+ |
CAMK2A | up-regulates activity
phosphorylation
|
CYLD |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266434 |
Ser362 |
FYTLNGSsVDSQPQS |
Homo sapiens |
E-18 Rat Primary Hippocampal Neuron |
pmid |
sentence |
24614225 |
NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy, […] Purified CaMKII phosphorylates CYLD on at least three residues (S-362, S-418, and S-772 on the human CYLD protein Q9NQC7-1) and promotes its deubiquitinase activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266442 |
Ser362 |
FYTLNGSsVDSQPQS |
Homo sapiens |
E-18 Rat Primary Hippocampal Neuron |
pmid |
sentence |
24614225 |
NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy, […] Purified CaMKII phosphorylates CYLD on at least three residues (S-362, S-418, and S-772 on the human CYLD protein Q9NQC7-1) and promotes its deubiquitinase activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266433 |
Ser772 |
LFKKIFPsLELNITD |
Homo sapiens |
E-18 Rat Primary Hippocampal Neuron |
pmid |
sentence |
24614225 |
NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy, […] Purified CaMKII phosphorylates CYLD on at least three residues (S-362, S-418, and S-772 on the human CYLD protein Q9NQC7-1) and promotes its deubiquitinase activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266441 |
Ser772 |
LFKKIFPsLELNITD |
Homo sapiens |
E-18 Rat Primary Hippocampal Neuron |
pmid |
sentence |
24614225 |
NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy, […] Purified CaMKII phosphorylates CYLD on at least three residues (S-362, S-418, and S-772 on the human CYLD protein Q9NQC7-1) and promotes its deubiquitinase activity. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
CAMK2B | up-regulates
phosphorylation
|
CYLD |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-25334 |
Ser362 |
FYTLNGSsVDSQPQS |
Homo sapiens |
|
pmid |
sentence |
24614225 |
Purified camkii phosphorylates cyld on at least three residues (s-362, s-418, and s-772 on the human cyld protein q9nqc7-1) and promotes its deubiquitinase activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-91403 |
Ser772 |
LFKKIFPsLELNITD |
Homo sapiens |
|
pmid |
sentence |
24614225 |
Purified camkii phosphorylates cyld on at least three residues (s-362, s-418, and s-772 on the human cyld protein q9nqc7-1) and promotes its deubiquitinase activity. |
|
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 |
+ |
IKBKB | down-regulates activity
phosphorylation
|
CYLD |
0.529 |
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 |
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-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 |
Cell Line |
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 |
+ |
IKK-complex | down-regulates activity
phosphorylation
|
CYLD |
0.615 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266435 |
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. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | NF-KB Canonical |
+ |
CAMK2B | up-regulates activity
phosphorylation
|
CYLD |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-25329 |
Ser418 |
TTENRFHsLPFSLTK |
Homo sapiens |
|
pmid |
sentence |
24614225 |
Purified camkii phosphorylates cyld on at least three residues (s-362, s-418, and s-772 on the human cyld protein q9nqc7-1) and promotes its deubiquitinase activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IKBKB | up-regulates activity
phosphorylation
|
CYLD |
0.529 |
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 |
Cell Line |
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 |
+ |
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 |
+ |
TRIM47 | down-regulates quantity
ubiquitination
|
CYLD |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266443 |
|
|
Mus musculus |
Hepatocyte |
pmid |
sentence |
29291351 |
CYLD is progressively degraded upon interaction with the E3 ligase TRIM47 in proportion to NASH severity |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
CYLD | down-regulates activity
deubiquitination
|
TRAF2 |
0.663 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-117860 |
|
|
Homo sapiens |
|
pmid |
sentence |
12917691 |
Cyld also interacts directly with tumour-necrosis factor receptor (tnfr)-associated factor 2 (traf2), an adaptor molecule involved in by members of the family of tnf/nerve growth factor receptors. (articolo-abstract) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | NF-KB Canonical |
+ |
CYLD | up-regulates
|
CCND1 |
0.401 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146777 |
|
|
Homo sapiens |
Skin Cancer Cell |
pmid |
sentence |
16713561 |
Cyld was also recently shown to deubiquitylate the p50 and p52 co-activator bcl-3, leading to both cyclin d1 expression and proliferation in keratinocytes |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CYLD | down-regulates
deubiquitination
|
TRAF6 |
0.781 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-117856 |
|
|
Homo sapiens |
|
pmid |
sentence |
12917689 |
The nf-kappab activation by cyld is mediated, at least in part, by the deubiquitination and inactivation of tnfr-associated factor 2 (traf2) and, to a lesser extent, traf6. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
Pathways: | NF-KB Canonical |
+ |
CYLD | down-regulates
deubiquitination
|
BCL3 |
0.527 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146774 |
|
|
Homo sapiens |
Skin Cancer Cell |
pmid |
sentence |
16713561 |
Cyld binds and deubiquitinates bcl-3in cyld+/+ keratinocytes, tpa or uv light triggers the translocation of cyld from the cytoplasm to the perinuclear region, where cyld binds and deubiquitinates bcl-3, thereby preventing nuclear accumulation of bcl-3 and p50/bcl-3- or p52/bcl-3-dependent proliferation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CYLD | up-regulates activity
deubiquitination
|
MAP3K7 |
0.62 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266437 |
|
|
Mus musculus |
|
pmid |
sentence |
29291351 |
Mechanistically, CYLD interacts directly with the kinase TAK1 and removes its K63-linked polyubiquitin chain, which blocks downstream activation of the JNK-p38 cascades. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | NF-KB Canonical |