| + |
IKBKB |
phosphorylation
|
IKBKG |
0.962 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251285 |
Ser31 |
QDVLGEEsPLGKPAM |
Homo sapiens |
|
| pmid |
sentence |
| 12657630 |
IKKbeta phosphorylates human IKKgamma at Ser-31, Ser-43, and Ser-376. IKKβ mediates IKKγ phosphorylation under physiologic signaling conditions. IKKγ is chronically phosphorylated in cells expressing the HTLV1 Tax oncoprotein, which interfaces directly with the IκB kinase complex.both Tax and TNF induce phosphorylation of human IKKγ at Ser-31, Ser-43, and Ser-376. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251286 |
Ser376 |
PPAPAYLsSPLALPS |
Homo sapiens |
|
| pmid |
sentence |
| 12657630 |
IKKbeta phosphorylates human IKKgamma at Ser-31, Ser-43, and Ser-376. IKKβ mediates IKKγ phosphorylation under physiologic signaling conditions. IKKγ is chronically phosphorylated in cells expressing the HTLV1 Tax oncoprotein, which interfaces directly with the IκB kinase complex.both Tax and TNF induce phosphorylation of human IKKγ at Ser-31, Ser-43, and Ser-376. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
Cell Line |
| 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 |
| + |
IKK-complex |
phosphorylation
|
IKBKG |
0.928 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209792 |
Ser376 |
PPAPAYLsSPLALPS |
Homo sapiens |
|
| pmid |
sentence |
| 12657630 |
Phosphopeptide-mapping experiments with metabolically radiolabeled cells indicate that ikkbeta phosphorylates human ikkgamma at ser-31, ser-43, and ser-376 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216403 |
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. I |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, IL1 Signaling , Inhibition of Apoptosis, NF-KB Canonical, Toll like receptors |
| + |
PRKDC | down-regulates activity 
phosphorylation
|
IKBKG |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277508 |
Ser43 |
PAMLHLPsEQGAPET |
in vitro |
|
| pmid |
sentence |
| 31932854 |
Here, we show that DNA-dependent protein kinase (DNA-PK), an enzyme involved in DNA double-strand break (DSB) repair, triggers the phosphorylation of NEMO by genotoxic stress, thereby enabling shuttling of NEMO through the nucleus with subsequent NF-κB activation. We identified serine 43 of NEMO as a DNA-PK phosphorylation site and point mutation of this serine to alanine led to a complete block of NF-κB activation by ionizing radiation (IR). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
IKBKG | up-regulates activity 
phosphorylation
|
RELA |
0.857 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129947 |
Ser536 |
SGDEDFSsIADMDFS |
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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IKBKB | down-regulates activity
phosphorylation
|
IKBKG |
0.962 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
Cell Line |
| 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 |
| + |
IKK-complex | down-regulates activity
phosphorylation
|
IKBKG |
0.928 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209788 |
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 |
Cell Line |
| SIGNOR-209784 |
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 |
| Pathways: | EBV infection, IL1 Signaling , Inhibition of Apoptosis, NF-KB Canonical, Toll like receptors |
| + |
ATM | down-regulates activity
phosphorylation
|
IKBKG |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144813 |
Ser85 |
ELLHFQAsQREEKEF |
Homo sapiens |
|
| pmid |
sentence |
| 16497931 |
Atm phosphorylates serine-85 of nemo to promote its ubiquitin-dependent nuclear export. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN | down-regulates activity
phosphorylation
|
IKBKG |
0.363 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276371 |
Tyr374 |
PLPPAPAyLSSPLAL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23131831 |
Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | down-regulates activity
phosphorylation
|
IKBKG |
0.426 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276370 |
Tyr374 |
PLPPAPAyLSSPLAL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23131831 |
Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | down-regulates activity
phosphorylation
|
IKBKG |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276369 |
Tyr374 |
PLPPAPAyLSSPLAL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23131831 |
Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
FGR | down-regulates activity
phosphorylation
|
IKBKG |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276368 |
Tyr374 |
PLPPAPAyLSSPLAL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23131831 |
Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL10 | up-regulates
binding
|
IKBKG |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18287044 |
Here, we show that bcl10 undergoes k63-linked polyubiquitination in response to t cell activation and subsequently binds nemo, the regulatory subunit of ikk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IKBKG | up-regulates
phosphorylation
|
NfKb-p65/p50 |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217382 |
|
|
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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, IL1 Signaling , Inhibition of Apoptosis, NF-KB Canonical, Toll like receptors |
| + |
IKBKG | up-regulates activity
binding
|
IKBKB |
0.962 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BPLF1 | down-regulates activity
deubiquitination
|
IKBKG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266743 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24586164 |
In the current study, we have found that BPLF1 interferes with innate immune activation by targeting multiple intermediates along the TLR signal transduction pathway, including TRAF6, NEMO, and IκBα. BPLF1 can remove ubiquitin tags from proteins in the TLR signaling cascade. This inhibits TLR signaling and decreases the expression of immune response genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
RIPK2 | up-regulates activity 
|
IKBKG |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252413 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16493424 |
In the case of NOD2, activation of RICK leads to K63 (Lys63)-linked polyubiquitylation of IKKgamma, the scaffold of the inhibitor of NF-kappaB (IkappaB)-kinase complex (the IKK complex), which also consists of IKKalpha and IKKbeta. This is followed by the phosphorylation of IKKbeta, as well as the phosphorylation of IkappaB and the release of nuclear factor-kappaB (NF-kappaB) for translocation to the nucleus. So, in activating the IKK complex, RICK either activates an E3 ubiquitin ligase that promotes K63-linked polyubiquitylation or inhibits an enzyme (such as cylindromatosis protein, CYLD) that de-ubiquitylates proteins that are modified with K63-linked polyubiquitin, so RICK does not require its own kinase activity for this function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IKBKG | form complex 
binding
|
IKK-complex |
0.928 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209762 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19666475 |
Proinflammatory NF-kappaB activation requires the IkappaB (inhibitor of NF-kappaB) kinase (IKK) complex that contains two catalytic subunits named IKKalpha and IKKbeta and a regulatory subunit named NF-kappaB essential modulator (NEMO). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217436 |
|
|
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: |
Mus Musculus, Homo Sapiens |
| Pathways: | EBV infection, IL1 Signaling , Inhibition of Apoptosis, NF-KB Canonical, Toll like receptors |
| + |
MAP3K7 | up-regulates activity
binding
|
IKBKG |
0.807 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162634 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20038579 |
This result suggests that ikkgamma/nemo binds to the polyubiquitinated tak1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, IL1 Signaling , Inhibition of Apoptosis, NF-KB Canonical, Toll like receptors |
| + |
RIPK1 | up-regulates activity
binding
|
IKBKG |
0.912 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145858 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16603398 |
Interestingly, polyubiquitinated rip1 recruits ikk through the binding between the polyubiquitin chains and nemo, a regulatory subunit of the ikk complex. Mutations of nemo that disrupt its polyubiquitin binding also abolish ikk activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Canonical |
| + |
RNF31 | up-regulates activity
polyubiquitination
|
IKBKG |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272052 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24469399 |
Involvement of Gln271 and Asp275 of NEMO in LUBAC-mediated linear polyubiquitination.vHOIP NZF1 also recognizes NEMO, and this recognition is involved in linear polyubiquitination of NEMO. Linear chains conjugated to NEMO are recognized by NEMO in trans on another IKK complex, thereby inducing multimerization of the IKK complex and trans autophosphorylation of IKK2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGLN3 | down-regulates activity
binding
|
IKBKG |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262005 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23732909 |
Here we report that EGLN3, but not EGLN1 or -2, interacts with and inhibits K63-linked ubiquitination of IKKγ. The effect appears to be related to inhibition of IKKγ ubiquitination mediated by cIAP1 rather than to stimulation of IKKγ deubiquitination by the deubiquitinases A20 and CYLD (cylindromatosis). EGLN3 does not affect the protein levels of cIAP1 or its E2 ubiquitin-conjugating enzymes UbcH5 and Ubc13. EGLN3 hydroxylase activity is not responsible for its effect on IKKγ ubiquitination and NF-κB signaling. Instead, interaction with IKKγ is required for the ability of EGLN3 to inhibit IKKγ ubiquitination and IKK-NF-κB signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUSC1 | up-regulates quantity by stabilization
|
IKBKG |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272775 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19365808 |
NESCA interacts with the IKK complex by the N-terminal region of NEMO. This experiment revealed that the overexpression of NESCA completely abolished the TRAF6-mediated polyubiquitination of NEMO, as it appears by using either anti-HA (Fig. 5A) or anti-NEMO (Fig. 5B) antibodies on immunoprecipitated extracts. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IKBKG | up-regulates activity
ubiquitination
|
BCL10 |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274149 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14695475 |
Here we show that Bcl10 targets NEMO for lysine-63-linked ubiquitination. Notably, a mutant form of NEMO that cannot be ubiquitinated inhibited Bcl10-induced NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
IKBKG
- 
- 