+ |
CSNK2A1 | down-regulates quantity by destabilization
phosphorylation
|
WEE1 |
0.418 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276038 |
Ser121 |
WEEEGFGsSSPVKSP |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
16085715 |
In the present study, we show that phosphorylation of S123 (pS123) by CDK promoted the binding of Wee1A to beta-TrCP through three independent mechanisms. S123 phosphorylation creates a PBD-binding motif and accelerates S53 phosphorylation by Plk1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK1 | down-regulates
phosphorylation
|
WEE1 |
0.854 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123824 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
|
pmid |
sentence |
15070733 |
We have found also that the major M-phase kinases polo-like kinase 1 (Plk1) and Cdc2 are responsible for the phosphorylation of S53 and S123, respectively, and that in each case phosphorylation generates an unconventional phospho-degron (signal for degradation) that can be recognized by beta-TrCP |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139465 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
|
pmid |
sentence |
16085715 |
We show that phosphorylation of S123 (pS123) by CDK promoted the binding of Wee1A to beta-TrCP through three independent mechanisms. The pS123 not only directly interacted with basic residues in the WD40 repeat domain of beta-TrCP but also primed phosphorylation by two independent protein kinases, Plk1 and CK2 (formerly casein kinase 2) |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CyclinB/CDK1 | down-regulates quantity by destabilization
phosphorylation
|
WEE1 |
0.777 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267471 |
Ser123 |
EEGFGSSsPVKSPAA |
|
|
pmid |
sentence |
23051732 |
Cdk1 phosphorylates Wee1 on Ser-123, which primes additional phosphorylation by other kinases, leading to the formation of phosphodegrons responsible for SCF (Skp1/cullin/F-box) ubiquitin-mediated degradation of Wee1 |
|
Publications: |
1 |
+ |
CDK2 | down-regulates quantity by destabilization
|
WEE1 |
0.651 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276039 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
16085715 |
PS123 primes CK2 to phosphorylate S121, resulting in creation of a β-TrCP phosphodegron (EEGFGpS121) that is responsible for the instability of Wee1A during interphase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDC14A | up-regulates quantity by stabilization
dephosphorylation
|
WEE1 |
0.562 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267469 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23051732 |
In particular, we found that Cdc14A inhibits Wee1 degradation through the dephosphorylation of Ser-123 and Ser-139 residues. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276952 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
|
pmid |
sentence |
23051732 |
However, when both Ser-123 and Ser-139 were modified (2A), although Wee1 was still phosphorylated by Cdk1, treatment with active Cdc14A did not decrease the phosphorylation signal to any significant extent ( xref , lane 5), indicating that Cdc14A dephosphorylates Wee1 at Ser-123 and Ser-139 residues.|Our results indicate that Wee1 is a substrate of Cdc14 phosphatases in human cells and that by reversing specific Cdk1 phosphorylation, the Cdc14A isoform induces Wee1 stability, which in turn directly inhibits Cdk1 activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267470 |
Ser139 |
YFLGSSFsPVRCGGP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23051732 |
In particular, we found that Cdc14A inhibits Wee1 degradation through the dephosphorylation of Ser-123 and Ser-139 residues. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276953 |
Ser139 |
YFLGSSFsPVRCGGP |
Homo sapiens |
|
pmid |
sentence |
23051732 |
However, when both Ser 123 and Ser 139 were modified (2A), although Wee1 was still phosphorylated by Cdk1, treatment with active Cdc14A did not decrease the phosphorylation signal to any significant extent (XREF_FIG, lane 5), indicating that Cdc14A dephosphorylates Wee1 at Ser 123 and Ser 139 residues.|Our results indicate that Wee1 is a substrate of Cdc14 phosphatases in human cells and that by reversing specific Cdk1 phosphorylation, the Cdc14A isoform induces Wee1 stability, which in turn directly inhibits Cdk1 activity. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
PLK1 | down-regulates
phosphorylation
|
WEE1 |
0.626 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139473 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
|
pmid |
sentence |
16085715 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-128643 |
Ser53 |
GHSTGEDsAFQEPDS |
Homo sapiens |
|
pmid |
sentence |
15350223 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123832 |
Ser53 |
GHSTGEDsAFQEPDS |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
15070733 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139477 |
Ser53 |
GHSTGEDsAFQEPDS |
Homo sapiens |
|
pmid |
sentence |
16085715 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
CDK2 | down-regulates
phosphorylation
|
WEE1 |
0.651 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139469 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
|
pmid |
sentence |
16085715 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. During the s and g2 phases, s123 (wee1) is phosphorylated by a cdk (possibly cdk2). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3B | down-regulates quantity by destabilization
phosphorylation
|
WEE1 |
0.335 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276632 |
Ser211 |
SSVKLRGsSLFMDTE |
in vitro |
|
pmid |
sentence |
24817118 |
Serine 211 phosphorylation occurred under control conditions in the absence of CK1δ and in the presence of GSK3-β (Fig. 5, D and E). |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CSNK1D | down-regulates quantity by destabilization
phosphorylation
|
WEE1 |
0.314 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276631 |
Ser212 |
SVKLRGSsLFMDTEK |
in vitro |
|
pmid |
sentence |
24817118 |
Casein kinase 1-mediated N-terminal Weee1 phosphorylation is required for interaction with the F-box protein β-TrCP.MS/MS spectra of human Wee1 identifying serine 212 as phosphorylated after incubation with recombinant CK1δ. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PLK1 | down-regulates quantity by destabilization
phosphorylation
|
WEE1 |
0.626 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276040 |
Ser53 |
GHSTGEDsAFQEPDS |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
16085715 |
In the present study, we show that phosphorylation of S123 (pS123) by CDK promoted the binding of Wee1A to beta-TrCP through three independent mechanisms. S123 phosphorylation creates a PBD-binding motif and accelerates S53 phosphorylation by Plk1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BRSK1 |
phosphorylation
|
WEE1 |
0.45 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250601 |
Ser642 |
KKMNRSVsLTIY |
in vitro |
|
pmid |
sentence |
15150265 |
HsSAD1 protein produced in Sf9 cells phosphorylated the GST-fused human wild-type Wee1A fragment but not its S642A mutant produced inEscherichia coli (Fig. 2). The kinase-dead hsSAD1 mutant (K59A) failed to phosphorylate the wild-type Wee1A fragment. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
WEE1 | down-regulates
phosphorylation
|
CDK2 |
0.651 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83139 |
Tyr15 |
EKIGEGTyGVVYKAR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11029659 |
Identification and characterization of human wee1b, a new member of the wee1 family of cdk-inhibitory kinases. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
WEE1 | down-regulates
phosphorylation
|
CDK1 |
0.854 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139491 |
Tyr15 |
EKIGEGTyGVVYKGR |
Homo sapiens |
|
pmid |
sentence |
16096060 |
The wee1 kinase phosphorylates and inhibits cyclin-dependent kinase 1 (cdk1), thereby delaying entry into mitosis until appropriate conditions have been met |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
WEE1 | down-regulates quantity by destabilization
phosphorylation
|
ERG |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277529 |
Tyr183 |
FQRLTPSyNADILLS |
Homo sapiens |
Prostate Cancer Cell Line |
pmid |
sentence |
32871104 |
Here, we demonstrate that DNA damage induces proteasomal degradation of wild-type ERG and TMPRSS2-ERG oncoprotein through ERG threonine-187 and tyrosine-190 phosphorylation mediated by GSK3β and WEE1, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK1 | down-regulates
phosphorylation
|
WEE1 |
0.303 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123528 |
|
|
Homo sapiens |
|
pmid |
sentence |
15037762 |
Kinases targeted sequentially to the neck, cla4/pak and cdc5/polo, are responsible for stepwise phosphorylation and down-regulation of swe1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHEK1 | up-regulates
phosphorylation
|
WEE1 |
0.595 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163164 |
|
|
Homo sapiens |
|
pmid |
sentence |
20068082 |
Chk1 also phosphorylates and stabilizes wee1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AR | down-regulates quantity by repression
transcriptional regulation
|
WEE1 |
0.263 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253678 |
|
|
Homo sapiens |
|
pmid |
sentence |
16281084 |
After AR antagonist flutamide treatment, three hundred and twenty-six genes (3.93%) expressed differentially, 97 down-regulated and 219 up-regulated. Among them, eight up-regulated genes might be cell cycle-related, namely CDC10, NRAS, BTG1, Wee1, CLK3, DKFZP564A122, CDKN1A and BTG2. The CDKN1A and BTG1 gene mRNA expression was confirmed to be higher in the experimental group by RT-PCR, while p53 mRNA expression had no significant changes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
1-[6-(2-hydroxypropan-2-yl)-2-pyridinyl]-6-[4-(4-methyl-1-piperazinyl)anilino]-2-prop-2-enyl-3-pyrazolo[3,4-d]pyrimidinone | down-regulates
chemical inhibition
|
WEE1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-194423 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163173 |
|
|
Homo sapiens |
|
pmid |
sentence |
20068082 |
Mk-1775 (merck). This wee1 inhibitor (ic50, 5.2nm) potentiates the activity of dna-damaging agents (e.g., gemcitabine, cisplatin, carboplatin) in vitro and in vivo, particularly in p53-negative cancers |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
SCF-betaTRCP | down-regulates
binding
|
WEE1 |
0.396 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-217184 |
|
|
Homo sapiens |
|
pmid |
sentence |
15340381 |
Scfb-trcp continues to have a role in this phase, however, through its induced degradation of the cdk1 inhibitor, wee1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP2R2A | up-regulates quantity by stabilization
dephosphorylation
|
WEE1 |
0.393 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266381 |
|
|
Homo sapiens |
A-549 Cell |
pmid |
sentence |
33108758 |
Knockout of FAM122A results in activation of PP2A-B55α, a phosphatase that dephosphorylates the WEE1 protein and rescues WEE1 from ubiquitin-mediated degradation. in tumor cells with oncogene-driven replication stress, CHK1 can directly phosphorylate FAM122A, leading to activation of the PP2A-B55α phosphatase and increased WEE1 expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SCF-betaTRCP | down-regulates quantity by destabilization
ubiquitination
|
WEE1 |
0.396 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276633 |
|
|
in vitro |
|
pmid |
sentence |
24817118 |
Casein kinase 1-mediated N-terminal Weee1 phosphorylation is required for interaction with the F-box protein β-TrCP.MS/MS spectra of human Wee1 identifying serine 212 as phosphorylated after incubation with recombinant CK1δ. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
BTRC | down-regulates
binding
|
WEE1 |
0.403 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-128439 |
|
|
Homo sapiens |
|
pmid |
sentence |
15340381 |
Scfb-trcp continues to have a role in this phase, however, through its induced degradation of the cdk1 inhibitor, wee1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTDP1 | up-regulates activity
dephosphorylation
|
WEE1 |
0.392 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277142 |
|
|
Homo sapiens |
|
pmid |
sentence |
27670139 |
At mitosis exit, Fcp1 promoted inhibitory Cdk1 phosphorylation by dephosphorylating Wee1, and ubiquitin dependent cyclin B degradation by dephosphorylating Cdc20 and USP44.|This lead us to hypothesize that, during prolonged mitosis in AMCDs treated cancer cells, progressive Fcp1 induced Wee1 reactivation might lead to progressive loss of Cdk1 activity that weakens the SAC to a point in which the mitotic state could not be sustained . |
|
Publications: |
1 |
Organism: |
Homo Sapiens |