Relation Results

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

Identifier	Residue	Sequence	Organism
SIGNOR-217845	Ser139	DNETGTEsMVSHRRE	Homo sapiens
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
SIGNOR-217849	Ser142	TGTESMVsHRRERAR	Homo sapiens
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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
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
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

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

Identifier	Residue	Sequence	Organism
SIGNOR-276645	Ser280	DGGIYIGsIMKGGAV	in vitro
pmid	sentence
24993822	Co-expression of CK1ϵ with FLAG-Dvl3 retards electrophoretic migration and induces phosphorylation-dependent shift of Dvl (PS-Dvl3). mutations of Ser-280 and Ser-311 prevent efficient activation of Wnt/β-catenin by Dvl3.

Identifier	Residue	Sequence	Organism
SIGNOR-276647	Ser311	EINFENMsNDDAVRV	in vitro
pmid	sentence
24993822	Co-expression of CK1ϵ with FLAG-Dvl3 retards electrophoretic migration and induces phosphorylation-dependent shift of Dvl (PS-Dvl3). mutations of Ser-280 and Ser-311 prevent efficient activation of Wnt/β-catenin by Dvl3.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
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

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:

Circadian clock, Hippo Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-277212	Ser349	QNWEEADsMKSSVES	Homo sapiens
pmid	sentence
26928339	CK1ɛ interacted with and phosphorylated TRAF3 at Ser349, which thereby promoted the Lys63 (K63)-linked ubiquitination of TRAF3 and subsequent recruitment of the kinase TBK1 to TRAF3.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277525	Tyr116	EILALQIyCRNESRG	Homo sapiens	HEK-293T Cell
pmid	sentence
32779804	We found that the interaction of CK1ε with TRAF3Y116F, TRAF3Y446F were markedly decreased compared with interactions with WT TRAF3 by Co‐IP (Figure 6C); as expected, TRAF3Y116F and TRAF3Y446F mutants exhibited reduced K63‐linked ubiquitination (Figure 6D). These data suggest that the phosphorylation of TRAF3 at Tyr 116 and Tyr 446 regulate CK1ε‐induced K63‐linked ubiquitination.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277524	Tyr446	SLYSQPFyTGYFGYK	Homo sapiens	HEK-293T Cell
pmid	sentence
32779804	We found that the interaction of CK1ε with TRAF3Y116F, TRAF3Y446F were markedly decreased compared with interactions with WT TRAF3 by Co‐IP (Figure 6C); as expected, TRAF3Y116F and TRAF3Y446F mutants exhibited reduced K63‐linked ubiquitination (Figure 6D). These data suggest that the phosphorylation of TRAF3 at Tyr 116 and Tyr 446 regulate CK1ε‐induced K63‐linked ubiquitination.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276064	Ser389	RGAPANVsSSDLTGR	in vitro
pmid	sentence
17525164	AMPK enhances mPer2 degradation and CKIɛ activity by phosphorylating Ser-389 of CKIɛ. One of the regulators of the period length is casein kinase Iepsilon (CKIepsilon), which by phosphorylating and inducing the degradation of the circadian clock component, mPer2, shortens the period length. AMPK phosphorylates Ser-389 of CKIepsilon, resulting in increased CKIepsilon activity and degradation of mPer2.

Publications:

1

Organism:

In Vitro

Pathways:

Circadian clock

Identifier	Residue	Sequence	Organism
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
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
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
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

Identifier	Residue	Sequence	Organism
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

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

Identifier	Residue	Sequence	Organism
SIGNOR-277419	Ser480	PVPHSGSsGYGSLGS	in vitro
pmid	sentence
30425162	Priming-independent clusters located in the C-terminal portion of PER2’s PAS domains are targeted by CK1ε/δ and are required for ubiquitin ligase–mediated degradation of PER2

Identifier	Residue	Organism
SIGNOR-276065		in vitro
pmid	sentence
17525164	AMPK enhances mPer2 degradation and CKIɛ activity by phosphorylating Ser-389 of CKIɛ. One of the regulators of the period length is casein kinase Iepsilon (CKIepsilon), which by phosphorylating and inducing the degradation of the circadian clock component, mPer2, shortens the period length. AMPK phosphorylates Ser-389 of CKIepsilon, resulting in increased CKIepsilon activity and degradation of mPer2.

Identifier	Residue	Organism
SIGNOR-267995		Mus musculus
pmid	sentence
15767683	The mammalian circadian regulatory proteins PER1 and PER2 undergo a daily cycle of accumulation followed by phosphorylation and degradation. CKIepsilon-mediated phosphorylation of PER2 recruits the ubiquitin ligase adapter protein beta-TrCP to a specific site, and dominant negative beta-TrCP blocks phosphorylation-dependent degradation of mPER2. These results provide a biochemical mechanism and functional relevance for the observed phosphorylation-degradation cycle of mammalian PER2.

Publications:

3

Organism:

In Vitro, Mus Musculus

Pathways:

Circadian clock

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

Pathways:

Circadian clock

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

Identifier	Residue	Sequence
SIGNOR-274047	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

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

Identifier	Residue	Organism
SIGNOR-267996		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

Identifier	Residue	Organism	Cell Line
SIGNOR-273763		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

Identifier	Residue	Organism
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

Pathways:

Circadian clock

Identifier	Residue	Organism
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

Identifier	Residue	Organism	Cell Line
SIGNOR-273761		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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	Organism	Cell Line
SIGNOR-273764		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

Identifier	Residue	Organism	Cell Line
SIGNOR-273762		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

Identifier	Residue	Organism
SIGNOR-110053		Homo sapiens
pmid	sentence
11524435	Cki-7, an inhibitor of ck1epsilon

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-267997		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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Name	CSNK1E View Modifications
Full Name	Casein kinase I isoform epsilon
Synonyms	CKI-epsilon, CKIe
Primary ID	P49674
Links	- -
Type	protein
Relations	59
Pathways	Circadian clock, YAP/TAZ regulation
Inhibitors	N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide
Function	Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates DVL1 and DVL2. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation.

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