| + |
DYRK2 | down-regulates activity 
phosphorylation
|
SNAI1 |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279328 |
Ser104 |
GKGSQPPsPPSPAPS |
Homo sapiens |
|
| pmid |
sentence |
| 25603354 |
DYRK2 mediated Snail degradation protects against tumor cell metastasis.|DYRK2 phosphorylation of Snail at Ser104 triggers sequential phosphorylation by GSK3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
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 |
0.497 |
| 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 |
0.401 |
| 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 |
0.255 |
| 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 | down-regulates quantity
phosphorylation
|
CDC25A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279367 |
Ser283 |
PERSQEEsPPGSTKR |
Homo sapiens |
|
| pmid |
sentence |
| 34363019 |
DYRK2 depletion by siRNA substantially increased CDC25A protein levels (Fig.\u00a01C) and led to an extension of its half-life (Supplementary Fig.\u00a01C).|Phosphorylation of CDC25A on S283 by DYRK2 could suggest a role for DYRK2 complementary to the CDK/cyclin complexes\u2019 action during mitotic exit. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK2 |
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DYRK2
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