| + |
DYRK2 | down-regulates quantity by destabilization 
phosphorylation
|
CDC25A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276738 |
Ser107 |
NPMRRIHsLPQKLLG |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34363019 |
Here we describe a novel ubiquitin/proteasome-mediated pathway negatively regulating CDC25A stability, dependent on its phosphorylation by the serine/threonine kinase DYRK2. DYRK2 phosphorylates CDC25A on at least 7 residues, resulting in its degradation independent of the known CDC25A E3 ubiquitin ligases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276740 |
Ser156 |
KKPVRPVsRGCLHSH |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34363019 |
Here we describe a novel ubiquitin/proteasome-mediated pathway negatively regulating CDC25A stability, dependent on its phosphorylation by the serine/threonine kinase DYRK2. DYRK2 phosphorylates CDC25A on at least 7 residues, resulting in its degradation independent of the known CDC25A E3 ubiquitin ligases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276736 |
Ser18 |
RRLLFACsPPPASQP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34363019 |
Here we describe a novel ubiquitin/proteasome-mediated pathway negatively regulating CDC25A stability, dependent on its phosphorylation by the serine/threonine kinase DYRK2. DYRK2 phosphorylates CDC25A on at least 7 residues, resulting in its degradation independent of the known CDC25A E3 ubiquitin ligases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276739 |
Ser185 |
SAPARMLsSNERDSS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34363019 |
Here we describe a novel ubiquitin/proteasome-mediated pathway negatively regulating CDC25A stability, dependent on its phosphorylation by the serine/threonine kinase DYRK2. DYRK2 phosphorylates CDC25A on at least 7 residues, resulting in its degradation independent of the known CDC25A E3 ubiquitin ligases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276734 |
Ser320 |
HQSLSLAsSPKGTIE |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34363019 |
Here we describe a novel ubiquitin/proteasome-mediated pathway negatively regulating CDC25A stability, dependent on its phosphorylation by the serine/threonine kinase DYRK2. DYRK2 phosphorylates CDC25A on at least 7 residues, resulting in its degradation independent of the known CDC25A E3 ubiquitin ligases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276735 |
Ser321 |
QSLSLASsPKGTIEN |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34363019 |
Here we describe a novel ubiquitin/proteasome-mediated pathway negatively regulating CDC25A stability, dependent on its phosphorylation by the serine/threonine kinase DYRK2. DYRK2 phosphorylates CDC25A on at least 7 residues, resulting in its degradation independent of the known CDC25A E3 ubiquitin ligases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276737 |
Ser88 |
DSGFCLDsPGPLDSK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34363019 |
Here we describe a novel ubiquitin/proteasome-mediated pathway negatively regulating CDC25A stability, dependent on its phosphorylation by the serine/threonine kinase DYRK2. DYRK2 phosphorylates CDC25A on at least 7 residues, resulting in its degradation independent of the known CDC25A E3 ubiquitin ligases. |
|
| Publications: |
7 |
Organism: |
Homo Sapiens |
| + |
DYRK2 | down-regulates quantity by destabilization
phosphorylation
|
KATNA1 |
0.524 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262847 |
Ser109 |
VPVERRPsPGPRKRQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19287380 |
DYRK2 mediated phosphorylation is required for Katanin p60 degradation. Serine 42, serine 109 and threonine 133 are likely to be the major DYRK2 phosphorylation sites as single mutations for these sites showed reduced phosphorylation by DYRK2 and the triple mutant showed almost no DYRK2 mediated phosphorylation (Fig. 5d). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262848 |
Ser42 |
QMNKYLYsVKDTYLQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19287380 |
DYRK2 mediated phosphorylation is required for Katanin p60 degradation. Serine 42, serine 109 and threonine 133 are likely to be the major DYRK2 phosphorylation sites as single mutations for these sites showed reduced phosphorylation by DYRK2 and the triple mutant showed almost no DYRK2 mediated phosphorylation (Fig. 5d). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262849 |
Thr133 |
HGNRPSTtVRVHRSS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19287380 |
DYRK2 mediated phosphorylation is required for Katanin p60 degradation. Serine 42, serine 109 and threonine 133 are likely to be the major DYRK2 phosphorylation sites as single mutations for these sites showed reduced phosphorylation by DYRK2 and the triple mutant showed almost no DYRK2 mediated phosphorylation (Fig. 5d). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
DYRK2 | up-regulates 
phosphorylation
|
SIAH2 |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198721 |
Ser16 |
PSANKPCsKQPPPQP |
Homo sapiens |
|
| pmid |
sentence |
| 22878263 |
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198725 |
Ser28 |
PQPQHTPsPAAPPAA |
Homo sapiens |
|
| pmid |
sentence |
| 22878263 |
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198729 |
Ser68 |
GGGAGPVsPQHHELT |
Homo sapiens |
|
| pmid |
sentence |
| 22878263 |
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198733 |
Thr119 |
PTCRGALtPSIRNLA |
Homo sapiens |
|
| pmid |
sentence |
| 22878263 |
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198737 |
Thr26 |
PPPQPQHtPSPAAPP |
Homo sapiens |
|
| pmid |
sentence |
| 22878263 |
In the present study, we identify the serine/threonine kinase dyrk2 as siah2 interaction partner that phosphorylates siah2 at five residues (ser16, thr26, ser28, ser68, and thr119). accordingly, phosphorylated siah2 is more active than the wild-type e3 ligase and shows an increased ability to trigger the hif-1?-Mediated transcriptional response and angiogenesis. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
DYRK2 | down-regulates
phosphorylation
|
JUN |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195771 |
Ser243 |
PGETPPLsPIDMESQ |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 22307329 |
Degradation of c-jun/c-myc is a critical process for the g(1)/s transition, which is initiated upon phosphorylation by glycogen synthase kinase 3 ? (gsk3?). However, a specific kinase or kinases responsible for priming phosphorylation events that precede this gsk3? Modification has not been definitively identified. Here, we found that the dual-specificity tyrosine phosphorylation-regulated kinase dyrk2 functions as a priming kinase of c-jun and c-myc.The finding that kinase-active dyrk2 phosphorylated gst_c-jun210_310-wt by detection with an anti_phospho_c-jun(ser243) antibody demonstrated that dyrk2 is a ser243 kinase in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK2 |
phosphorylation
|
CARHSP1 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137474 |
Ser30 |
TPRSRERsPSPLRGN |
Homo sapiens |
|
| pmid |
sentence |
| 15910284 |
Dyrk2 (dual-specificity tyrosine-phosphorylated and -regulated protein kinase 2) phosphorylated crhsp24 at ser30, ser32 and ser41 in vitro, and ser41 was identified as a site phosphorylated in cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137478 |
Ser32 |
RSRERSPsPLRGNVV |
Homo sapiens |
|
| pmid |
sentence |
| 15910284 |
Dyrk2 (dual-specificity tyrosine-phosphorylated and -regulated protein kinase 2) phosphorylated crhsp24 at ser30, ser32 and ser41 in vitro, and ser41 was identified as a site phosphorylated in cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170781 |
Ser41 |
LRGNVVPsPLPTRRT |
Homo sapiens |
|
| pmid |
sentence |
| 21177848 |
Ser41 is known to be phosphorylated by a dyrk isoform in serum-fed or -starved cells (21). A phosphomimetic mutation of ser41 to asp resulted in complete loss of human crhsp-24 binding ability whether in the oxidative state or not |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
ATM | up-regulates quantity by stabilization
phosphorylation
|
DYRK2 |
0.538 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275577 |
Ser442 |
IELLGMPsQKLLDAS |
|
|
| pmid |
sentence |
| 19965871 |
ATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the apoptotic response to DNA damage|Upon exposure to genotoxic stress, ATM phosphorylates DYRK2 at Thr-33 and Ser-369, which enables DYRK2 to escape from degradation by dissociation from MDM2 and to induce the kinase activity toward p53 at Ser-46 in the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275576 |
Thr106 |
NKRTVLTtQPNGLTT |
|
|
| pmid |
sentence |
| 19965871 |
ATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the apoptotic response to DNA damage|Upon exposure to genotoxic stress, ATM phosphorylates DYRK2 at Thr-33 and Ser-369, which enables DYRK2 to escape from degradation by dissociation from MDM2 and to induce the kinase activity toward p53 at Ser-46 in the nucleus. |
|
| Publications: |
2 |
| + |
DYRK2 | up-regulates activity
phosphorylation
|
TP53 |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275578 |
Ser46 |
AMDDLMLsPDDIEQW |
|
|
| pmid |
sentence |
| 19965871 |
Phosphorylation of p53 at Ser-46 is indispensable for the commitment to apoptotic cell death. |Upon exposure to genotoxic stress, ATM phosphorylates DYRK2 at Thr-33 and Ser-369, which enables DYRK2 to escape from degradation by dissociation from MDM2 and to induce the kinase activity toward p53 at Ser-46 in the nucleus. |
|
| Publications: |
1 |
| + |
DYRK2 | up-regulates
phosphorylation
|
TP53 |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153544 |
Ser46 |
AMDDLMLsPDDIEQW |
Homo sapiens |
|
| pmid |
sentence |
| 17349958 |
Here, we demonstrate that the dual-specificity tyrosine-phosphorylation-regulated kinase 2 (dyrk2) directly phosphorylates p53 at ser46. these findings indicate that dyrk2 regulates p53 to induce apoptosis in response to dna damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK2 | up-regulates activity
phosphorylation
|
DPYSL3 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145975 |
Ser518 |
KGGTPAGsARGSPTR |
Homo sapiens |
|
| pmid |
sentence |
| 16611631 |
Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145979 |
Thr509 |
PVFDLTTtPKGGTPA |
Homo sapiens |
|
| pmid |
sentence |
| 16611631 |
Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145987 |
Thr514 |
TTTPKGGtPAGSARG |
Homo sapiens |
|
| pmid |
sentence |
| 16611631 |
Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
DYRK2 | down-regulates quantity by destabilization
phosphorylation
|
TBK1 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276939 |
Ser527 |
QDIDSRLsPGGSLAD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26407194 |
We further found that DYRK2 phosphorylated Ser527 of TBK1, which is essential for the recruitment of NLRP4 and for the E3 ubiquitin ligase DTX4 to degrade TBK1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK2 | down-regulates quantity by destabilization
phosphorylation
|
PSMC4 |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275845 |
Thr25 |
LSVSRPQtGLSFLGP |
|
|
| pmid |
sentence |
| 26655835 |
Through a kinome-wide screen, we have identified dual-specificity tyrosine-regulated kinase 2 (DYRK2) as the primary kinase that phosphorylates Rpt3-Thr25, leading to enhanced substrate translocation and degradation. |
|
| Publications: |
1 |
| + |
CDC25A | down-regulates activity
dephosphorylation
|
DYRK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277098 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34363019 |
Finally, DYRK2 is dephosphorylated by CDC25A, suggesting a feedback regulatory loop.|Notably, the co-expression of CDC25A inhibited the DYRK2 pro-apoptotic effect (Fig.\u00a06D), concurring with a possible inhibitory role on DYRK2 activity and further suggesting that the effect of DYRK2 was dependent on CDC25A. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MDM2 | down-regulates quantity by destabilization
ubiquitination
|
DYRK2 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275579 |
|
|
|
|
| pmid |
sentence |
| 19965871 |
Under normal conditions, nuclear and not cytoplasmic DYRK2 is ubiquitinated by MDM2, resulting in its constitutive degradation.|Upon exposure to genotoxic stress, ATM phosphorylates DYRK2 at Thr-33 and Ser-369, which enables DYRK2 to escape from degradation by dissociation from MDM2 and to induce the kinase activity toward p53 at Ser-46 in the nucleus. |
|
| Publications: |
1 |
| + |
DYRK2 | up-regulates activity
binding
|
EDVP |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271792 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19287380 |
DYRK2 functions as an adaptor in the EDVP E3 ligase complex. These experiments suggest that DYRK2 functions as a molecular assembler required for the specific recruitment of EDD to DDB1-VPRBP, thus forming a novel EDVP E3 ligase complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DYRK2
- 
- 