| + |
CSNK1A1L | up-regulates activity 
phosphorylation
|
NFAT5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274111 |
Ser158 |
LLDNSRMsCQDEGCG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18411282 |
However, the siRNA knockdown of CK1α1L significantly reduced the nuclear export of OREBP/TonEBP under hypotonic conditions (Fig. 5F). Taken together, these data suggest that CK1α1L is the kinase that phosphorylates Ser-158 in the regulation of OREBP/TonEBP export. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1A1L | down-regulates 
phosphorylation
|
CTNNB1 |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87430 |
Ser45 |
GATTTAPsLSGKGNP |
Homo sapiens |
|
| pmid |
sentence |
| 12000790 |
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 |
| + |
CSNK1A1L | up-regulates
phosphorylation
|
GLI2 |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179972 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18698484 |
Gli2 is phosphorylated by gsk3 and ck1 for the fbxw11 (betatrcp2)-mediated degradation ci is phosphorylated by pka at multiple sites priming phosphorylation by both gsk3 and cki, leading to partial proteolysis. The pka, gsk3, and cki sites are conserved in gli2 and gli3, vertebrate homologs of ci that are similarly processed |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144551 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16481469 |
Gli2 is phosphorylated by gsk3 and ck1 for the fbxw11 (betatrcp2)-mediated degradation ci is phosphorylated by pka at multiple sites priming phosphorylation by both gsk3 and cki, leading to partial proteolysis. The pka, gsk3, and cki sites are conserved in gli2 and gli3, vertebrate homologs of ci that are similarly processed |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FAM83E | up-regulates quantity
binding
|
CSNK1A1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273758 |
|
|
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 |
| + |
FAM83A | up-regulates quantity
binding
|
CSNK1A1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273756 |
|
|
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 |
| + |
FAM83C | up-regulates quantity
binding
|
CSNK1A1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273760 |
|
|
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 |
| + |
FAM83G | up-regulates quantity
binding
|
CSNK1A1L |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273753 |
|
|
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
|
CSNK1A1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273757 |
|
|
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 |
| + |
FAM83F | up-regulates quantity
binding
|
CSNK1A1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273759 |
|
|
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 |
| + |
CSNK1A1L | up-regulates
phosphorylation
|
LRP6 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184699 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19293931 |
Ck1 also phosphorylates lrp6 at the second ser residue in the pppspxs motif ck1_ in the lrp5/e-cadherin/p120-catenin complex temporally coincides with p120-catenin phosphorylation in ser268. moreover, and considering the close similarity between the catalytic domains of ck1_ and ck1_, it is possible that ck1_ is indeed responsible for the phosphorylation at ser1420 and ser1430 in lrp5/6 that negatively affects wnt signaling by still not defined mechanisms |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173853 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21606194 |
Ck1 also phosphorylates lrp6 at the second ser residue in the pppspxs motif ck1_ in the lrp5/e-cadherin/p120-catenin complex temporally coincides with p120-catenin phosphorylation in ser268. moreover, and considering the close similarity between the catalytic domains of ck1_ and ck1_, it is possible that ck1_ is indeed responsible for the phosphorylation at ser1420 and ser1430 in lrp5/6 that negatively affects wnt signaling by still not defined mechanisms |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FAM83H | up-regulates quantity
binding
|
CSNK1A1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273755 |
|
|
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 |
| + |
CSNK1A1L | up-regulates 
|
GLIS2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152962 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289029 |
We decided to focus on the interaction between _-catenin and glis2. the critical role of the first zinc finger motif was confirmed by the observation that a point mutation in the first zinc finger motif, that destroys its tetrahedral configuration, abolished the interaction. _-catenin contains several functional domains, the amino terminus interacts with gsk3_ and casein kinase i_ (ck1) binding sites while its 12 armadillo repeats provides an interface for tcf/lefs, the co-activator cbp, and several other proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates
phosphorylation
|
CSNK1A1L |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144557 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16481469 |
Mutation of either the three pka sites or pka-primed cki sites prevents phosphorylation of ci by cki in vitro and blocks ci cleavage in embryos |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FAM83B | up-regulates quantity
binding
|
CSNK1A1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273754 |
|
|
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 |
| + |
CSNK1A1L | up-regulates
phosphorylation
|
GLI3 |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144554 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16481469 |
Ci is phosphorylated by pka at multiple sites priming phosphorylation by both gsk3 and cki, leading to partial proteolysis. The pka, gsk3, and cki sites are conserved in gli2 and gli3, vertebrate homologs of ci that are similarly processed |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CSNK1A1L
- 
- 