| + |
CSNK1D | down-regulates 
phosphorylation
|
MDM2 |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167497 |
Ser118 |
NQQESSDsGTSVSEN |
Homo sapiens |
|
| pmid |
sentence |
| 20708156 |
Phosphorylation by casein kinase i promotes the turnover of the mdm2 oncoprotein via the scf(beta-trcp) ubiquitin ligase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167501 |
Ser121 |
ESSDSGTsVSENRCH |
Homo sapiens |
|
| pmid |
sentence |
| 20708156 |
Phosphorylation by casein kinase i promotes the turnover of the mdm2 oncoprotein via the scf(beta-trcp) ubiquitin ligase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167509 |
Ser246 |
DSVSDQFsVEFEVES |
Homo sapiens |
|
| pmid |
sentence |
| 20708156 |
Cki phosphorylates mdm2 at multiple sites to trigger mdm2/beta-trcp1 interactionbeta-trcp promotes mdm2 turnover and ubiquitination |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167513 |
Ser253 |
SVEFEVEsLDSEDYS |
Homo sapiens |
|
| pmid |
sentence |
| 20708156 |
Cki phosphorylates mdm2 at multiple sites to trigger mdm2/beta-trcp1 interactionbeta-trcp promotes mdm2 turnover and ubiquitination |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91195 |
Ser253 |
SVEFEVEsLDSEDYS |
Homo sapiens |
|
| pmid |
sentence |
| 12167711 |
Hypophosphorylation of mdm2 augments p53 stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91199 |
Ser262 |
DSEDYSLsEEGQELS |
Homo sapiens |
|
| pmid |
sentence |
| 12167711 |
Hypophosphorylation of mdm2 augments p53 stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167517 |
Ser262 |
DSEDYSLsEEGQELS |
Homo sapiens |
|
| pmid |
sentence |
| 20708156 |
Cki phosphorylates mdm2 at multiple sites to trigger mdm2/beta-trcp1 interactionbeta-trcp promotes mdm2 turnover and ubiquitination |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167520 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20708156 |
Phosphorylation by casein kinase i promotes the turnover of the mdm2 oncoprotein via the scf(beta-trcp) ubiquitin ligase. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | up-regulates 
phosphorylation
|
DVL2 |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197547 |
Ser143 |
FHPNVSSsHENLEPE |
Homo sapiens |
|
| pmid |
sentence |
| 22609948 |
Ck1_/__dependent phosphorylation of dvl2 at s143 and t224and that this event is critical to interact with plk1 in early stages of the cell cycle |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197551 |
Thr224 |
MSRFSSStEQSSASR |
Homo sapiens |
|
| pmid |
sentence |
| 22609948 |
Ck1_/__dependent phosphorylation of dvl2 at s143 and t224and that this event is critical to interact with plk1 in early stages of the cell cycle |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | up-regulates activity
phosphorylation
|
CDK5 |
0.53 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250798 |
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. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CSNK1D |
phosphorylation
|
PSEN2 |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250799 |
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-250803 |
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-250804 |
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 |
| + |
CSNK1D | up-regulates
phosphorylation
|
TP53 |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73266 |
Ser20 |
PLSQETFsDLWKLLP |
Homo sapiens |
|
| pmid |
sentence |
| 10606744 |
Protein kinase ck1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75889 |
Ser20 |
PLSQETFsDLWKLLP |
Homo sapiens |
|
| pmid |
sentence |
| 10734067 |
Here we show that the direct association between a p53 n-terminal peptide and mdm2 is disrupted by phosphorylation of the peptide on thr(18) but not by phosphorylation at other n-terminal sites, including ser(15) and ser(37). Thr(18) was phosphorylated in vitro by casein kinase (ck1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73270 |
Thr18 |
EPPLSQEtFSDLWKL |
Homo sapiens |
|
| pmid |
sentence |
| 10606744 |
Protein kinase ck1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | up-regulates
phosphorylation
|
PRH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75272 |
Ser24 |
QDLDEDVsQEDVPLV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10684652 |
Ser22 may be phosphorylated by a g-ck that recognizes an atypical substrate sequence or by a novel kinase. While prp1 secreted from salivary glands is fully phosphorylated at ser8 and 22 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
CSNK1D | down-regulates
phosphorylation
|
HIF1A |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167476 |
Ser247 |
KTFLSRHsLDMKFSY |
Homo sapiens |
|
| pmid |
sentence |
| 20699359 |
In this work, we investigate the phosphorylation of the n-terminal heterodimerization (pas) domain of hif-1alpha and identify ser247 as a major site of in vitro modification by casein kinase 1delta (ck1delta). Mutation of this site to alanine, surprisingly, enhanced the transcriptional activity of hif-1alpha |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | down-regulates activity
phosphorylation
|
MDM2 |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91191 |
Ser269 |
SEEGQELsDEDDEVY |
Homo sapiens |
|
| pmid |
sentence |
| 12167711 |
Hypophosphorylation of mdm2 augments p53 stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | down-regulates
phosphorylation
|
WWTR1 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-234438 |
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 |
| + |
CSNK1D | up-regulates activity
phosphorylation
|
GJA1 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249329 |
Ser325 |
NRMGQAGsTISNSHA |
Rattus norvegicus |
Kidney Cell Line |
| pmid |
sentence |
| 12270943 |
We have examined the role of casein kinase 1 (CK1) in connexin-43 (Cx43) gap junction assembly. Cellular co-immunoprecipitation experiments and in vitro CK1 phosphorylation reactions indicate that CK1 interacted with and phosphorylated Cx43, initially on serine(s) 325, 328, or 330.| To examine CK1 function, normal rat kidney cells were treated with CKI-7, and Cx43 content was analyzed by Triton X-100 extraction, cell-surface biotinylation, and immunofluorescence. Western blot analysis indicated a slight increase in total Cx43, whereas gap junctional (Triton-insoluble) Cx43 decreased, and non-junctional plasma membrane Cx43 increased (as detected by cell surface biotinylation). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249330 |
Ser328 |
GQAGSTIsNSHAQPF |
Rattus norvegicus |
Kidney Cell Line |
| pmid |
sentence |
| 12270943 |
We have examined the role of casein kinase 1 (CK1) in connexin-43 (Cx43) gap junction assembly. Cellular co-immunoprecipitation experiments and in vitro CK1 phosphorylation reactions indicate that CK1 interacted with and phosphorylated Cx43, initially on serine(s) 325, 328, or 330.| To examine CK1 function, normal rat kidney cells were treated with CKI-7, and Cx43 content was analyzed by Triton X-100 extraction, cell-surface biotinylation, and immunofluorescence. Western blot analysis indicated a slight increase in total Cx43, whereas gap junctional (Triton-insoluble) Cx43 decreased, and non-junctional plasma membrane Cx43 increased (as detected by cell surface biotinylation). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249331 |
Ser330 |
AGSTISNsHAQPFDF |
Rattus norvegicus |
Kidney Cell Line |
| pmid |
sentence |
| 12270943 |
We have examined the role of casein kinase 1 (CK1) in connexin-43 (Cx43) gap junction assembly. Cellular co-immunoprecipitation experiments and in vitro CK1 phosphorylation reactions indicate that CK1 interacted with and phosphorylated Cx43, initially on serine(s) 325, 328, or 330.| To examine CK1 function, normal rat kidney cells were treated with CKI-7, and Cx43 content was analyzed by Triton X-100 extraction, cell-surface biotinylation, and immunofluorescence. Western blot analysis indicated a slight increase in total Cx43, whereas gap junctional (Triton-insoluble) Cx43 decreased, and non-junctional plasma membrane Cx43 increased (as detected by cell surface biotinylation). |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus |
| + |
CSNK1D | up-regulates activity
phosphorylation
|
PSEN2 |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250800 |
Ser327 |
DPEMEEDsYDSFGEP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250801 |
Ser330 |
MEEDSYDsFGEPSYP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250802 |
Ser335 |
YDSFGEPsYPEVFEP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CSNK1D | up-regulates
phosphorylation
|
KIR3DL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158121 |
Ser385 |
AGNRTANsEDSDEQD |
Homo sapiens |
|
| pmid |
sentence |
| 17911614 |
In this study, we have mapped constitutive phosphorylation sites for casein kinases, protein kinase c, and an unidentified kinase on the kir cytoplasmic domain. Three of these phosphorylation sites are highly conserved in human inhibitory kir. Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of ser(394) by protein kinase c slightly suppresses kir3dl1 inhibitory function, and reduces receptor internalization and turnover. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158125 |
Ser388 |
RTANSEDsDEQDPEE |
Homo sapiens |
|
| pmid |
sentence |
| 17911614 |
In this study, we have mapped constitutive phosphorylation sites for casein kinases, protein kinase c, and an unidentified kinase on the kir cytoplasmic domain. Three of these phosphorylation sites are highly conserved in human inhibitory kir. Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of ser(394) by protein kinase c slightly suppresses kir3dl1 inhibitory function, and reduces receptor internalization and turnover. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | down-regulates quantity by destabilization
phosphorylation
|
ZNF322 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264892 |
Ser396 |
ELSPPHAsEASQMS |
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 28581525 |
CK1delta and GSK3beta kinases sequentially phosphorylate ZNF322A at serine-396 and then serine-391. Moreover, the doubly phosphorylated ZNF322A protein creates a destruction motif for the ubiquitin ligase FBXW7alpha leading to ZNF322A protein destruction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | down-regulates
phosphorylation
|
MAPT |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121709 |
Ser396 |
DDKKAKTsTRSSAKT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14761950 |
Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules.Here we characterized the contribution of one ck1 isoform, ckidelta, to the phosphorylation of tau at residues ser202/thr205 and ser396/ser404 in human embryonic kidney 293 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121705 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14761950 |
Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules.Here we characterized the contribution of one ck1 isoform, ckidelta, to the phosphorylation of tau at residues ser202/thr205 and ser396/ser404 in human embryonic kidney 293 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121713 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14761950 |
Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules.Here we characterized the contribution of one ck1 isoform, ckidelta, to the phosphorylation of tau at residues ser202/thr205 and ser396/ser404 in human embryonic kidney 293 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121717 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14761950 |
Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules.Here we characterized the contribution of one ck1 isoform, ckidelta, to the phosphorylation of tau at residues ser202/thr205 and ser396/ser404 in human embryonic kidney 293 cells. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | down-regulates
phosphorylation
|
YAP1 |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-230738 |
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-201143 |
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-201154 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-230743 |
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) |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
CSNK1D | down-regulates
phosphorylation
|
CTNNB1 |
0.606 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87441 |
Ser45 |
GATTTAPsLSGKGNP |
Homo sapiens |
|
| pmid |
sentence |
| 12000790 |
However, ckiepsilon 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 -catenin degradation complex (rubinfeld et al. 2001). We have, therefore, evaluated cki as a candidate s45-kinase in several assays, both in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | up-regulates
phosphorylation, binding
|
AXIN1 |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87437 |
Ser46 |
PASYSFCsGKGVGIK |
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/mscomplex of axin and casein kinase i (cki) induces betBeta-catenin phosphorylation at a single site: serine 45 (s45) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87433 |
|
|
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 beta-catenin phosphorylation cascade at s45. This process is mediated by cki, the alfa, delta, or epsilon isoform, all detected in association with axin by lc/ms. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK1D |
phosphorylation
|
BACE1 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250797 |
Ser498 |
DDFADDIsLLK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11278841 |
Here, we report that BACE can be phosphorylated within its cytoplasmic domain at serine residue 498 by casein kinase 1. Phosphorylation exclusively occurs after full maturation of BACE by propeptide cleavage and complex N-glycosylation. | After reinternalization, BACE wild type as well as BACE S498D are efficiently retrieved from early endosomal compartments and further targeted to later endosomal compartments and/or the trans-Golgi network. In contrast, nonphosphorylatable BACE S498A is retained within early endosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | up-regulates
phosphorylation
|
NCOA3 |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184946 |
Ser601 |
SDKESKEsSVEGAEN |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 19339517 |
In this study, we show that both eralpha and aib1 are substrates for ck1delta in vitro, and identify a novel aib1 phosphorylation site (s601) targeted by ck1delta, significant for the co-activator function of aib1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | up-regulates activity
phosphorylation
|
DCK |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275799 |
Ser74 |
EFEELTMsQKNGGNV |
|
|
| pmid |
sentence |
| 20637175 |
We showed that recombinant CKI delta phosphorylated several residues of bacterially overexpressed dCK: Ser-74, but also Ser-11, Ser-15, and Thr-72. Phosphorylation of dCK by CKI delta correlated with increased activity reaching at least 4-fold. Site-directed mutagenesis demonstrated that only Ser-74 phosphorylation was involved in dCK activation by CKI delta, |
|
| Publications: |
1 |
| + |
CSNK1D | down-regulates activity
phosphorylation
|
CDH1 |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274046 |
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 |
| Pathways: | Hippo Signaling |
| + |
CSNK1D | up-regulates
phosphorylation
|
UHRF1 |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200349 |
Ser95 |
SELSDTDsGCCLGQS |
Homo sapiens |
|
| pmid |
sentence |
| 23297342 |
We further show that uhrf1 physically interacts with _-trcp1 in a manner dependent on phosphorylation of serine 108 (s108(uhrf1)) within the dsg degron. Furthermore, we demonstrate that s108(uhrf1) phosphorylation is catalyzed by casein kinase 1 delta (ck1_) and is important for the recognition of uhrf1 by scf(_-trcp). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | up-regulates activity
phosphorylation
|
LRP6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275402 |
Thr1479 |
SSSSTKGtYFPAILN |
Homo sapiens |
|
| pmid |
sentence |
| 35487243 |
Central to WNT signalosome formation is phosphorylation of LRP6 at multiple sites, with GSK3β phosphorylating LRP6 at S1490 and CK1 family members phosphorylating LRP6 at T1479 and T1493 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275403 |
Thr1493 |
NPPPSPAtERSHYTM |
Homo sapiens |
|
| pmid |
sentence |
| 35487243 |
Central to WNT signalosome formation is phosphorylation of LRP6 at multiple sites, with GSK3β phosphorylating LRP6 at S1490 and CK1 family members phosphorylating LRP6 at T1479 and T1493 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FAM83A | up-regulates quantity
binding
|
CSNK1D |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273765 |
|
|
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 |
| + |
CSNK1D | down-regulates quantity by destabilization
phosphorylation
|
PER3 |
0.711 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267998 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11865049 |
We show here that mPer proteins, negative limbs of the autoregulatory loop, are specific substrates for CKIepsilon and CKIdelta. The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Circadian clock |
| + |
FAM83E | up-regulates quantity
binding
|
CSNK1D |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273767 |
|
|
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
|
CSNK1D |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273768 |
|
|
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 |
| + |
CSNK1D | down-regulates quantity by destabilization
phosphorylation
|
PER1 |
0.796 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267999 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11865049 |
We show here that mPer proteins, negative limbs of the autoregulatory loop, are specific substrates for CKIepsilon and CKIdelta. The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268001 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11165242 |
Human casein kinase Idelta phosphorylation of human circadian clock proteins period 1 and 2. We have now extended our previous studies to show that human casein kinase Idelta (hCKIdelta), the closest homologue to hCKIepsilon, associates with and phosphorylates hPER1 and causes protein instability. Furthermore, we observed that both hCKIdelta and hCKIepsilon phosphorylated and caused protein instability of human period 2 protein (hPER2). |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| Pathways: | Circadian clock |
| + |
CSNK1D | up-regulates
phosphorylation, binding
|
GSK3B/Axin/APC |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227970 |
|
|
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/mscomplex of axin and casein kinase i (cki) induces betBeta-catenin phosphorylation at a single site: serine 45 (s45) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227973 |
|
|
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 beta-catenin phosphorylation cascade at s45. This process is mediated by cki, the alfa, delta, or epsilon isoform, all detected in association with axin by lc/ms. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FAM83B | up-regulates quantity
binding
|
CSNK1D |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273766 |
|
|
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 |
| + |
CSNK1D | down-regulates quantity by destabilization
phosphorylation
|
PER2 |
0.863 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268000 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11165242 |
Human casein kinase Idelta phosphorylation of human circadian clock proteins period 1 and 2. We have now extended our previous studies to show that human casein kinase Idelta (hCKIdelta), the closest homologue to hCKIepsilon, associates with and phosphorylates hPER1 and causes protein instability. Furthermore, we observed that both hCKIdelta and hCKIepsilon phosphorylated and caused protein instability of human period 2 protein (hPER2). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Circadian clock |
| + |
CSNK1D | down-regulates
phosphorylation
|
LEF1 |
0.254 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134494 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15747065 |
Cki_/_ binds and phosphorylates lef-1, and this phosphorylation disrupts lef-1_-catenin interaction |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B/Axin/APC | up-regulates
binding
|
CSNK1D |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227908 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12000790 |
Complex of axin and casein kinase i (cki) induces beta-catenin phosphorylation at a single site: serine 45 (s45). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AXIN1 | up-regulates
binding
|
CSNK1D |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87401 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12000790 |
Complex of axin and casein kinase i (cki) induces beta-catenin phosphorylation at a single site: serine 45 (s45). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CSNK1D
- 
- 