+ |
CSNK1A1 | up-regulates
phosphorylation
|
CREB1 |
0.318 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64258 |
Ser100 |
ESEDSQEsVDSVTDS |
Homo sapiens |
|
pmid |
sentence |
9931297 |
Ser108, ser111 and ser114, located in a region matching the consensus sequence for the casein kinase ii target, were required.These results strongly suggest that the casein kinase ii target region is involved in cell cycle-regulated phosphorylation of the creb protein and also in transcriptional enhancement. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64250 |
Ser94 |
QISTIAEsEDSQESV |
Homo sapiens |
|
pmid |
sentence |
9931297 |
Ser108, ser111 and ser114, located in a region matching the consensus sequence for the casein kinase ii target, were required.These results strongly suggest that the casein kinase ii target region is involved in cell cycle-regulated phosphorylation of the creb protein and also in transcriptional enhancement. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | WNT Signaling |
+ |
CSNK1A1 |
phosphorylation
|
LGALS3 |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250789 |
Ser12 |
FSLHDALsGSGNPNP |
in vitro |
|
pmid |
sentence |
8253806 |
L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CSNK1A1 | down-regulates quantity by destabilization
phosphorylation
|
RAPGEF2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276605 |
Ser1244 |
ASLDAADsGRGSWTS |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
24290981 |
Here, we report that in response to factors that promote cell motility, the Rap guanine exchange factor RAPGEF2 is rapidly phosphorylated by I-kappa-B-kinase-β and casein kinase-1α and consequently degraded by the proteasome via the SCF(βTrCP) ubiquitin ligase. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276604 |
Ser1248 |
AADSGRGsWTSCSSG |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
24290981 |
Here, we report that in response to factors that promote cell motility, the Rap guanine exchange factor RAPGEF2 is rapidly phosphorylated by I-kappa-B-kinase-β and casein kinase-1α and consequently degraded by the proteasome via the SCF(βTrCP) ubiquitin ligase. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
SNCA |
0.379 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-73795 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
pmid |
sentence |
10617630 |
In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2.| together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of alpha-synuclein could affect its binding to membranes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates quantity by destabilization
phosphorylation
|
PHLPP1 |
0.313 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276261 |
Ser1359 |
VPRPHVQsVLLTPQD |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
19797085 |
We show that the beta-TrCP-mediated degradation requires phosphorylation of PHLPP1 by casein kinase I and glycogen synthase kinase 3beta (GSK-3beta), and activation of the phosphatidylinositol 3-kinase/Akt pathway suppresses the degradation of PHLPP1 by inhibiting the GSK-3beta activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276262 |
Thr1363 |
HVQSVLLtPQDEFFI |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
19797085 |
We show that the beta-TrCP-mediated degradation requires phosphorylation of PHLPP1 by casein kinase I and glycogen synthase kinase 3beta (GSK-3beta), and activation of the phosphatidylinositol 3-kinase/Akt pathway suppresses the degradation of PHLPP1 by inhibiting the GSK-3beta activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
CDK5 |
0.303 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275966 |
Ser159 |
GIPVRCYsAEVVTLW |
in vitro |
|
pmid |
sentence |
10500146 |
We also show that casein kinase I, but not casein kinase II, can phosphorylate and activate cdk5 in vitro. Ser(159) in cdk5 is homologous to the regulatory Thr(160) in cdk2. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
JADE1 |
0.282 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273618 |
Ser18 |
EDSDDNGsLSTTWSQ |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25100726 |
We demonstrate that the destruction complex component casein kinase 1α (CK1α) phosphorylates Jade-1 at a conserved SLS motif and reduces the ability of Jade-1 to inhibit β-catenin signaling. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273617 |
Ser20 |
SDDNGSLsTTWSQNS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25100726 |
We demonstrate that the destruction complex component casein kinase 1α (CK1α) phosphorylates Jade-1 at a conserved SLS motif and reduces the ability of Jade-1 to inhibit β-catenin signaling. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
RHOB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179255 |
Ser185 |
ALQKRYGsQNGCINC |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18590726 |
Mass spectrometry analysis demonstrates that rhob is monophosphorylated by ck1, in its c-terminal end, on serine 185. lastly we show that the inhibition of ck1 activates rhob and promotes rhob dependent actin fiber formation and egf-r level. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates
phosphorylation
|
FOXG1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154386 |
Ser19 |
MIPKSSFsINSLVPE |
Homo sapiens |
Neuron |
pmid |
sentence |
17435750 |
Cki phosphorylation of ser 19 of foxg1 promotes nuclear import |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
CSNK1A1 |
phosphorylation
|
PSEN2 |
0.4 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250790 |
Ser19 |
EVCDERTsLMSAESP |
in vitro |
|
pmid |
sentence |
8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250791 |
Ser7 |
sDSEEEVC |
in vitro |
|
pmid |
sentence |
8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250792 |
Ser9 |
LTFMASDsEEEVCDE |
in vitro |
|
pmid |
sentence |
8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
FADD |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139307 |
Ser194 |
QNRSGAMsPMSWNSD |
Homo sapiens |
|
pmid |
sentence |
16061179 |
FADD is essential for death receptor (DR)-induced apoptosis.|Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 |
phosphorylation
|
TP53 |
0.58 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-162648 |
Ser20 |
PLSQETFsDLWKLLP |
Homo sapiens |
|
pmid |
sentence |
20041275 |
Our data support the concept that non-primed phosphorylation of p53 by ck1 is an isoform-specific reaction preferentially affecting s20 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
NFATC3 |
0.571 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109800 |
Ser207 |
AARFTLGsPLTSPGG |
Homo sapiens |
BHK Cell |
pmid |
sentence |
9630228 |
Dominant-negative cki? Induces nuclear import of nf-at4these results demonstrated that the cki? Phosphorylation sites identified in vitro were also specifically phosphorylated by cki? In vivo, and that these residues were crucial for the masking of the nls of nf-at4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109763 |
Ser211 |
TLGSPLTsPGGSPGG |
Homo sapiens |
BHK Cell |
pmid |
sentence |
9630228 |
Dominant-negative cki alpha Induces nuclear import of nf-at4 these results demonstrated that the cki alpha Phosphorylation sites identified in vitro were also specifically phosphorylated by cki alpha In vivo, and that these residues were crucial for the masking of the nls of nf-at4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109781 |
Ser215 |
PLTSPGGsPGGCPGE |
Homo sapiens |
BHK Cell |
pmid |
sentence |
9630228 |
Dominant-negative cki alpha Induces nuclear import of nf-at4 these results demonstrated that the cki alpha Phosphorylation sites identified in vitro were also specifically phosphorylated by cki alpha In vivo, and that these residues were crucial for the masking of the nls of nf-at4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109768 |
Thr204 |
NEAAARFtLGSPLTS |
Homo sapiens |
|
pmid |
sentence |
9630228 |
Dominant-negative cki alpha Induces nuclear import of nf-at4 these results demonstrated that the cki alpha Phosphorylation sites identified in vitro were also specifically phosphorylated by cki alpha In vivo, and that these residues were crucial for the masking of the nls of nf-at4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109776 |
Thr210 |
FTLGSPLtSPGGSPG |
Homo sapiens |
BHK Cell |
pmid |
sentence |
9630228 |
Dominant-negative cki alpha Induces nuclear import of nf-at4 these results demonstrated that the cki alpha Phosphorylation sites identified in vitro were also specifically phosphorylated by cki alpha In vivo, and that these residues were crucial for the masking of the nls of nf-at4. |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
ZRANB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273621 |
Ser209 |
RWRGSCSsGNSQRRS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
30686098 |
Interestingly, ZRANB1 is phosphorylated at Thr35, and Ser209 residues by CSNK1A1, and this phosphorylation activates its deubiquitinating activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273620 |
Thr35 |
RAQRPSGtIITEDPF |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
30686098 |
Interestingly, ZRANB1 is phosphorylated at Thr35, and Ser209 residues by CSNK1A1, and this phosphorylation activates its deubiquitinating activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
YWHAQ |
0.494 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250795 |
Ser232 |
LTLWTSDsAGEECDA |
in vitro |
|
pmid |
sentence |
9360956 |
This protein kinase has been identified as casein kinase Ialpha (CKIalpha) by peptide mapping analysis and sequencing. Among mammalian 14-3-3, only 14-3-3 tau possesses a phosphorylatable residue at the same position (Ser-233), and we show that this residue is also phosphorylated by CKI. In addition, we show that 14-3-3 zeta is exclusively phosphorylated on Thr-233 in human embryonic kidney 293 cells. The residue 233 is located within a region shown to be important for the association of 14-3-3 to target proteins. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CSNK1A1 | down-regulates quantity by destabilization
phosphorylation
|
BHLHE40 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276851 |
Ser243 |
GSDTDTDsGYGGESE |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25202122 |
CK1α-mediated phosphorylation of DEC1 on a conserved degron is required for DEC1 degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
HNRNPC |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133528 |
Ser253 |
ETNVKMEsEGGADDS |
Homo sapiens |
|
pmid |
sentence |
15687492 |
A kinase activity was identified in mouse liver that phosphorylates the acd of hnrnp-c at ser(240) and at two sites at ser(225)-ser(228). The kinase was purified and identified by tandem mass spectrometry as protein kinase ck1alpha (formerly casein kinase 1alpha).hnrnp-c1 that was also modified at the ck1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that ck1alpha-mediated phosphorylation modulates the mrna binding ability of hnrnp-c. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
HNRNPC |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133532 |
Ser260 |
SEGGADDsAEEGDLL |
Homo sapiens |
|
pmid |
sentence |
15687492 |
In contrast, hnRNP-C1 that was also modified at the CK1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133536 |
Ser299 |
EGEDDRDsANGEDDS |
Homo sapiens |
|
pmid |
sentence |
15687492 |
In contrast, hnRNP-C1 that was also modified at the CK1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates quantity by destabilization
phosphorylation
|
FOXO4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277325 |
Ser265 |
PRSSSNAsSVSTRLS |
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
28945225 |
Here we report that CK1α similarly destabilizes FOXO4 in RAS-mutant cells by phosphorylation at serines 265/268. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277326 |
Ser268 |
SSNASSVsTRLSPLR |
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
28945225 |
Here we report that CK1α similarly destabilizes FOXO4 in RAS-mutant cells by phosphorylation at serines 265/268. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates quantity by destabilization
phosphorylation
|
MYC |
0.286 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276387 |
Ser267 |
PPTTSSDsEEEQEDE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22025562 |
Together, our findings provide evidence for CK1α-mediated destruction of c-Myc and identify c-Myc S252 as a crucial CK1α phosphorylation site for c-Myc degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Wnt in cancer, WNT Signaling, WNT/FLT3 |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
DEPTOR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176871 |
Ser286 |
SSMSSCGsSGYFSSS |
Homo sapiens |
|
pmid |
sentence |
22017877 |
Phosphorylation of all three serine residues in the deptor degron (ser286, ser287, and ser291) is necessary for - and directly mediates - the interaction with _trcp. ck1 phosphorylated the degron of deptor, as shown by western blotting with the phospho-specific antibody (fig. S3e-f). In contrast, mtor alone was unable to induce phosphorylation of deptor on ser286, ser287, and ser291. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176875 |
Ser287 |
SMSSCGSsGYFSSSP |
Homo sapiens |
|
pmid |
sentence |
22017877 |
Phosphorylation of all three serine residues in the deptor degron (ser286, ser287, and ser291) is necessary for - and directly mediates - the interaction with _trcp. ck1 phosphorylated the degron of deptor, as shown by western blotting with the phospho-specific antibody (fig. S3e-f). In contrast, mtor alone was unable to induce phosphorylation of deptor on ser286, ser287, and ser291. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176879 |
Ser291 |
CGSSGYFsSSPTLSS |
Homo sapiens |
|
pmid |
sentence |
22017877 |
Phosphorylation of all three serine residues in the deptor degron (ser286, ser287, and ser291) is necessary for - and directly mediates - the interaction with _trcp. ck1 phosphorylated the degron of deptor, as shown by western blotting with the phospho-specific antibody (fig. S3e-f). In contrast, mtor alone was unable to induce phosphorylation of deptor on ser286, ser287, and ser291. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates
phosphorylation
|
MDM4 |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-199015 |
Ser289 |
DDLEDSKsLSDDTDV |
Homo sapiens |
|
pmid |
sentence |
23028042 |
Previous studies showed that casein kinase 1? (ck1?) Stably associates with mdmx, stimulates mdmx-p53 binding, and cooperates with mdmx to inactivate p53ck1? Binding to the mdmx central domain and phosphorylation of s289 disrupts the intramolecular interaction, allowing the n terminus to bind p53 with increased affinity. After dna damage, the mdmx-ck1? Complex is disrupted by chk2-mediated phosphorylation of mdmx at s367, leading to reduced mdmx-p53 binding. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
RELA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276916 |
Ser316 |
FKSIMKKsPFSGPTD |
in vitro |
|
pmid |
sentence |
26082493 |
These data strongly suggested that CKI phosphorylated Ser-316 of p65. Our data suggested that phosphorylation of p65 on Ser-316 controls the activity and function of NF-κB. Importantly, we found that phosphorylation at the novel Ser-316 site and other two known phosphorylation sites, Ser-529 and Ser-536, either individually or cooperatively, regulated distinct groups of NF-κB-dependent genes, suggesting the unique role of each individual phosphorylation site on NF-κB-dependent gene regulation. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
FOXO |
0.392 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252899 |
Ser318 |
SRTNSNAsTVSGRLS |
Homo sapiens |
|
pmid |
sentence |
20110348 |
Casein kinase (ck) 1 mediates the hierarchical phosphorylation of foxo3a at s318 and s321, which like foxo1 (rena et al., 2002 blue right-pointing triangle, 2004 blue right-pointing triangle), is probably to enhance its rate of nuclear export |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252900 |
Ser321 |
NSNASTVsGRLSPIM |
Homo sapiens |
|
pmid |
sentence |
20110348 |
Casein kinase (ck) 1 mediates the hierarchical phosphorylation of foxo3a at s318 and s321, which like foxo1 (rena et al., 2002 blue right-pointing triangle, 2004 blue right-pointing triangle), is probably to enhance its rate of nuclear export |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252898 |
|
|
Homo sapiens |
|
pmid |
sentence |
19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
FOXO3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163672 |
Ser318 |
SRTNSNAsTVSGRLS |
Homo sapiens |
|
pmid |
sentence |
20110348 |
Casein kinase (ck) 1 mediates the hierarchical phosphorylation of foxo3a at s318 and s321, which like foxo1 (rena et al., 2002 blue right-pointing triangle, 2004 blue right-pointing triangle), is probably to enhance its rate of nuclear export |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163676 |
Ser321 |
NSNASTVsGRLSPIM |
Homo sapiens |
|
pmid |
sentence |
20110348 |
Casein kinase (ck) 1 mediates the hierarchical phosphorylation of foxo3a at s318 and s321, which like foxo1 (rena et al., 2002 blue right-pointing triangle, 2004 blue right-pointing triangle), is probably to enhance its rate of nuclear export |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183661 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
pmid |
sentence |
19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates quantity by destabilization
phosphorylation
|
TIAM1 |
0.313 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276673 |
Ser329 |
DVNAGEGsEFADSGI |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25124033 |
Phosphorylation of Ser329, Ser334, and Thr340 in Tiam1 is required for its interaction with βTrCP1. The proteolysis of Tiam1 is prevented by βTrCP silencing, inhibition of CK1 and MEK, or mutation of the Tiam1 degron site. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
SQSTM1 |
0.4 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273769 |
Ser349 |
SSKEVDPsTGELQSL |
Mus musculus |
|
pmid |
sentence |
37723657 |
Mechanistically, CSNK1A1 interacted with STING1 upon the CGAS-STING1 pathway activation and promoted STING1 autophagic degradation by enhancing the phosphorylation of SQSTM1/p62 at serine 351 (serine 349 in human), which was critical for SQSTM1-mediated STING1 autophagic degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
CSNK1A1 | down-regulates quantity by destabilization
phosphorylation
|
ERG |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276936 |
Ser38 |
TEMTASSsSDYGQTS |
in vitro |
|
pmid |
sentence |
26344095 |
Using in vitro kinase assays, we further demonstrated that deletion of degron 1 largely abolished CKI-mediated phosphorylation of ERG (Figure S5B), indicating that serine residues within degron 1 are the major CKI phosphorylation sites. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276935 |
Ser39 |
EMTASSSsDYGQTSK |
in vitro |
|
pmid |
sentence |
26344095 |
Using in vitro kinase assays, we further demonstrated that deletion of degron 1 largely abolished CKI-mediated phosphorylation of ERG (Figure S5B), indicating that serine residues within degron 1 are the major CKI phosphorylation sites. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
CTNNB1 |
0.783 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165022 |
Ser45 |
GATTTAPsLSGKGNP |
Homo sapiens |
|
pmid |
sentence |
20419129 |
Specifically, ck1_ phosphorylates _-catenin at s45, which primes this n-terminal region for subsequent phosphorylations by gsk3 at t41, s37 and s33 [7]. These latter two phosphorylations are recognized by the e3-ligase component, _-trcp, for ultimate ubiquitylation and destruction by the proteosome |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Wnt in cancer, WNT Signaling, WNT/FLT3 |
+ |
CSNK1A1 |
phosphorylation
|
EIF2B5 |
0.328 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250787 |
Ser466 |
DEDDGEFsDDSGADQ |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11500362 |
The fifth site, which lies outside the catalytic domain of eIF2Bepsilon, can be phosphorylated by casein kinase 1. All five sites are phosphorylated in the eIF2B complex in vivo. | A phosphopeptide corresponding to this region was identified in Asp‐N digests of eIF2Bϵ phosphorylated in vitro by CK1, suggesting that Ser461 or Ser464 may be phosphorylated by this kinase in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250788 |
Ser469 |
DGEFSDDsGADQEKD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11500362 |
The fifth site, which lies outside the catalytic domain of eIF2Bepsilon, can be phosphorylated by casein kinase 1. All five sites are phosphorylated in the eIF2B complex in vivo. | A phosphopeptide corresponding to this region was identified in Asp‐N digests of eIF2Bϵ phosphorylated in vitro by CK1, suggesting that Ser461 or Ser464 may be phosphorylated by this kinase in vivo. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
AXIN1 |
0.776 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249192 |
Ser469 |
AHEENPEsILDEHVQ |
in vitro |
|
pmid |
sentence |
17318175 |
Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249189 |
Ser75 |
LGYEPEGsASPTPPY |
in vitro |
|
pmid |
sentence |
17318175 |
Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249191 |
Ser77 |
YEPEGSAsPTPPYLK |
in vitro |
|
pmid |
sentence |
17318175 |
Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
SRPK2 |
0.253 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275460 |
Ser497 |
SRTVSASsTGDLPKA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29153836 |
Here, we demonstrate that mTORC1 promotes lipid biogenesis via SRPK2, a key regulator of RNA-binding SR proteins. mTORC1-activated S6K1 phosphorylates SRPK2 at Ser494, which primes Ser497 phosphorylation by CK1. These phosphorylation events promote SRPK2 nuclear translocation and phosphorylation of SR proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 |
phosphorylation
|
SLC18A2 |
0.327 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250794 |
Ser511 |
PIGEDEEsESD |
in vitro |
|
pmid |
sentence |
9045708 |
Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250793 |
Ser513 |
GEDEESEsD |
in vitro |
|
pmid |
sentence |
9045708 |
Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
CTPS2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167623 |
Ser568 |
LSSSDRYsDASDDSF |
Homo sapiens |
|
pmid |
sentence |
20739275 |
Hctps2 ser(568) was phosphorylated by casein kinase 1 both in vitro and in vivo. Mutation of ser(568) (s568a) significantly increased hctps2 activity, demonstrating that ser(568) is a major inhibitory phosphorylation site. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates
phosphorylation
|
LGALS3 |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124583 |
Ser6 |
sLHDALSG |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
15121858 |
These results indicate that phosphorylation of gal-3 promotes its nuclear export after apoptotic stimuli through enhanced nuclear export. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
TUT1 |
0.271 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273619 |
Ser6 |
sDVESLPR |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
26138484 |
We identified a phosphorylated residue (serine 6, S6) on Star-PAP in the zinc finger region, the domain required for PIPKIα interaction. We show that S6 is phosphorylated by CKIα within the nucleus which is required for Star-PAP nuclear retention and interaction with PIPKIα. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
BID |
0.289 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250785 |
Ser64 |
LQTDGNRsSHSRLGR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11583622 |
Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. | These results suggest that residues S61, S64, and to a much lesser extent T58 are sites of phosphorylation of Bid. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250786 |
Thr59 |
EGYDELQtDGNRSSH |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11583622 |
Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. | These results suggest that residues S61, S64, and to a much lesser extent T58 are sites of phosphorylation of Bid. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 |
phosphorylation
|
AHCYL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249185 |
Ser77 |
SSTDSYSsAASYTDS |
Chlorocebus aethiops |
|
pmid |
sentence |
17635105 |
Residue 68 resides in a consensus phosphorylation site for PKD (Figure 1A) [22,23]. Interestingly, phosphorylation of Ser68 could allow for subsequent phosphorylation of Ser71, Ser74, Ser77 and Ser80 by CK1, for which the consensus phosphorylation site is pS/T-X-X-S/T |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
CDC25A |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164734 |
Ser79 |
QRMGSSEsTDSGFCL |
Homo sapiens |
|
pmid |
sentence |
20348946 |
Here, we report that casein kinase 1 alpha (ck1alpha) phosphorylates cdc25a on both s79 and s82 in a hierarchical manner requiring prior phosphorylation of s76 by chk1 or gsk-3beta. This facilitates beta-trcp binding and ubiquitin-mediated proteolysis of cdc25a |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164738 |
Ser82 |
GSSESTDsGFCLDSP |
Homo sapiens |
|
pmid |
sentence |
20348946 |
Here, we report that casein kinase 1 alpha (ck1alpha) phosphorylates cdc25a on both s79 and s82 in a hierarchical manner requiring prior phosphorylation of s76 by chk1 or gsk-3beta. This facilitates beta-trcp binding and ubiquitin-mediated proteolysis of cdc25a |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
AGO2 |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276511 |
Ser824 |
LVDKEHDsAEGSHTS |
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
28114302 |
Our experiments demonstrated that target engagement by AGO2 stimulates its hierarchical, multi-site phosphorylation by CSNK1A1 on a series of highly conserved residues (S824-S834).Although this impairs target binding, dephosphorylation by ANKRD52-PPP6C allows AGO2 to engage new targets. Inactivation of this cycle strongly inhibits global miRNA-mediated repression. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276512 |
Ser828 |
EHDSAEGsHTSGQSN |
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
28114302 |
Our experiments demonstrated that target engagement by AGO2 stimulates its hierarchical, multi-site phosphorylation by CSNK1A1 on a series of highly conserved residues (S824-S834).Although this impairs target binding, dephosphorylation by ANKRD52-PPP6C allows AGO2 to engage new targets. Inactivation of this cycle strongly inhibits global miRNA-mediated repression. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276508 |
Ser831 |
SAEGSHTsGQSNGRD |
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
28114302 |
Our experiments demonstrated that target engagement by AGO2 stimulates its hierarchical, multi-site phosphorylation by CSNK1A1 on a series of highly conserved residues (S824-S834).Although this impairs target binding, dephosphorylation by ANKRD52-PPP6C allows AGO2 to engage new targets. Inactivation of this cycle strongly inhibits global miRNA-mediated repression. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276509 |
Ser834 |
GSHTSGQsNGRDHQA |
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
28114302 |
Our experiments demonstrated that target engagement by AGO2 stimulates its hierarchical, multi-site phosphorylation by CSNK1A1 on a series of highly conserved residues (S824-S834).Although this impairs target binding, dephosphorylation by ANKRD52-PPP6C allows AGO2 to engage new targets. Inactivation of this cycle strongly inhibits global miRNA-mediated repression. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276510 |
Thr830 |
DSAEGSHtSGQSNGR |
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
28114302 |
Our experiments demonstrated that target engagement by AGO2 stimulates its hierarchical, multi-site phosphorylation by CSNK1A1 on a series of highly conserved residues (S824-S834).Although this impairs target binding, dephosphorylation by ANKRD52-PPP6C allows AGO2 to engage new targets. Inactivation of this cycle strongly inhibits global miRNA-mediated repression. |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
CDH1 |
0.317 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274045 |
Ser844 |
GSGSEAAsLSSLNSS |
|
|
pmid |
sentence |
17353278 |
Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts|CK1 colocalizes with E-cadherin and phosphorylates the cytoplasmic domain of E-cadherin in vitro and in a cell culture system. We show that the major CK1 phosphorylation site of E-cadherin is serine 846 |
|
Publications: |
1 |
+ |
CSNK1A1 | up-regulates
phosphorylation
|
SNCA |
0.379 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-73799 |
Ser87 |
KTVEGAGsIAAATGF |
Homo sapiens |
Neuron |
pmid |
sentence |
10617630 |
In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2. These data demonstrate that alpha-synuclein is constitutively phosphorylated within its c terminus and may indicate that the function of alpha-synuclein is regulated by phosphorylation/dephosphorylation.From these data we conclude that _-synuclein is predominantly phosphorylated at serine residue 129. However, a second serine at position 87 is also used for phosphorylation to some extent. together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of _-synuclein could affect its binding to membranes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
CREB1 |
0.318 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64254 |
Ser97 |
TIAESEDsQESVDSV |
Homo sapiens |
|
pmid |
sentence |
9931297 |
Ser108, ser111 and ser114, located in a region matching the consensus sequence for the casein kinase ii target, were required.These results strongly suggest that the casein kinase ii target region is involved in cell cycle-regulated phosphorylation of the creb protein and also in transcriptional enhancement. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | WNT Signaling |
+ |
CSNK1A1 | up-regulates
phosphorylation
|
LRP6 |
0.534 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-143034 |
Thr1493 |
NPPPSPAtERSHYTM |
Homo sapiens |
|
pmid |
sentence |
16341017 |
We show that wnt induces sequential phosphorylation of lrp6 by gsk3 and casein kinase 1, and this dual phosphorylation promotes the engagement of lrp6 with the scaffolding protein axin.Site ii, like site i, was phosphorylated, as detected by means of a phospho-specific antibody (ab1493, for phosphorylated t1493 in lrp6) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-143037 |
|
|
Homo sapiens |
|
pmid |
sentence |
16341017 |
We show that wnt induces sequential phosphorylation of lrp6 by gsk3 and casein kinase 1, and this dual phosphorylation promotes the engagement of lrp6 with the scaffolding protein axin. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | WNT Signaling, WNT/FLT3 |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
YWHAZ |
0.56 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250796 |
Thr232 |
LTLWTSDtQGDEAEA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
9360956 |
This protein kinase has been identified as casein kinase Ialpha (CKIalpha) by peptide mapping analysis and sequencing. Among mammalian 14-3-3, only 14-3-3 tau possesses a phosphorylatable residue at the same position (Ser-233), and we show that this residue is also phosphorylated by CKI. In addition, we show that 14-3-3 zeta is exclusively phosphorylated on Thr-233 in human embryonic kidney 293 cells. The residue 233 is located within a region shown to be important for the association of 14-3-3 to target proteins. | We have now shown that in vivo phosphorylation of 14-3-3 zeta at the CKIalpha site (Thr-233) negatively regulates its binding to c-Raf, and may be important in Raf-mediated signal transduction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates quantity by destabilization
phosphorylation
|
CBX4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277512 |
Thr437 |
ARSISTPtCLGGSPA |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
32111827 |
The phosphorylation of CBX4 at T437 by casein kinase 1α (CK1α) facilitated its ubiquitination at both K178 and K280 and subsequent degradation by CHIP, and this phosphorylation of CBX4 could be reduced by TNFα. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FAM83A | up-regulates quantity
binding
|
CSNK1A1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273748 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
OSBP2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264877 |
|
|
|
|
pmid |
sentence |
30925160 |
CK1a1, JNK1 and CDK1 had the highest site-specific activity for ORP4L, while CDK1, GSK3a, CK1a1 and GSK3b showed the highest specificity for the site when corrected for background activity with ORP4L-S4A. Because of the complexity of the serine/proline-rich site, we did not determine which serine(s) in ORP4L were phosphorylated by candidate kinases.|We conclude that phosphorylation of a unique serine/proline motif in the ORD induces a conformation change in ORP4L that enhances interaction with vimentin and cholesterol extraction from membranes. |
|
Publications: |
1 |
+ |
CSNK1A1 | up-regulates activity
binding
|
GSK3B/Axin/APC |
0.658 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-227967 |
|
|
Homo sapiens |
|
pmid |
sentence |
22083140 |
In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)] |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-227964 |
|
|
Homo sapiens |
|
pmid |
sentence |
19293931 |
In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)] |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Wnt in cancer, WNT Signaling |
+ |
FAM83C | up-regulates quantity
binding
|
CSNK1A1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273752 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
binding
|
GSK3B |
0.562 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184696 |
|
|
Homo sapiens |
|
pmid |
sentence |
19293931 |
In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)] |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-177233 |
|
|
Homo sapiens |
|
pmid |
sentence |
22083140 |
In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)] |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | WNT/FLT3 |
+ |
FAM83B | up-regulates quantity
binding
|
CSNK1A1 |
0.349 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273746 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FAM83D | up-regulates quantity
binding
|
CSNK1A1 |
0.391 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273749 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
lenalidomide | down-regulates quantity by destabilization
|
CSNK1A1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236895 |
|
|
Homo sapiens |
KG-1 Cell |
pmid |
sentence |
26131937 |
We demonstrate that lenalidomide induces the ubiquitination of casein kinase 1A1 (CK1a) by the E3 ubiquitin ligase CUL4RBX1DDB1CRBN (known as CRL4CRBN) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
FOXO1 |
0.392 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183658 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
pmid |
sentence |
19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | WNT/FLT3 |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
GLI2 |
0.549 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154222 |
|
|
Homo sapiens |
|
pmid |
sentence |
17419683 |
In the absence of hedgehog signaling, gli1 is transcriptionally repressed, gli2 is phosphorylated by gsk3 and ck1 for the fbxw11 (betatrcp2)-mediated degradation, and gli3 is processed to a cleaved repressor. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146112 |
|
|
Homo sapiens |
|
pmid |
sentence |
16611981 |
Gli2 can also be phosphorylated directly by ck-1 at the non-optimal sites |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
FOXO4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183664 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
pmid |
sentence |
19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FAM83F | up-regulates quantity
binding
|
CSNK1A1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273751 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FAM83H | up-regulates quantity
binding
|
CSNK1A1 |
0.395 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273747 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
FOXO6 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183667 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
pmid |
sentence |
19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FAM83G | up-regulates quantity
binding
|
CSNK1A1 |
0.381 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273745 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FAM83E | up-regulates quantity
binding
|
CSNK1A1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273750 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Cullin4-RBX1-DDB1 | down-regulates quantity by destabilization
ubiquitination
|
CSNK1A1 |
0.384 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236907 |
|
|
Homo sapiens |
KG-1 Cell |
pmid |
sentence |
26131937 |
We demonstrate that lenalidomide induces the ubiquitination of casein kinase 1A1 (CK1a) by the E3 ubiquitin ligase CUL4RBX1DDB1CRBN (known as CRL4CRBN) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates
phosphorylation
|
SMO |
0.5 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174542 |
|
|
Homo sapiens |
|
pmid |
sentence |
21695114 |
We demonstrate that mammalian Smo (mSmo) is activated through multi-site phosphorylation of its carboxyl-terminal tail by CK1α and GRK2. Phosphorylation of mSmo induces its active conformation and simultaneously promotes its ciliary accumulation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | down-regulates
phosphorylation
|
GLI3 |
0.581 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-116512 |
|
|
Homo sapiens |
|
pmid |
sentence |
11955435 |
In principle, pka, ck-1 and gsk3 can phosphorylate as many as 19 serine residues in gli3: fourpkasites, three primarygsk3sites, four primary ck-1 sites and eight secondary gsk3 and ck-1 sites |
|
Publications: |
1 |
Organism: |
Homo Sapiens |