Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-256441	Asp242	VRQKSEVdIVVSEDL	Homo sapiens
pmid	sentence
11741536	Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-256436	Asp373	PATQCISdGKLNEGH	Homo sapiens
pmid	sentence
11741536	Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-256435	Asp546	ALQTDIVdLQRSPMG	Homo sapiens
pmid	sentence
11741536	Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-256434	Asp78	PNVVAARdVPEGMQN	Homo sapiens
pmid	sentence
11741536	Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-112788	Asp242	VRQKSEVdIVVSEDL	Homo sapiens
pmid	sentence
11741536	Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-112792	Asp373	PATQCISdGKLNEGH	Homo sapiens
pmid	sentence
11741536	Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-112796	Asp546	ALQTDIVdLQRSPMG	Homo sapiens
pmid	sentence
11741536	Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-112800	Asp78	PNVVAARdVPEGMQN	Homo sapiens
pmid	sentence
11741536	Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277364	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
SIGNOR-277365	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

Identifier	Residue	Sequence	Organism
SIGNOR-138608	Ser132	GDYFRYLsEVASGDN	Homo sapiens
pmid	sentence
16024783	We provide a mechanism for these observations through the phosphorylation of 14-3-3beta by ikkbeta and pkcdelta on serine residues ser132 and ser60, respectively, which interferes with its binding to ttp and hence the retention of ttp in the cytoplasm.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276291	Ser134	DGATNNLsRSNSDES	Homo sapiens	HEK-293 Cell
pmid	sentence
16818229	Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276290	Ser136	ATNNLSRsNSDESNF	Homo sapiens	HEK-293 Cell
pmid	sentence
16818229	Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276292	Ser138	NNLSRSNsDESNFSE	Homo sapiens	HEK-293 Cell
pmid	sentence
16818229	Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276293	Ser141	SRSNSDEsNFSEKLR	Homo sapiens	HEK-293 Cell
pmid	sentence
16818229	Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276289	Ser144	NSDESNFsEKLRAST	Homo sapiens	HEK-293 Cell
pmid	sentence
16818229	Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-109490	Ser177	AKELDQGsLCTSFVG	Homo sapiens
pmid	sentence
11460167	Tak1 become activated and then phosphorylates and activates ikk2 which in turn now phosphorylates ikba, marking it for k48-ubiquitination and proteasomal degradation. tak1 kinase complex phosphorylates and activates ikk in a manner that depends on traf6 and ubc13-uev1a our studies suggests that tak1_ acts as an upstream activating kinase for ikkbeta.

Identifier	Residue	Sequence	Organism
SIGNOR-109494	Ser181	DQGSLCTsFVGTLQY	Homo sapiens
pmid	sentence
11460167	Tak1 become activated and then phosphorylates and activates ikk2 which in turn now phosphorylates ikba, marking it for k48-ubiquitination and proteasomal degradation. tak1 kinase complex phosphorylates and activates ikk in a manner that depends on traf6 and ubc13-uev1a our studies suggests that tak1_ acts as an upstream activating kinase for ikkbeta.

Identifier	Residue	Organism
SIGNOR-187242		Homo sapiens
pmid	sentence
19632174	Tak1 become activated and then phosphorylates and activates ikk2 which in turn now phosphorylates ikba, marking it for k48-ubiquitination and proteasomal degradation. tak1 kinase complex phosphorylates and activates ikk in a manner that depends on traf6 and ubc13-uev1a our studies suggests that tak1_ acts as an upstream activating kinase for ikkbeta.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248581	Ser177	AKELDQGsLCTSFVG	Homo sapiens	Carcinoma Cell
pmid	sentence
19607706	Permanent activation of the upstream kinase IKK beta results from UVB-induced inhibition of the catalytic subunit of Ser-Thr phosphatase PP2A (PP2Ac), leading to immediate phosphorylation and degradation of newly synthesized I kappaB alpha\|Chronic Ser 177/181 phosphorylation of IKKβ was due to UVB-induced inhibition of the catalytic subunit of the Ser-Thr phosphatase PP2A (PP2Ac)

Identifier	Residue	Sequence	Organism
SIGNOR-248580	Ser181	DQGSLCTsFVGTLQY	Homo sapiens
pmid	sentence
19607706	Permanent activation of the upstream kinase IKK beta results from UVB-induced inhibition of the catalytic subunit of Ser-Thr phosphatase PP2A (PP2Ac), leading to immediate phosphorylation and degradation of newly synthesized I kappaB alpha\|Chronic Ser 177/181 phosphorylation of IKKβ was due to UVB-induced inhibition of the catalytic subunit of the Ser-Thr phosphatase PP2A (PP2Ac)

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
SIGNOR-181663	Ser177	AKELDQGsLCTSFVG	Homo sapiens
pmid	sentence
18930133	Using a functional genomic approach, we have identified two protein serine/threonine phosphatases, ppm1a and ppm1b, as ikkbeta phosphatases. Overexpression of ppm1a or ppm1b results in dephosphorylation of ikkbeta at ser177 and ser181 and termination of ikkbeta-induced nf-kappab activation

Identifier	Residue	Sequence	Organism
SIGNOR-181667	Ser181	DQGSLCTsFVGTLQY	Homo sapiens
pmid	sentence
18930133	Using a functional genomic approach, we have identified two protein serine/threonine phosphatases, ppm1a and ppm1b, as ikkbeta phosphatases. Overexpression of ppm1a or ppm1b results in dephosphorylation of ikkbeta at ser177 and ser181 and termination of ikkbeta-induced nf-kappab activation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248486	Ser177	AKELDQGsLCTSFVG	Homo sapiens
pmid	sentence
18930133	PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation\|Overexpression of PPM1A or PPM1B results in dephosphorylation of IKKbeta at Ser177 and Ser181 and termination of IKKbeta-induced NF-kappaB activation.

Identifier	Residue	Sequence	Organism
SIGNOR-248487	Ser181	DQGSLCTsFVGTLQY	Homo sapiens
pmid	sentence
18930133	PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation\|Overexpression of PPM1A or PPM1B results in dephosphorylation of IKKbeta at Ser177 and Ser181 and termination of IKKbeta-induced NF-kappaB activation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181655	Ser177	AKELDQGsLCTSFVG	Homo sapiens
pmid	sentence
18930133	Using a functional genomic approach, we have identified two protein serine/threonine phosphatases, ppm1a and ppm1b, as ikkbeta phosphatases. Overexpression of ppm1a or ppm1b results in dephosphorylation of ikkbeta at ser177 and ser181 and termination of ikkbeta-induced nf-kappab activation

Identifier	Residue	Sequence	Organism
SIGNOR-181659	Ser181	DQGSLCTsFVGTLQY	Homo sapiens
pmid	sentence
18930133	Using a functional genomic approach, we have identified two protein serine/threonine phosphatases, ppm1a and ppm1b, as ikkbeta phosphatases. Overexpression of ppm1a or ppm1b results in dephosphorylation of ikkbeta at ser177 and ser181 and termination of ikkbeta-induced nf-kappab activation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248343	Ser177	AKELDQGsLCTSFVG	Homo sapiens
pmid	sentence
18930133	PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation\|Overexpression of PPM1A or PPM1B results in dephosphorylation of IKKbeta at Ser177 and Ser181 and termination of IKKbeta-induced NF-kappaB activation.

Identifier	Residue	Sequence	Organism
SIGNOR-248344	Ser181	DQGSLCTsFVGTLQY	Homo sapiens
pmid	sentence
18930133	PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation\|Overexpression of PPM1A or PPM1B results in dephosphorylation of IKKbeta at Ser177 and Ser181 and termination of IKKbeta-induced NF-kappaB activation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249015	Ser177	AKELDQGsLCTSFVG	Homo sapiens
pmid	sentence
10022904	Activation of IkappaB kinase beta by protein kinase C isoforms. \| Interestingly, recombinant active zetaPKC and alphaPKC are able to stimulate in vitro the activity of IKKbeta but not that of IKKalpha. In addition, evidence is presented here that recombinant zetaPKC directly phosphorylates IKKbeta in vitro, involving Ser177 and Ser181. Collectively, these results demonstrate a critical role for the PKC isoforms in the NF-kappaB pathway at the level of IKKbeta activation and IkappaB degradation.

Identifier	Residue	Sequence	Organism
SIGNOR-249016	Ser181	DQGSLCTsFVGTLQY	Homo sapiens
pmid	sentence
10022904	Activation of IkappaB kinase beta by protein kinase C isoforms. \| Interestingly, recombinant active zetaPKC and alphaPKC are able to stimulate in vitro the activity of IKKbeta but not that of IKKalpha. In addition, evidence is presented here that recombinant zetaPKC directly phosphorylates IKKbeta in vitro, involving Ser177 and Ser181. Collectively, these results demonstrate a critical role for the PKC isoforms in the NF-kappaB pathway at the level of IKKbeta activation and IkappaB degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-174401	Ser177	AKELDQGsLCTSFVG	Homo sapiens
pmid	sentence
21673972	These results demonstrate that the ikk is a direct substrate of ampk_2 and that its phosphorylation on ser177 and ser181no initiates the activation of the ampk_2 in endothelial cells which in turn phosphorylates and activates the _-subunit of the ikk. The latter also induces a higher rate of ikk auto-inactivation and thus attenuates the activation of nf_b and the expression of inflammatory genes

Identifier	Residue	Sequence	Organism
SIGNOR-174405	Ser181	DQGSLCTsFVGTLQY	Homo sapiens
pmid	sentence
21673972	These results demonstrate that the ikk is a direct substrate of ampk_2 and that its phosphorylation on ser177 and ser181no initiates the activation of the ampk_2 in endothelial cells which in turn phosphorylates and activates the _-subunit of the ikk. The latter also induces a higher rate of ikk auto-inactivation and thus attenuates the activation of nf_b and the expression of inflammatory genes

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275518	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
SIGNOR-275519	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273642	Ser220	GKDQRGQsIYSTSFP	Homo sapiens	HEK-293 Cell
pmid	sentence
32978258	Manipulating the IκB kinase β activity coupled with in vivo and in vitro kinase assays demonstrated that IκB kinase β is a key serine/threonine kinase activated by autophagy stimuli and that it catalyzes phosphorylation of IGPR-1 at Ser220 The subsequent activation of IGPR-1, in turn, stimulates phosphorylation of AMP-activated protein kinase, which leads to phosphorylation of the major pro-autophagy proteins ULK1 and Beclin-1 (BECN1), increased LC3-II levels, and accumulation of LC3 punctum.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251288	Ser268	SDEFRPRsKSQSSSN	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251289	Ser270	EFRPRSKsQSSSNCS	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251290	Ser272	RPRSKSQsSSNCSNP	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251291	Ser274	RSKSQSSsNCSNPIS	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251292	Ser307	TRRSRTEsITATSPA	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251293	Ser312	TESITATsPASMVGG	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251294	Ser341	GTMSRPAsVDGSPVS	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251295	Ser345	RPASVDGsPVSPSTN	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251296	Ser527	RFRKRTHsAGTSPTI	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251297	Ser531	RTHSAGTsPTITHQK	in vitro
pmid	sentence
12351658	IRS-1 is a novel direct substrate for IKK and that phosphorylation of IRS-1 at Ser(312) (and other sites) by IKK may contribute to the insulin resistance mediated by activation of inflammatory pathways.

Publications:

10

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-277278	Ser269	QGRIGGDsGLSSRGK	in vitro
pmid	sentence
27585591	IKKβ promotes metabolic adaptation to glutamine deprivation via phosphorylation and inhibition of PFKFB3.We demonstrate that IKKβ directly interacts with and phosphorylates 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase isoform 3 (PFKFB3), a major driver of aerobic glycolysis, at Ser269 upon glutamine deprivation to inhibit its activity, thereby down-regulating aerobic glycolysis when glutamine levels are low.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251285	Ser31	QDVLGEEsPLGKPAM	Homo sapiens
pmid	sentence
12657630	IKKbeta phosphorylates human IKKgamma at Ser-31, Ser-43, and Ser-376. IKK≈í‚â§ mediates IKK≈í‚â• phosphorylation under physiologic signaling conditions. IKK≈í‚â• is chronically phosphorylated in cells expressing the HTLV1 Tax oncoprotein, which interfaces directly with the I≈í‚à´B kinase complex.both Tax and TNF induce phosphorylation of human IKK≈í‚â• at Ser-31, Ser-43, and Ser-376.

Identifier	Residue	Sequence	Organism
SIGNOR-251286	Ser376	PPAPAYLsSPLALPS	Homo sapiens
pmid	sentence
12657630	IKKbeta phosphorylates human IKKgamma at Ser-31, Ser-43, and Ser-376. IKK≈í‚â§ mediates IKK≈í‚â• phosphorylation under physiologic signaling conditions. IKK≈í‚â• is chronically phosphorylated in cells expressing the HTLV1 Tax oncoprotein, which interfaces directly with the I≈í‚à´B kinase complex.both Tax and TNF induce phosphorylation of human IKK≈í‚â• at Ser-31, Ser-43, and Ser-376.

Identifier	Residue	Sequence	Organism
SIGNOR-158655	Ser43	PAMLHLPsEQGAPET	Homo sapiens
pmid	sentence
17977820	In this study we analyze the ikkbeta-mediated phosphorylation of the ikk-binding domain of nemo. In vitro, ikkbeta phosphorylates three serine residues in the domain of nemo at positions 43, 68, and 85. However, mutational analysis revealed that only the phosphorylation of serine 68 in the center of the ikk-binding domain plays an essential role for the formation and the function of the ikk complex. Thus, ser(68) phosphorylation attenuates the amino-terminal dimerization of nemo as well as the ikkbeta-nemo interaction.

Identifier	Residue	Sequence	Organism
SIGNOR-251287	Ser43	PAMLHLPsEQGAPET	Homo sapiens
pmid	sentence
12657630	IKKbeta phosphorylates human IKKgamma at Ser-31, Ser-43, and Ser-376\|Thus far, we have no compelling evidence that inducible phosphorylation of these IKKgamma domains is important for their assigned functions.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272242	Ser31	RTIAAIRsFPHDNVE	Homo sapiens	HEK-293 Cell
pmid	sentence
31009856	We found that ASB8 was phosphorylated at the N-terminal Ser-31 by host IkappaB kinase beta (IKKbeta). In turn, ASB8 facilitated K48-linked ubiquitination and degradation of IKKbeta via the ubiquitin-proteasome pathway, resulting in remarkable inhibition of I-kappa-B-alpha (IkappaBalpha) and of p65 phosphorylation, consequently suppressing NF-kappaB activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-249365	Ser32	LLDDRHDsGLDSMKD
pmid	sentence
11815618	Nuclear factor-kappaB activation depends on phosphorylation and degradation of its inhibitor protein, IkapapB. The phosphorylation of I_Balpha on Ser32 and Ser36 is initiated by an IkapapB kinase (IKK) complex that includes a catalytic heterodimer composed of I_B kinase 1 (IKK-1) and IkapapB kinase 2 (IKK-2) as well as a regulatory adaptor subunit, NF-kappaB essential modulator.

Identifier	Residue	Sequence
SIGNOR-249366	Ser36	RHDSGLDsMKDEEYE
pmid	sentence
11815618	Nuclear factor-kappaB activation depends on phosphorylation and degradation of its inhibitor protein, IkapapB. The phosphorylation of I_Balpha on Ser32 and Ser36 is initiated by an IkapapB kinase (IKK) complex that includes a catalytic heterodimer composed of I_B kinase 1 (IKK-1) and IkapapB kinase 2 (IKK-2) as well as a regulatory adaptor subunit, NF-kappaB essential modulator.

Publications:

2

Pathways:

FLT3-ITD signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266436	Ser418	TTENRFHsLPFSLTK	Homo sapiens	JURKAT Cell
pmid	sentence
15870263	In response to cellular stimuli, CYLD undergoes rapid and transient phosphorylation, which is required for signal-induced TRAF2 ubiquitination and activation of downstream signaling events. Interestingly, the CYLD phosphorylation requires IkappaB kinase gamma (IKKgamma) and can be induced by IKK catalytic subunits.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-204716	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
SIGNOR-204724	Ser432	KMPNTNGsIGHSPLS	Homo sapiens
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
SIGNOR-204728	Ser436	TNGSIGHsPLSLSAQ	Homo sapiens
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-204732	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-204740	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:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-204720	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
SIGNOR-204736	Ser441	GHSPLSLsAQSVMEE	Homo sapiens
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

Identifier	Residue	Sequence	Organism
SIGNOR-131447	Ser439	EPGTATGsGIKSHNS	Homo sapiens
pmid	sentence
15574499	Ikkbeta phosphorylates dok1 s(439)s(443) and s(446)s(450) after tnf-alpha, il-1, or gamma-radiation. mutant dok1 a(439), a(443), a(446), and a(450) differed from wild-type dok1 in not inhibiting platelet-derived growth factor-induced extracellular signal-regulated kinase 1/2 phosphorylation or cell growth. Mutant dok1 a(439), a(443), a(446), and a(450) also did not promote cell motility whereas wild-type dok1 promoted cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-131451	Ser443	ATGSGIKsHNSALYS	Homo sapiens
pmid	sentence
15574499	Ikkbeta phosphorylates dok1 s(439)s(443) and s(446)s(450) after tnf-alpha, il-1, or gamma-radiation. mutant dok1 a(439), a(443), a(446), and a(450) differed from wild-type dok1 in not inhibiting platelet-derived growth factor-induced extracellular signal-regulated kinase 1/2 phosphorylation or cell growth. Mutant dok1 a(439), a(443), a(446), and a(450) also did not promote cell motility whereas wild-type dok1 promoted cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-131455	Ser446	SGIKSHNsALYSQVQ	Homo sapiens
pmid	sentence
15574499	Ikkbeta phosphorylates dok1 s(439)s(443) and s(446)s(450) after tnf-alpha, il-1, or gamma-radiation. mutant dok1 a(439), a(443), a(446), and a(450) differed from wild-type dok1 in not inhibiting platelet-derived growth factor-induced extracellular signal-regulated kinase 1/2 phosphorylation or cell growth. Mutant dok1 a(439), a(443), a(446), and a(450) also did not promote cell motility whereas wild-type dok1 promoted cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-131556	Ser450	SHNSALYsQVQKSGA	Homo sapiens
pmid	sentence
15574499	Ikkbeta phosphorylates dok1 s(439)s(443) and s(446)s(450) after tnf-alpha, il-1, or gamma-radiation. mutant dok1 a(439), a(443), a(446), and a(450) differed from wild-type dok1 in not inhibiting platelet-derived growth factor-induced extracellular signal-regulated kinase 1/2 phosphorylation or cell growth. Mutant dok1 a(439), a(443), a(446), and a(450) also did not promote cell motility whereas wild-type dok1 promoted cell motility.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-138903	Ser468	AVFTDLAsVDNSEFQ	Homo sapiens	Breast Cancer Cell, T-lymphocyte
pmid	sentence
16046471	Rela is phosphorylated at ser536 by ikkbeta, ikkalfa, ikkepsilon, nf-kb activating kinase (nak, also known as tank-binding kinase-1 tbk1) and rsk1 (also known as p90 ribosomal protein s6 kinase (p90s6k). We now present evidence that suggests that the upstream kinase ikkbeta plays an important role in tax-induced p53 inhibition through phosphorylation of p65/rela at ser-536. Ikkbeta plays an important role in tax-induced p53 inhibition through phosphorylation of p65/rela at ser-536.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-129935	Ser536	SGDEDFSsIADMDFS	Homo sapiens	HEK-293 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.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-157296	Ser487	AAISRELsEITTAEA	Homo sapiens	Breast Cancer Cell
pmid	sentence
17693255	Here we show that ikkbeta, a major downstream kinase in the tnfalpha signaling pathway, physically interacts with and phosphorylates tsc1 at ser487 and ser511, resulting in suppression of tsc1phosphorylation of tsc2 (by akt and erk;refs. 28, 29) and tsc1(by ikkbeta;ref. 30) results in the disruption of the tsc1/2 complex, and thereby activates the oncogenic mtor signaling contributing to tumor progression.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-183688	Ser487	AAISRELsEITTAEA	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Here we show that ikkbeta, a major downstream kinase in the tnfalpha signaling pathway, physically interacts with and phosphorylates tsc1 at ser487 and ser511, resulting in suppression of tsc1phosphorylation of tsc2 (by akt and erk;refs. 28, 29) and tsc1(by ikkbeta;ref. 30) results in the disruption of the tsc1/2 complex, and thereby activates the oncogenic mtor signaling contributing to tumor progression.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-183692	Ser511	DSPFYRDsLPGSQRK	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Here we show that ikkbeta, a major downstream kinase in the tnfalpha signaling pathway, physically interacts with and phosphorylates tsc1 at ser487 and ser511, resulting in suppression of tsc1phosphorylation of tsc2 (by akt and erk;refs. 28, 29) and tsc1(by ikkbeta;ref. 30) results in the disruption of the tsc1/2 complex, and thereby activates the oncogenic mtor signaling contributing to tumor progression.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-157300	Ser511	DSPFYRDsLPGSQRK	Homo sapiens	Breast Cancer Cell
pmid	sentence
17693255	Here we show that ikkbeta, a major downstream kinase in the tnfalpha signaling pathway, physically interacts with and phosphorylates tsc1 at ser487 and ser511, resulting in suppression of tsc1phosphorylation of tsc2 (by akt and erk;refs. 28, 29) and tsc1(by ikkbeta;ref. 30) results in the disruption of the tsc1/2 complex, and thereby activates the oncogenic mtor signaling contributing to tumor progression.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-183684	Ser644	GLDFNFDsLISTQNV	Homo sapiens
pmid	sentence
19188143	Ikkbeta phosphorylates foxo3a at ser644. Ikappab kinase (ikk) physically interacts with, phosphorylates, and inhibits foxo3a independent of akt and causes proteolysis of foxo3a via the ub-dependent proteasome pathway

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124207	Ser644	GLDFNFDsLISTQNV	Homo sapiens	Breast Cancer Cell
pmid	sentence
15084260	Ikkbeta phosphorylates foxo3a at ser644. Ikappab kinase (ikk) physically interacts with, phosphorylates, and inhibits foxo3a independent of akt and causes proteolysis of foxo3a via the ub-dependent proteasome pathway

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252947	Ser644	GLDFNFDsLISTQNV	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Ikkbeta phosphorylates foxo3a at ser644. Ikappab kinase (ikk) physically interacts with, phosphorylates, and inhibits foxo3a independent of akt and causes proteolysis of foxo3a via the ub-dependent proteasome pathway

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252948	Ser644	GLDFNFDsLISTQNV	Homo sapiens	Breast Cancer Cell
pmid	sentence
15084260	Ikkbeta phosphorylates foxo3a at ser644. Ikappab kinase (ikk) physically interacts with, phosphorylates, and inhibits foxo3a independent of akt and causes proteolysis of foxo3a via the ub-dependent proteasome pathway

Publications:

2

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251274	Ser670	SKVRGPVsGSPDSMN	Homo sapiens	HEK-293 Cell
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251275	Ser672	VRGPVSGsPDSMNAS	Homo sapiens	HEK-293 Cell
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251276	Ser675	PVSGSPDsMNASRLS	Homo sapiens	HEK-293 Cell
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251277	Ser679	SPDSMNAsRLSQPGQ	Homo sapiens	HEK-293 Cell
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251278	Ser682	SMNASRLsQPGQLMS	Homo sapiens	HEK-293 Cell
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism
SIGNOR-251279	Ser689	SQPGQLMsQPSTASN	Homo sapiens
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism
SIGNOR-251280	Ser692	GQLMSQPsTASNSLP	Homo sapiens
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism
SIGNOR-251281	Ser695	MSQPSTAsNSLPEPA	Homo sapiens
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism
SIGNOR-251282	Ser697	QPSTASNsLPEPAKK	Homo sapiens
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism
SIGNOR-251283	Ser705	LPEPAKKsEELVAEA	Homo sapiens
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Identifier	Residue	Sequence	Organism
SIGNOR-66344	Ser733	TVREQDQsFTALDWS	Homo sapiens
pmid	sentence
10195894	Once activated, ikkbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased ikk activity and may prevent prolonged activation of the inflammatory response

Identifier	Residue	Sequence	Organism
SIGNOR-236048	Ser740	SFTALDWsWLQTEEE	Homo sapiens
pmid	sentence
10195894	Once activated, ikkbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased ikk activity and may prevent prolonged activation of the inflammatory response

Identifier	Residue	Sequence	Organism
SIGNOR-66352	Ser750	QTEEEEHsCLEQAS	Homo sapiens
pmid	sentence
10195894	Once activated, ikkbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased ikk activity and may prevent prolonged activation of the inflammatory response

Identifier	Residue	Sequence	Organism
SIGNOR-251284	Ser756	HSCLEQAs	Homo sapiens
pmid	sentence
10195894	Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.

Publications:

14

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling

Identifier	Residue	Sequence	Organism
SIGNOR-158659	Ser68	LRDAIRQsNQILRER	Homo sapiens
pmid	sentence
17977820	In this study we analyze the ikkbeta-mediated phosphorylation of the ikk-binding domain of nemo. In vitro, ikkbeta phosphorylates three serine residues in the domain of nemo at positions 43, 68, and 85. However, mutational analysis revealed that only the phosphorylation of serine 68 in the center of the ikk-binding domain plays an essential role for the formation and the function of the ikk complex. Thus, ser(68) phosphorylation attenuates the amino-terminal dimerization of nemo as well as the ikkbeta-nemo interaction. I

Identifier	Residue	Sequence	Organism
SIGNOR-158663	Ser85	ELLHFQAsQREEKEF	Homo sapiens
pmid	sentence
17977820	In this study we analyze the ikkbeta-mediated phosphorylation of the ikk-binding domain of nemo. In vitro, ikkbeta phosphorylates three serine residues in the domain of nemo at positions 43, 68, and 85. However, mutational analysis revealed that only the phosphorylation of serine 68 in the center of the ikk-binding domain plays an essential role for the formation and the function of the ikk complex. Thus, ser(68) phosphorylation attenuates the amino-terminal dimerization of nemo as well as the ikkbeta-nemo interaction. I

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181798	Ser733	TVREQDQsFTALDWS	Homo sapiens
pmid	sentence
18957422	Plk1 phosphorylates serines 733, 740, and 750 in the gammabd of ikkbeta in vitro. Phosphorylating gammabd with plk1 decreased its affinity for ikkgamma

Identifier	Residue	Sequence	Organism
SIGNOR-181802	Ser740	SFTALDWsWLQTEEE	Homo sapiens
pmid	sentence
18957422	Plk1 phosphorylates serines 733, 740, and 750 in the gammabd of ikkbeta in vitro. Phosphorylating gammabd with plk1 decreased its affinity for ikkgamma

Identifier	Residue	Sequence	Organism
SIGNOR-181806	Ser750	QTEEEEHsCLEQAS	Homo sapiens
pmid	sentence
18957422	Plk1 phosphorylates serines 733, 740, and 750 in the gammabd of ikkbeta in vitro. Phosphorylating gammabd with plk1 decreased its affinity for ikkgamma

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163801	Ser8	MEPAAGSsMEPSADW	Homo sapiens
pmid	sentence
20152798	Ikkbeta specifically binds to p16 and phosphorylates ser8 of p16 phosphorylation at ser8 of p16 brings about a significant loss of its cyclin-dependent kinase (cdk) 4-inhibitory activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-70465	Ser923	DELRDSDsVCDSGVE	Homo sapiens	Fibrosarcoma Cell
pmid	sentence
10469655	Ikkbeta phosphorylates p105 resulting in its degradation, which releases tpl2 resulting in activation of the pro-proliferative map kinase- pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-70469	Ser927	DSDSVCDsGVETSFR	Homo sapiens	Fibrosarcoma Cell
pmid	sentence
10469655	Ikkbeta phosphorylates p105 resulting in its degradation, which releases tpl2 resulting in activation of the pro-proliferative map kinase- pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-70473	Ser932	CDSGVETsFRKLSFT	Homo sapiens	Fibrosarcoma Cell
pmid	sentence
10469655	Ikkbeta phosphorylates p105 resulting in its degradation, which releases tpl2 resulting in activation of the pro-proliferative map kinase- pathway.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104803	Ser923	DELRDSDsVCDSGVE	Homo sapiens	HEK-293 Cell
pmid	sentence
11158290	Ikkbeta phosphorylates p105 resulting in its degradation, which releases tpl2 resulting in activation of the pro-proliferative map kinase- pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104807	Ser927	DSDSVCDsGVETSFR	Homo sapiens	HEK-293 Cell
pmid	sentence
11158290	Ikkbeta phosphorylates p105 resulting in its degradation, which releases tpl2 resulting in activation of the pro-proliferative map kinase- pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104811	Ser932	CDSGVETsFRKLSFT	Homo sapiens	HEK-293 Cell
pmid	sentence
11158290	Ikkbeta phosphorylates p105 resulting in its degradation, which releases tpl2 resulting in activation of the pro-proliferative map kinase- pathway.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-100784	Tyr188	SFVGTLQyLAPELLE	Homo sapiens
pmid	sentence
12707358	These results indicate that c-src can associate with ikkbeta and phosphorylate its tyrosine residues after tnf-alfa or tpa stimulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-99314	Tyr188	SFVGTLQyLAPELLE	Homo sapiens
pmid	sentence
12645577	These results indicate that c-src can associate with ikkbeta and phosphorylate its tyrosine residues after tnf-alfa or tpa stimulation.

Identifier	Residue	Sequence	Organism
SIGNOR-99318	Tyr199	ELLEQQKyTVTVDYW	Homo sapiens
pmid	sentence
12645577	These results indicate that c-src can associate with ikkbeta and phosphorylate its tyrosine residues after tnf-alfa or tpa stimulation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-217376		Homo sapiens
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	Organism
SIGNOR-217427		Homo sapiens
pmid	sentence
16046471	Rela is phosphorylated at ser536 by ikkbeta, ikkalfa, ikkepsilon, nf-kb activating kinase (nak, also known as tank-binding kinase-1 tbk1) and rsk1 (also known as p90 ribosomal protein s6 kinase (p90s6k) .we now present evidence that suggests that the upstream kinase ikkbeta plays an important role in tax-induced p53 inhibition through phosphorylation of p65/rela at ser-536. .Ikkbeta Plays an important role in tax-induced p53 inhibition through phosphorylation of p65/rela at ser-536. .

Publications:

2

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-164512		Homo sapiens
pmid	sentence
20300203	The n-terminal domain of ikkgamma is required both for the binding of ikkalfa and ikkbeta and their assembly into a high-molecular-weight complex essential for activation

Identifier	Residue	Organism
SIGNOR-91705		Homo sapiens
pmid	sentence
12192055	The n-terminal domain of ikkgamma is required both for the binding of ikkalfa and ikkbeta and their assembly into a high-molecular-weight complex essential for activation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258249		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

Identifier	Residue	Organism	Cell Line
SIGNOR-235400		Mus musculus	MEF Cell, Macrophage
pmid	sentence
21232017	Tak1 become activated and then phosphorilates and activates ikk2 which in turn now phosphorylates ikba, marking it for k48-ubiquitination and proteasomal degradation

Publications:

1

Organism:

Mus Musculus

Pathways:

FLT3-ITD signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-269673		Homo sapiens	HEK-293 Cell
pmid	sentence
15951441	We demonstrated by immunohistochemistry that NIBP expression in the brain is localized to neurons. NIBP physically interacts with NIK, IKK(beta), but not IKK(alpha) or IKK(gamma). NIBP overexpression potentiates tumor necrosis factor-alpha-induced NF-kappaB activation through increased phosphorylation of the IKK complex and its downstream I(kappa)B(alpha) and p65 substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-272253		Homo sapiens	HEK-293 Cell
pmid	sentence
31009856	In turn, ASB8 facilitated K48-linked ubiquitination and degradation of IKKbeta via the ubiquitin-proteasome pathway, resulting in remarkable inhibition of I-kappa-B-alpha (IkappaBalpha) and of p65 phosphorylation, consequently suppressing NF-kappaB activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258190		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

Identifier	Residue	Organism	Cell Line
SIGNOR-251298		Homo sapiens	HeLa Cell
pmid	sentence
11971985	We demonstrated the in vitro phosphorylation of SRC-3 by the two catalytic subunits of the IKK complex, IKKα and IKKβ. IKK kinase activity is required for synergistic activation with SRC-3

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-192614		Homo sapiens
pmid	sentence
23332762	Ikk phosphorylates bad at serine-26 (ser26) and primes it for inactivation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-251965		Homo sapiens	Astrocytoma Cell
pmid	sentence
19291302	TNFα-dependent COMT downregulation was indeed mediated by the NF-κB pathway. Transient expression of p65, the essential component of NF-κB complexes, or IKKβ, the major positive regulator of NF-κB activition, significantly decreased P2-COMT reporter expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-255089		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

Identifier	Residue	Organism
SIGNOR-55949		Homo sapiens
pmid	sentence
9520446	Activation of the transcription factor nf-kappab by inflammatory cytokines involves the successive action of nf-kappab-inducing kinase (nik) and two ikappab kinases, ikk-alpha and ikk-beta. Here we show that nik preferentially phosphorylates ikk-alpha over ikk-beta

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-121576		Homo sapiens
pmid	sentence
14743216	A physical and functional map of the human tnf-alpha/nf-kappa b signal transduction pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-217403		Homo sapiens
pmid	sentence
11158290	Ikkbeta phosphorylates p105 resulting in its degradation, which releases tpl2 resulting in activation of the pro-proliferative map kinase- pathway.

Identifier	Residue	Organism
SIGNOR-217400		Homo sapiens
pmid	sentence
10469655	Ikkbeta phosphorylates p105 resulting in its degradation, which releases tpl2 resulting in activation of the pro-proliferative map kinase- pathway.

Publications:

2

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-272544		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

Identifier	Residue	Organism
SIGNOR-253585		Homo sapiens
pmid	sentence
22056382	Tnf-α enhanced the transcriptional activity of a classical Notch target gene via Ikk2 by inducing histone H3 phosphorylation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-164509		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:

FLT3-ITD signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-271431		Homo sapiens	LNCaP Cell
pmid	sentence
20068069	CLU-2 is a ubiquitin binding protein (UBP) that enhances proteasome activity. sCLU promotes degradation of COMMD1. sCLU interacts with the SCF-βTrCP E3 ligase complex, serving as a scaffolding chaperone to form a multimeric protein complex that facilitates COMMD1 and I-κB ubiquitination and proteasomal degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-271433		Homo sapiens	LNCaP Cell
pmid	sentence
20068069	CLU-2 is a ubiquitin binding protein (UBP) that enhances proteasome activity. sCLU promotes degradation of COMMD1. sCLU interacts with the SCF-βTrCP E3 ligase complex, serving as a scaffolding chaperone to form a multimeric protein complex that facilitates COMMD1 and I-κB ubiquitination and proteasomal degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-272547		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

Identifier	Residue	Organism	Cell Line
SIGNOR-273646		Homo sapiens	HEK-293 Cell
pmid	sentence
29180417	IFNγ induced JAK1-mediated phosphorylation of SNX8 at Tyr95 and Tyr126, which promoted the recruitment of IKKβ to the JAK1 complex.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-52932		Homo sapiens
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:

1

Organism:

Homo Sapiens

Name	IKBKB View Modifications
Full Name	Inhibitor of nuclear factor kappa-B kinase subunit beta
Synonyms	I-kappa-B-kinase beta, IKK-B, IKK-beta, IkBKB, I-kappa-B kinase 2, IKK2, Nuclear factor NF-kappa-B inhibitor kinase beta, NFKBIKB \| IKKB
Primary ID	O14920
Links	- -
Type	protein
Relations	132
Pathways	FLT3-ITD signaling
Inhibitors	N-(6-Chloro-7-methoxy-9H-pyrido[3,4-b]indol-8-yl)-2-methylnicotinamide; N'-(1,8-dimethyl-4-imidazo[1,2-a]quinoxalinyl)ethane-1,2-diamine
Function	Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:30337470). Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation. Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:20410276). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NCOA3, BCL10 and IRS1 (PubMed:17213322). Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation (PubMed:11297557). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418).

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