| + |
CSNK1E | up-regulates activity 
phosphorylation
|
APC |
0.22 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109660 |
Ser1279 |
SRCSSLSsLSSAEDE |
Homo sapiens |
SW-480 Cell |
| pmid |
sentence |
| 11487578 |
Apc can be phosphorylated by ck1epsilon at ser1279 and ser1392. Mutation of conserved serine residues in the beta-catenin regulatory motifs of APC interfered with both axin-dependent phosphorylation and phosphorylation by CKIepsilon and impaired the ability of APC to regulate beta-catenin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109664 |
Ser1392 |
SRCTSVSsLDSFESR |
Homo sapiens |
SW-480 Cell |
| pmid |
sentence |
| 11487578 |
Apc can be phosphorylated by ck1epsilon at ser1279 and ser1392. Mutation of conserved serine residues in the beta-catenin regulatory motifs of APC interfered with both axin-dependent phosphorylation and phosphorylation by CKIepsilon and impaired the ability of APC to regulate beta-catenin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | up-regulates activity
phosphorylation
|
DVL1 |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217845 |
Ser139 |
DNETGTEsMVSHRRE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16965538 |
Phenotypic analysis of mutant mDvl-1 indicates that phosphorylation of these sites stimulates the Dvl-activated beta-catenin-dependent Wnt signaling pathway in both cell culture and in Xenopus development. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217849 |
Ser142 |
TGTESMVsHRRERAR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16965538 |
Phenotypic analysis of mutant mDvl-1 indicates that phosphorylation of these sites stimulates the Dvl-activated beta-catenin-dependent Wnt signaling pathway in both cell culture and in Xenopus development. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | up-regulates
phosphorylation
|
LRP6 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145049 |
Ser1420 |
YVVHGPAsVPLGYVP |
Homo sapiens |
|
| pmid |
sentence |
| 16513652 |
We find that ckiepsilon binds to lrp5 and lrp6 in vitro and in vivo and identify three ckiepsilon-specific phosphorylation sites in lrp6. Two of the identified phosphorylation sites, ser1420 and ser1430, influence wnt signaling in vivo, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145053 |
Ser1430 |
LGYVPHPsSLSGSLP |
Homo sapiens |
|
| pmid |
sentence |
| 16513652 |
We find that ckiepsilon binds to lrp5 and lrp6 in vitro and in vivo and identify three ckiepsilon-specific phosphorylation sites in lrp6. Two of the identified phosphorylation sites, ser1420 and ser1430, influence wnt signaling in vivo, |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | up-regulates
phosphorylation
|
DVL2 |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197063 |
Ser143 |
FHPNVSSsHENLEPE |
Homo sapiens |
|
| pmid |
sentence |
| 22609948 |
We demonstrated that dvl2 is phosphorylated at s143 and t224 in a manner that requires both non-canonical wnt5a ligand and casein kinase 1 epsilon (ck1_), and that this event is critical to interact with plk1 in early stages of the cell cycle |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197555 |
Thr224 |
MSRFSSStEQSSASR |
Homo sapiens |
|
| pmid |
sentence |
| 22609948 |
We demonstrated that dvl2 is phosphorylated at s143 and t224 in a manner that requires both non-canonical wnt5a ligand and casein kinase 1 epsilon (ck1_), and that this event is critical to interact with plk1 in early stages of the cell cycle |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | down-regulates 
phosphorylation
|
CTNND1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-24443 |
Ser268 |
PQVRVGGsSVDLHRF |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 3133391 |
Moreover, in response to wnt3a, p120-catenin is phosphorylated at ser268, a modification dependent on ck1epsilon activity, which disrupts its interaction with e-cadherin and, subsequently, with lrp5/6, promoting the release of ck1epsilon/p120-catenin from the wnt receptor complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | down-regulates
phosphorylation
|
WWTR1 |
0.22 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-230747 |
Ser314 |
SREQSTDsGLGLGCY |
Homo sapiens |
|
| pmid |
sentence |
| 24715453 |
LATS1/2-mediated phosphorylation of a conserved serine in this region (Ser311 in human TAZ; Ser397 in human YAP) primes for further phosphorylation by CK1_/_ kinases (Ser314 on human TAZ; Ser400/403 in human YAP) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
CSNK1E | down-regulates activity
phosphorylation
|
CSNK1E |
0.22 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250807 |
Ser323 |
RMGQLRGsATRALPP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10542239 |
Amino acids Ser-323, Thr-325, Thr-334, Thr-337, Ser-368, Ser-405, Thr-407, and Ser-408 in the carboxyl-terminal tail of CKIepsilon were identified as probable in vivo autophosphorylation sites. A recombinant CKIepsilon protein with serine and threonine to alanine mutations eliminating these autophosphorylation sites was 8-fold more active than wild-type CKIepsilon using IkappaBalpha as a substrate. T |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250808 |
Ser368 |
NTSPRAIsRVDRERK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10542239 |
Amino acids Ser-323, Thr-325, Thr-334, Thr-337, Ser-368, Ser-405, Thr-407, and Ser-408 in the carboxyl-terminal tail of CKIepsilon were identified as probable in vivo autophosphorylation sites. A recombinant CKIepsilon protein with serine and threonine to alanine mutations eliminating these autophosphorylation sites was 8-fold more active than wild-type CKIepsilon using IkappaBalpha as a substrate. T |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250809 |
Ser405 |
EVSRIPAsQTSVPFD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10542239 |
Amino acids Ser-323, Thr-325, Thr-334, Thr-337, Ser-368, Ser-405, Thr-407, and Ser-408 in the carboxyl-terminal tail of CKIepsilon were identified as probable in vivo autophosphorylation sites. A recombinant CKIepsilon protein with serine and threonine to alanine mutations eliminating these autophosphorylation sites was 8-fold more active than wild-type CKIepsilon using IkappaBalpha as a substrate. T |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250810 |
Ser408 |
RIPASQTsVPFDHLG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10542239 |
Amino acids Ser-323, Thr-325, Thr-334, Thr-337, Ser-368, Ser-405, Thr-407, and Ser-408 in the carboxyl-terminal tail of CKIepsilon were identified as probable in vivo autophosphorylation sites. A recombinant CKIepsilon protein with serine and threonine to alanine mutations eliminating these autophosphorylation sites was 8-fold more active than wild-type CKIepsilon using IkappaBalpha as a substrate. T |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250811 |
Thr325 |
GQLRGSAtRALPPGP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10542239 |
Amino acids Ser-323, Thr-325, Thr-334, Thr-337, Ser-368, Ser-405, Thr-407, and Ser-408 in the carboxyl-terminal tail of CKIepsilon were identified as probable in vivo autophosphorylation sites. A recombinant CKIepsilon protein with serine and threonine to alanine mutations eliminating these autophosphorylation sites was 8-fold more active than wild-type CKIepsilon using IkappaBalpha as a substrate. T |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250812 |
Thr334 |
ALPPGPPtGATANRL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10542239 |
Amino acids Ser-323, Thr-325, Thr-334, Thr-337, Ser-368, Ser-405, Thr-407, and Ser-408 in the carboxyl-terminal tail of CKIepsilon were identified as probable in vivo autophosphorylation sites. A recombinant CKIepsilon protein with serine and threonine to alanine mutations eliminating these autophosphorylation sites was 8-fold more active than wild-type CKIepsilon using IkappaBalpha as a substrate. T |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250813 |
Thr337 |
PGPPTGAtANRLRSA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10542239 |
Amino acids Ser-323, Thr-325, Thr-334, Thr-337, Ser-368, Ser-405, Thr-407, and Ser-408 in the carboxyl-terminal tail of CKIepsilon were identified as probable in vivo autophosphorylation sites. A recombinant CKIepsilon protein with serine and threonine to alanine mutations eliminating these autophosphorylation sites was 8-fold more active than wild-type CKIepsilon using IkappaBalpha as a substrate. T |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250814 |
Thr407 |
SRIPASQtSVPFDHL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10542239 |
Amino acids Ser-323, Thr-325, Thr-334, Thr-337, Ser-368, Ser-405, Thr-407, and Ser-408 in the carboxyl-terminal tail of CKIepsilon were identified as probable in vivo autophosphorylation sites. A recombinant CKIepsilon protein with serine and threonine to alanine mutations eliminating these autophosphorylation sites was 8-fold more active than wild-type CKIepsilon using IkappaBalpha as a substrate. T |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
CSNK1E | down-regulates
phosphorylation
|
YAP1 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201165 |
Ser400 |
SRDESTDsGLSMSSY |
Homo sapiens |
|
| pmid |
sentence |
| 23431053 |
Phosphorylation of YAP (S381) and TAZ (S311) by Lats1/2 primes subsequent phosphorylation events by casein kinase 1 (CK1d/e); this sequential phosphorylation results in recruitment of b-transducin repeat-containing proteins (b-TRCP; a subunit of the SCF ubiquitin E3 ligase) and consequently leads to degradation of YAP/TAZ |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-230728 |
Ser400 |
SRDESTDsGLSMSSY |
Homo sapiens |
|
| pmid |
sentence |
| 24715453 |
LATS1/2-mediated phosphorylation of a conserved serine in this region (Ser311 in human TAZ; Ser397 in human YAP) primes for further phosphorylation by CK1_/_ kinases (Ser314 on human TAZ; Ser400/403 in human YAP) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-230733 |
Ser403 |
ESTDSGLsMSSYSVP |
Homo sapiens |
|
| pmid |
sentence |
| 24715453 |
LATS1/2-mediated phosphorylation of a conserved serine in this region (Ser311 in human TAZ; Ser397 in human YAP) primes for further phosphorylation by CK1_/_ kinases (Ser314 on human TAZ; Ser400/403 in human YAP) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201170 |
Ser403 |
ESTDSGLsMSSYSVP |
Homo sapiens |
|
| pmid |
sentence |
| 23431053 |
Phosphorylation of YAP (S381) and TAZ (S311) by Lats1/2 primes subsequent phosphorylation events by casein kinase 1 (CK1d/e); this sequential phosphorylation results in recruitment of b-transducin repeat-containing proteins (b-TRCP; a subunit of the SCF ubiquitin E3 ligase) and consequently leads to degradation of YAP/TAZ |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
CSNK1E | down-regulates activity
phosphorylation
|
CTNNB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244102 |
Ser45 |
GATTTAPsLSGKGNP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12176352 |
Using mass spectrometry and phosphopeptide-specific antibodies, we show that a complex of axin and casein kinase I (CKI) induces Beta-catenin phosphorylation at a single site: serine 45 (S45). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | down-regulates
phosphorylation
|
CTNNB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87448 |
Ser45 |
GATTTAPsLSGKGNP |
Homo sapiens |
|
| pmid |
sentence |
| 12000790 |
However, ck1epsilon has been recently shown to interact with axin (sakanaka et al. 1999;rubinfeld et al. 2001), and it was proposed that this kinase mediates axin-induced apc phosphorylation, thereby stabilizing the beta-catenin degradation complex (rubinfeld et al. 2001). We have, therefore, evaluated ck1epsilon as a candidate s45-kinase in several assays, both in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | down-regulates activity
phosphorylation
|
PER3 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250815 |
Ser622 |
ILSTAMLsLGSGISQ |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250816 |
Ser625 |
TAMLSLGsGISQCGY |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250817 |
Ser628 |
LSLGSGIsQCGYSST |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250818 |
Ser633 |
GISQCGYsSTIVHVP |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250819 |
Ser634 |
ISQCGYSsTIVHVPP |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250820 |
Thr635 |
SQCGYSStIVHVPPP |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
| Publications: |
6 |
Organism: |
Chlorocebus Aethiops |
| + |
CSNK1E | up-regulates activity
phosphorylation
|
BID |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250805 |
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-250806 |
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 |
| + |
CSNK1E | up-regulates
phosphorylation
|
PER2 |
0.49 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152094 |
Ser662 |
ALPGKAEsVASLTSQ |
Homo sapiens |
|
| pmid |
sentence |
| 17218255 |
Altering ckidelta dosage modulates the s662 phenotype demonstrating that ckidelta can regulate period through per2 in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | down-regulates
phosphorylation
|
EIF4EBP1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203240 |
Thr41 |
YSTTPGGtLFSTTPG |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 24247720 |
Mechanistic investigations showed that ck1_ interacted with and phosphorylated 4e-bp1 at two novel sites t41 and t50, which were essential for 4e-bp1 inactivation along with increased mrna translation and cell proliferation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203276 |
Thr50 |
FSTTPGGtRIIYDRK |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 24247720 |
Mechanistic investigations showed that ck1_ interacted with and phosphorylated 4e-bp1 at two novel sites t41 and t50, which were essential for 4e-bp1 inactivation along with increased mrna translation and cell proliferation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide | down-regulates
chemical inhibition
|
CSNK1E |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110053 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11524435 |
Cki-7, an inhibitor of ck1epsilon |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | up-regulates
phosphorylation
|
ROR2 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129117 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15375164 |
We also show that ror2 is phosphorylated by ckiepsilon on serine/threonine residues. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | down-regulates
phosphorylation
|
PER1 |
0.53 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137706 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15917222 |
Ck1_ and ck1_2 can promote proteasome-dependent per1 degradation in mammalian tissue culture cells, and their removal by rnai leads to an increased abundance of per1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | down-regulates
phosphorylation
|
LEF1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134497 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15747065 |
Here, we identify ck1 and ck2 as major kinases that directly bind to and phosphorylate lef-1 inducing distinct, kinase-specific changes in the lef-1/dna complex.CK1-dependent phosphorylation inhibits, whereas ck2 activates lef-1/beta-catenin transcriptional activity in reporter gene assays. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | up-regulates
phosphorylation
|
GSK3B/Axin/APC |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227976 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12000790 |
We conclude that a major role of axin in the wnt is to provide the kinase activity that initiates the betBeta-catenin phosphorylation cascade at s45. This process is mediated by cki, the alfa, delta, or ? Isoform, all detected in association with axin by lc/ms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | up-regulates
phosphorylation
|
AXIN1 |
0.22 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87444 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12000790 |
We conclude that a major role of axin in the wnt is to provide the kinase activity that initiates the betBeta-catenin phosphorylation cascade at s45. This process is mediated by cki, the alfa, delta, or ? Isoform, all detected in association with axin by lc/ms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | up-regulates activity
phosphorylation
|
DVL2 |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244097 |
|
|
Caenorhabditis elegans |
|
| pmid |
sentence |
| 10517632 |
In addition, CKI bound to and increased the phosphorylation of dishevelled, a known component of the Wnt pathway |
|
| Publications: |
1 |
Organism: |
Caenorhabditis Elegans |
| + |
DVL3 | up-regulates
binding
|
CSNK1E |
0.22 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71759 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10535959 |
Ckiepsilon was in a complex with axin and other downstream components of the wnt pathway, including dishevelled. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | up-regulates
phosphorylation
|
TCF3 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110056 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11524435 |
Tcf3 is a substrate for both glycogen synthase kinase (gsk) 3 and casein kinase (ck) 1epsilon, and phosphorylation of tcf3 by ckiepsilon stimulates its binding to beta-catenin, an effect reversed by gsk3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
CSNK1E
- 
- 