kinase) alfa and beta. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-129931 |
Ser536 |
SGDEDFSsIADMDFS |
Homo sapiens |
HEK-293 Cell, HeLa Cell |
pmid |
sentence |
15489227 |
Chromatographic fractionation of cell extracts allowed the identification of two distinct enzymatic activities phosphorylating ser-536. Peak 1 represents an unknown kinase, whereas peak 2 contained ikkalpha, ikkbeta, ikkepsilon, and tbk1. collectively, our results provide evidence for at least five kinases that converge on ser-536 of p65 and a novel function for this phosphorylation site in the recruitment of components of the basal transcriptional machinery to the interleukin-8 promoter. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132568 |
Ser536 |
SGDEDFSsIADMDFS |
Homo sapiens |
Monocyte |
pmid |
sentence |
15611276 |
Our data suggest that the stimulation of nfkb by akt is dependent on the phosphorylation of p65 at s534, mediated by ikk (ikb kinase) alfa and beta. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates activity
phosphorylation
|
MTURN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273612 |
Ser58 |
GDNFHVWsESEDCLP |
in vitro |
|
pmid |
sentence |
28704656 |
INKIT interacted with IKKα/β and TBK1/IKKɛ, impairing the recruitment and phosphorylation of p65 and IRF3. Viral infection induced IKK-mediated phosphorylation of INKIT at Ser58, resulting in its dissociation from the IKKs. Our findings thus uncover INKIT as a regulator of innate antiviral responses. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CHUK | up-regulates activity
phosphorylation
|
TAX1BP1 |
0.39 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-175058 |
Ser593 |
NYKELKRsLENPAER |
Mus musculus |
MEF Cell |
pmid |
sentence |
21765415 |
Here we demonstrate that tax1bp1 was inducibly phosphorylated on ser593 and ser624 in response to proinflammatory stimuli. The kinase ikkalpha, But not ikkbeta, was required for phosphorylation of tax1bp1 and directly phosphorylated tax1bp1 in response to stimulation with tumor necrosis factor (tnf) or interleukin 1 (il-1). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-175062 |
Ser666 |
RPPVRVPsWGLEDNV |
Mus musculus |
MEF Cell |
pmid |
sentence |
21765415 |
Here we demonstrate that tax1bp1 was inducibly phosphorylated on ser593 and ser624 in response to proinflammatory stimuli. The kinase ikkalpha, but not ikkbeta, was required for phosphorylation of tax1bp1 and directly phosphorylated tax1bp1 in response to stimulation with tumor necrosis factor (tnf) or interleukin 1 (il-1). |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
CHUK | down-regulates
phosphorylation
|
FOXO3 |
0.553 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124203 |
Ser644 |
GLDFNFDsLISTQNV |
Homo sapiens |
|
pmid |
sentence |
15084260 |
Ikappab kinase promotes tumorigenesis through inhibition of forkhead foxo3a. The tnf treatment of ht-29 cells increased ikk-dependent foxo3 ser644 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates
phosphorylation
|
FOXO |
0.553 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252893 |
Ser644 |
GLDFNFDsLISTQNV |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
15084260 |
Ikappab kinase promotes tumorigenesis through inhibition of forkhead foxo3a. The tnf treatment of ht-29 cells increased ikk-dependent foxo3 ser644 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | up-regulates
phosphorylation
|
NCOA3 |
0.403 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127064 |
Ser857 |
PPYNRAVsLDSPVSV |
Homo sapiens |
|
pmid |
sentence |
15383283 |
Herein, we report the successful identification of six functional in vivo src-3 phosphorylation sites. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196953 |
Ser857 |
PPYNRAVsLDSPVSV |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
22505454 |
Herein, we report the successful identification of six functional in vivo src-3 phosphorylation sites. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-135050 |
|
|
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
15808510 |
Ikkalpha phosphorylates eralpha, aib1/src-3, and histone h3. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CHUK | up-regulates activity
phosphorylation
|
NFKB2 |
0.784 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124226 |
Ser866 |
TAEVKEDsAYGSQSV |
Mus musculus |
Lymphoma Cell |
pmid |
sentence |
15084608 |
Ikkalfa phosphorylates p100, leading to its proteasomal processing to p52. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124230 |
Ser870 |
KEDSAYGsQSVEQEA |
Mus musculus |
Lymphoma Cell |
pmid |
sentence |
15084608 |
Ikkalfa phosphorylates p100, leading to its proteasomal processing to p52. |
|
Publications: |
2 |
Organism: |
Mus Musculus |
Pathways: | NF-KB Non Canonical |
+ |
CHUK | down-regulates quantity by destabilization
phosphorylation
|
NFKB1 |
0.737 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235434 |
Ser923 |
DELRDSDsVCDSGVE |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
11297557 |
The i b kinase (ikk) complex rapidly phosphorylates nf- b1 p105 on serine 927 in the pest region romashkova et al. demonstrated that akt binds to and activates inhibitor of kappa b kinase-alfa (ikkalfa), which in turn phosphorylates and thereby promotes the degradation of the inhibitory cofactor of nf-kb, i-kb the scf-betatrcp complex is responsible for the ubiquitination of p100 and p105 following their phosphorylation by ikk. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70449 |
Ser923 |
DELRDSDsVCDSGVE |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10469655 |
All residues of p105 phosphorylated by ikka are c-terminal; the major phosphorylation region contains three serines (ser923; ser927;ser932) and two threonines (thr927 and thr391). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235438 |
Ser927 |
DSDSVCDsGVETSFR |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
11297557 |
The i b kinase (ikk) complex rapidly phosphorylates nf- b1 p105 on serine 927 in the pest region romashkova et al. demonstrated that akt binds to and activates inhibitor of kappa b kinase-alfa (ikkalfa), which in turn phosphorylates and thereby promotes the degradation of the inhibitory cofactor of nf-kb, i-kb the scf-betatrcp complex is responsible for the ubiquitination of p100 and p105 following their phosphorylation by ikk. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70453 |
Ser927 |
DSDSVCDsGVETSFR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10469655 |
All residues of p105 phosphorylated by ikka are c-terminal; the major phosphorylation region contains three serines (ser923; ser927;ser932) and two threonines (thr927 and thr391). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235442 |
Ser932 |
CDSGVETsFRKLSFT |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
11297557 |
The i b kinase (ikk) complex rapidly phosphorylates nf- b1 p105 on serine 927 in the pest region romashkova et al. demonstrated that akt binds to and activates inhibitor of kappa b kinase-alfa (ikkalfa), which in turn phosphorylates and thereby promotes the degradation of the inhibitory cofactor of nf-kb, i-kb the scf-betatrcp complex is responsible for the ubiquitination of p100 and p105 following their phosphorylation by ikk. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70457 |
Ser932 |
CDSGVETsFRKLSFT |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10469655 |
All residues of p105 phosphorylated by ikka are c-terminal; the major phosphorylation region contains three serines (ser923; ser927;ser932) and two threonines (thr927 and thr391). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70461 |
Thr931 |
VCDSGVEtSFRKLSF |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10469655 |
All residues of p105 phosphorylated by ikka are c-terminal; the major phosphorylation region contains three serines (ser923; ser927;ser932) and two threonines (thr927 and thr391). |
|
Publications: |
7 |
Organism: |
Mus Musculus, Homo Sapiens |
+ |
AKT3 | up-regulates
phosphorylation
|
CHUK |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-187062 |
Thr23 |
EMRERLGtGGFGNVC |
Homo sapiens |
|
pmid |
sentence |
19609947 |
Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | up-regulates
phosphorylation
|
CHUK |
0.653 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-187006 |
Thr23 |
EMRERLGtGGFGNVC |
Homo sapiens |
|
pmid |
sentence |
19609947 |
Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT2 | up-regulates
phosphorylation
|
CHUK |
0.508 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-187010 |
Thr23 |
EMRERLGtGGFGNVC |
Homo sapiens |
|
pmid |
sentence |
19609947 |
Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT | up-regulates
phosphorylation
|
CHUK |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244210 |
Thr23 |
EMRERLGtGGFGNVC |
Homo sapiens |
|
pmid |
sentence |
19609947 |
Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates
phosphorylation
|
CCND1 |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139570 |
Thr286 |
EEVDLACtPTDVRDV |
Homo sapiens |
|
pmid |
sentence |
16103118 |
Ikkalpha regulates subcellular localization and proteolysis of cyclin d1 by phosphorylation of cyclin d1 at thr286. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates quantity by destabilization
phosphorylation
|
MAP3K14 |
0.684 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165622 |
Thr559 |
TGDYIPGtETHMAPE |
Homo sapiens |
B-lymphocyte |
pmid |
sentence |
20501937 |
Upon activation by nik, ikkalfa phosphorylates nik, triggering its proteolysis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | NF-KB Non Canonical |
+ |
N'-(1,8-dimethyl-4-imidazo[1,2-a]quinoxalinyl)ethane-1,2-diamine | down-regulates activity
chemical inhibition
|
CHUK |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258085 |
|
|
in vitro |
|
pmid |
sentence |
22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CHUK | down-regulates
phosphorylation
|
NfKb-p65/p50 |
0.789 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-217397 |
|
|
Homo sapiens |
|
pmid |
sentence |
10469655 |
All residues of p105 phosphorylated by ikka are c-terminal; the major phosphorylation region contains three serines (ser923; ser927;ser932) and two threonines (thr927 and thr391). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | down-regulates
phosphorylation
|
TSC2 |
0.301 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178664 |
|
|
Homo sapiens |
MCF-7 Cell |
pmid |
sentence |
18490760 |
Insulin activation of mtor requires akt in a manner that involves ikkalpha, preferentially to ikkbeta, and tsc2 phosphorylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXW11 | down-regulates quantity by destabilization
binding
|
CHUK |
0.416 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272545 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10321728 |
We identified a human F-box/WD40 repeats protein (HOS), which is homologous to Slimb/h betaTrCP. Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | form complex
binding
|
IKK-complex |
0.774 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164506 |
|
|
Homo sapiens |
|
pmid |
sentence |
20300203 |
The kinase(s) responsible for the phosphorylation of the ikb inhibitors remained elusive for many years, until the biochemical purification of a cytoplasmic high-molecular weight complex migrating around 700900 kda and containing two related catalytic subunits, ikkalfa and ikkbeta. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | NF-KB Non Canonical |
+ |
RUNX3 | down-regulates quantity by repression
transcriptional regulation
|
CHUK |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255090 |
|
|
Homo sapiens |
|
pmid |
sentence |
17956589 |
Comprehensive analysis using a cDNA microarray showed that RUNX3 upregulated 17 apoptosis-related genes (including FADD, TRAF6, caspase-2, ING1, ING4, Calpain 10, and DNase1) and downregulated 135 apoptosis-related genes (including FLIP, PEA15, TXN2, HSPD1, IKK, and TIAL1) in MKN-1 cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ERC1 | up-regulates
binding
|
CHUK |
0.573 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-126430 |
|
|
Homo sapiens |
|
pmid |
sentence |
15218148 |
Elks likely functions by recruiting ikappabalpha to the ikk complex and thus serves a regulatory function for ikk activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHUK | up-regulates
phosphorylation
|
IRF7 |
0.68 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146116 |
|
|
Homo sapiens |
|
pmid |
sentence |
16612387 |
Ikkalfa associated with and phosphorylated and activate interferon regulatory factor-7 (irf7), which is required for interferon-alfa (ifnalfa) production. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
CHUK |
0.519 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272548 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10321728 |
We identified a human F-box/WD40 repeats protein (HOS), which is homologous to Slimb/h betaTrCP. Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |