Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-64258	Ser100	ESEDSQEsVDSVTDS	Homo sapiens
pmid	sentence
9931297	Ser108, ser111 and ser114, located in a region matching the consensus sequence for the casein kinase ii target, were required.These results strongly suggest that the casein kinase ii target region is involved in cell cycle-regulated phosphorylation of the creb protein and also in transcriptional enhancement.

Identifier	Residue	Sequence	Organism
SIGNOR-64250	Ser94	QISTIAEsEDSQESV	Homo sapiens
pmid	sentence
9931297	Ser108, ser111 and ser114, located in a region matching the consensus sequence for the casein kinase ii target, were required.These results strongly suggest that the casein kinase ii target region is involved in cell cycle-regulated phosphorylation of the creb protein and also in transcriptional enhancement.

Publications:

2

Organism:

Homo Sapiens

Pathways:

WNT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-250789	Ser12	FSLHDALsGSGNPNP	in vitro
pmid	sentence
8253806	L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-73795	Ser129	NEAYEMPsEEGYQDY	Homo sapiens
pmid	sentence
10617630	In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2.\| together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of alpha-synuclein could affect its binding to membranes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276261	Ser1359	VPRPHVQsVLLTPQD	Homo sapiens	HEK-293T Cell
pmid	sentence
19797085	We show that the beta-TrCP-mediated degradation requires phosphorylation of PHLPP1 by casein kinase I and glycogen synthase kinase 3beta (GSK-3beta), and activation of the phosphatidylinositol 3-kinase/Akt pathway suppresses the degradation of PHLPP1 by inhibiting the GSK-3beta activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276262	Thr1363	HVQSVLLtPQDEFFI	Homo sapiens	HEK-293T Cell
pmid	sentence
19797085	We show that the beta-TrCP-mediated degradation requires phosphorylation of PHLPP1 by casein kinase I and glycogen synthase kinase 3beta (GSK-3beta), and activation of the phosphatidylinositol 3-kinase/Akt pathway suppresses the degradation of PHLPP1 by inhibiting the GSK-3beta activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275966	Ser159	GIPVRCYsAEVVTLW	in vitro
pmid	sentence
10500146	We also show that casein kinase I, but not casein kinase II, can phosphorylate and activate cdk5 in vitro. Ser(159) in cdk5 is homologous to the regulatory Thr(160) in cdk2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273618	Ser18	EDSDDNGsLSTTWSQ	Homo sapiens	HEK-293 Cell
pmid	sentence
25100726	We demonstrate that the destruction complex component casein kinase 1α (CK1α) phosphorylates Jade-1 at a conserved SLS motif and reduces the ability of Jade-1 to inhibit β-catenin signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273617	Ser20	SDDNGSLsTTWSQNS	Homo sapiens	HEK-293 Cell
pmid	sentence
25100726	We demonstrate that the destruction complex component casein kinase 1α (CK1α) phosphorylates Jade-1 at a conserved SLS motif and reduces the ability of Jade-1 to inhibit β-catenin signaling.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-179255	Ser185	ALQKRYGsQNGCINC	Homo sapiens	HeLa Cell
pmid	sentence
18590726	Mass spectrometry analysis demonstrates that rhob is monophosphorylated by ck1, in its c-terminal end, on serine 185. lastly we show that the inhibition of ck1 activates rhob and promotes rhob dependent actin fiber formation and egf-r level.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250790	Ser19	EVCDERTsLMSAESP	in vitro
pmid	sentence
8972483	In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-250791	Ser7	sDSEEEVC	in vitro
pmid	sentence
8972483	In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-250792	Ser9	LTFMASDsEEEVCDE	in vitro
pmid	sentence
8972483	In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-154386	Ser19	MIPKSSFsINSLVPE	Homo sapiens	Neuron
pmid	sentence
17435750	Cki phosphorylation of ser 19 of foxg1 promotes nuclear import

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-139307	Ser194	QNRSGAMsPMSWNSD	Homo sapiens
pmid	sentence
16061179	FADD is essential for death receptor (DR)-induced apoptosis.\|Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-162648	Ser20	PLSQETFsDLWKLLP	Homo sapiens
pmid	sentence
20041275	Our data support the concept that non-primed phosphorylation of p53 by ck1 is an isoform-specific reaction preferentially affecting s20

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-109800	Ser207	AARFTLGsPLTSPGG	Homo sapiens	BHK Cell
pmid	sentence
9630228	Dominant-negative cki? Induces nuclear import of nf-at4these results demonstrated that the cki? Phosphorylation sites identified in vitro were also specifically phosphorylated by cki? In vivo, and that these residues were crucial for the masking of the nls of nf-at4.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-109763	Ser211	TLGSPLTsPGGSPGG	Homo sapiens	BHK Cell
pmid	sentence
9630228	Dominant-negative cki alpha Induces nuclear import of nf-at4 these results demonstrated that the cki alpha Phosphorylation sites identified in vitro were also specifically phosphorylated by cki alpha In vivo, and that these residues were crucial for the masking of the nls of nf-at4.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-109781	Ser215	PLTSPGGsPGGCPGE	Homo sapiens	BHK Cell
pmid	sentence
9630228	Dominant-negative cki alpha Induces nuclear import of nf-at4 these results demonstrated that the cki alpha Phosphorylation sites identified in vitro were also specifically phosphorylated by cki alpha In vivo, and that these residues were crucial for the masking of the nls of nf-at4.

Identifier	Residue	Sequence	Organism
SIGNOR-109768	Thr204	NEAAARFtLGSPLTS	Homo sapiens
pmid	sentence
9630228	Dominant-negative cki alpha Induces nuclear import of nf-at4 these results demonstrated that the cki alpha Phosphorylation sites identified in vitro were also specifically phosphorylated by cki alpha In vivo, and that these residues were crucial for the masking of the nls of nf-at4.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-109776	Thr210	FTLGSPLtSPGGSPG	Homo sapiens	BHK Cell
pmid	sentence
9630228	Dominant-negative cki alpha Induces nuclear import of nf-at4 these results demonstrated that the cki alpha Phosphorylation sites identified in vitro were also specifically phosphorylated by cki alpha In vivo, and that these residues were crucial for the masking of the nls of nf-at4.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273621	Ser209	RWRGSCSsGNSQRRS	Homo sapiens	HEK-293 Cell
pmid	sentence
30686098	Interestingly, ZRANB1 is phosphorylated at Thr35, and Ser209 residues by CSNK1A1, and this phosphorylation activates its deubiquitinating activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273620	Thr35	RAQRPSGtIITEDPF	Homo sapiens	HEK-293 Cell
pmid	sentence
30686098	Interestingly, ZRANB1 is phosphorylated at Thr35, and Ser209 residues by CSNK1A1, and this phosphorylation activates its deubiquitinating activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250795	Ser232	LTLWTSDsAGEECDA	in vitro
pmid	sentence
9360956	This protein kinase has been identified as casein kinase Ialpha (CKIalpha) by peptide mapping analysis and sequencing. Among mammalian 14-3-3, only 14-3-3 tau possesses a phosphorylatable residue at the same position (Ser-233), and we show that this residue is also phosphorylated by CKI. In addition, we show that 14-3-3 zeta is exclusively phosphorylated on Thr-233 in human embryonic kidney 293 cells. The residue 233 is located within a region shown to be important for the association of 14-3-3 to target proteins.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-133528	Ser253	ETNVKMEsEGGADDS	Homo sapiens
pmid	sentence
15687492	A kinase activity was identified in mouse liver that phosphorylates the acd of hnrnp-c at ser(240) and at two sites at ser(225)-ser(228). The kinase was purified and identified by tandem mass spectrometry as protein kinase ck1alpha (formerly casein kinase 1alpha).hnrnp-c1 that was also modified at the ck1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that ck1alpha-mediated phosphorylation modulates the mrna binding ability of hnrnp-c.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-133532	Ser260	SEGGADDsAEEGDLL	Homo sapiens
pmid	sentence
15687492	In contrast, hnRNP-C1 that was also modified at the CK1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C.

Identifier	Residue	Sequence	Organism
SIGNOR-133536	Ser299	EGEDDRDsANGEDDS	Homo sapiens
pmid	sentence
15687492	In contrast, hnRNP-C1 that was also modified at the CK1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-176871	Ser286	SSMSSCGsSGYFSSS	Homo sapiens
pmid	sentence
22017877	Phosphorylation of all three serine residues in the deptor degron (ser286, ser287, and ser291) is necessary for - and directly mediates - the interaction with _trcp. ck1 phosphorylated the degron of deptor, as shown by western blotting with the phospho-specific antibody (fig. S3e-f). In contrast, mtor alone was unable to induce phosphorylation of deptor on ser286, ser287, and ser291.

Identifier	Residue	Sequence	Organism
SIGNOR-176875	Ser287	SMSSCGSsGYFSSSP	Homo sapiens
pmid	sentence
22017877	Phosphorylation of all three serine residues in the deptor degron (ser286, ser287, and ser291) is necessary for - and directly mediates - the interaction with _trcp. ck1 phosphorylated the degron of deptor, as shown by western blotting with the phospho-specific antibody (fig. S3e-f). In contrast, mtor alone was unable to induce phosphorylation of deptor on ser286, ser287, and ser291.

Identifier	Residue	Sequence	Organism
SIGNOR-176879	Ser291	CGSSGYFsSSPTLSS	Homo sapiens
pmid	sentence
22017877	Phosphorylation of all three serine residues in the deptor degron (ser286, ser287, and ser291) is necessary for - and directly mediates - the interaction with _trcp. ck1 phosphorylated the degron of deptor, as shown by western blotting with the phospho-specific antibody (fig. S3e-f). In contrast, mtor alone was unable to induce phosphorylation of deptor on ser286, ser287, and ser291.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-199015	Ser289	DDLEDSKsLSDDTDV	Homo sapiens
pmid	sentence
23028042	Previous studies showed that casein kinase 1? (ck1?) Stably associates with mdmx, stimulates mdmx-p53 binding, and cooperates with mdmx to inactivate p53ck1? Binding to the mdmx central domain and phosphorylation of s289 disrupts the intramolecular interaction, allowing the n terminus to bind p53 with increased affinity. After dna damage, the mdmx-ck1? Complex is disrupted by chk2-mediated phosphorylation of mdmx at s367, leading to reduced mdmx-p53 binding.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252899	Ser318	SRTNSNAsTVSGRLS	Homo sapiens
pmid	sentence
20110348	Casein kinase (ck) 1 mediates the hierarchical phosphorylation of foxo3a at s318 and s321, which like foxo1 (rena et al., 2002 blue right-pointing triangle, 2004 blue right-pointing triangle), is probably to enhance its rate of nuclear export

Identifier	Residue	Sequence	Organism
SIGNOR-252900	Ser321	NSNASTVsGRLSPIM	Homo sapiens
pmid	sentence
20110348	Casein kinase (ck) 1 mediates the hierarchical phosphorylation of foxo3a at s318 and s321, which like foxo1 (rena et al., 2002 blue right-pointing triangle, 2004 blue right-pointing triangle), is probably to enhance its rate of nuclear export

Identifier	Residue	Organism
SIGNOR-252898		Homo sapiens
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163672	Ser318	SRTNSNAsTVSGRLS	Homo sapiens
pmid	sentence
20110348	Casein kinase (ck) 1 mediates the hierarchical phosphorylation of foxo3a at s318 and s321, which like foxo1 (rena et al., 2002 blue right-pointing triangle, 2004 blue right-pointing triangle), is probably to enhance its rate of nuclear export

Identifier	Residue	Sequence	Organism
SIGNOR-163676	Ser321	NSNASTVsGRLSPIM	Homo sapiens
pmid	sentence
20110348	Casein kinase (ck) 1 mediates the hierarchical phosphorylation of foxo3a at s318 and s321, which like foxo1 (rena et al., 2002 blue right-pointing triangle, 2004 blue right-pointing triangle), is probably to enhance its rate of nuclear export

Identifier	Residue	Organism	Cell Line
SIGNOR-183661		Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273769	Ser349	SSKEVDPsTGELQSL	Mus musculus
pmid	sentence
37723657	Mechanistically, CSNK1A1 interacted with STING1 upon the CGAS-STING1 pathway activation and promoted STING1 autophagic degradation by enhancing the phosphorylation of SQSTM1/p62 at serine 351 (serine 349 in human), which was critical for SQSTM1-mediated STING1 autophagic degradation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-165022	Ser45	GATTTAPsLSGKGNP	Homo sapiens
pmid	sentence
20419129	Specifically, ck1_ phosphorylates _-catenin at s45, which primes this n-terminal region for subsequent phosphorylations by gsk3 at t41, s37 and s33 [7]. These latter two phosphorylations are recognized by the e3-ligase component, _-trcp, for ultimate ubiquitylation and destruction by the proteosome

Publications:

1

Organism:

Homo Sapiens

Pathways:

Wnt in cancer, WNT Signaling, WNT/FLT3

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250787	Ser466	DEDDGEFsDDSGADQ	Homo sapiens	HEK-293 Cell
pmid	sentence
11500362	The fifth site, which lies outside the catalytic domain of eIF2Bepsilon, can be phosphorylated by casein kinase 1. All five sites are phosphorylated in the eIF2B complex in vivo. \| A phosphopeptide corresponding to this region was identified in Asp‐N digests of eIF2Bϵ phosphorylated in vitro by CK1, suggesting that Ser461 or Ser464 may be phosphorylated by this kinase in vivo.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250788	Ser469	DGEFSDDsGADQEKD	Homo sapiens	HEK-293 Cell
pmid	sentence
11500362	The fifth site, which lies outside the catalytic domain of eIF2Bepsilon, can be phosphorylated by casein kinase 1. All five sites are phosphorylated in the eIF2B complex in vivo. \| A phosphopeptide corresponding to this region was identified in Asp‐N digests of eIF2Bϵ phosphorylated in vitro by CK1, suggesting that Ser461 or Ser464 may be phosphorylated by this kinase in vivo.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249192	Ser469	AHEENPEsILDEHVQ	in vitro
pmid	sentence
17318175	Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.\|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling.

Identifier	Residue	Sequence	Organism
SIGNOR-249189	Ser75	LGYEPEGsASPTPPY	in vitro
pmid	sentence
17318175	Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.\|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling.

Identifier	Residue	Sequence	Organism
SIGNOR-249191	Ser77	YEPEGSAsPTPPYLK	in vitro
pmid	sentence
17318175	Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.\|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275460	Ser497	SRTVSASsTGDLPKA	Homo sapiens	HEK-293 Cell
pmid	sentence
29153836	Here, we demonstrate that mTORC1 promotes lipid biogenesis via SRPK2, a key regulator of RNA-binding SR proteins. mTORC1-activated S6K1 phosphorylates SRPK2 at Ser494, which primes Ser497 phosphorylation by CK1. These phosphorylation events promote SRPK2 nuclear translocation and phosphorylation of SR proteins.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250794	Ser511	PIGEDEEsESD	in vitro
pmid	sentence
9045708	Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells.

Identifier	Residue	Sequence	Organism
SIGNOR-250793	Ser513	GEDEESEsD	in vitro
pmid	sentence
9045708	Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-167623	Ser568	LSSSDRYsDASDDSF	Homo sapiens
pmid	sentence
20739275	Hctps2 ser(568) was phosphorylated by casein kinase 1 both in vitro and in vivo. Mutation of ser(568) (s568a) significantly increased hctps2 activity, demonstrating that ser(568) is a major inhibitory phosphorylation site.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273619	Ser6	sDVESLPR	Homo sapiens	HEK-293 Cell
pmid	sentence
26138484	We identified a phosphorylated residue (serine 6, S6) on Star-PAP in the zinc finger region, the domain required for PIPKIα interaction. We show that S6 is phosphorylated by CKIα within the nucleus which is required for Star-PAP nuclear retention and interaction with PIPKIα.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124583	Ser6	sLHDALSG	Homo sapiens	Breast Cancer Cell
pmid	sentence
15121858	These results indicate that phosphorylation of gal-3 promotes its nuclear export after apoptotic stimuli through enhanced nuclear export.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250785	Ser64	LQTDGNRsSHSRLGR	Homo sapiens	HeLa Cell
pmid	sentence
11583622	Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. \| These results suggest that residues S61, S64, and to a much lesser extent T58 are sites of phosphorylation of Bid.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250786	Thr59	EGYDELQtDGNRSSH	Homo sapiens	HeLa Cell
pmid	sentence
11583622	Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. \| These results suggest that residues S61, S64, and to a much lesser extent T58 are sites of phosphorylation of Bid.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249185	Ser77	SSTDSYSsAASYTDS	Chlorocebus aethiops
pmid	sentence
17635105	Residue 68 resides in a consensus phosphorylation site for PKD (Figure 1A) [22,23]. Interestingly, phosphorylation of Ser68 could allow for subsequent phosphorylation of Ser71, Ser74, Ser77 and Ser80 by CK1, for which the consensus phosphorylation site is pS/T-X-X-S/T

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-164734	Ser79	QRMGSSEsTDSGFCL	Homo sapiens
pmid	sentence
20348946	Here, we report that casein kinase 1 alpha (ck1alpha) phosphorylates cdc25a on both s79 and s82 in a hierarchical manner requiring prior phosphorylation of s76 by chk1 or gsk-3beta. This facilitates beta-trcp binding and ubiquitin-mediated proteolysis of cdc25a

Identifier	Residue	Sequence	Organism
SIGNOR-164738	Ser82	GSSESTDsGFCLDSP	Homo sapiens
pmid	sentence
20348946	Here, we report that casein kinase 1 alpha (ck1alpha) phosphorylates cdc25a on both s79 and s82 in a hierarchical manner requiring prior phosphorylation of s76 by chk1 or gsk-3beta. This facilitates beta-trcp binding and ubiquitin-mediated proteolysis of cdc25a

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-274045	Ser844	GSGSEAAsLSSLNSS
pmid	sentence
17353278	Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts\|CK1 colocalizes with E-cadherin and phosphorylates the cytoplasmic domain of E-cadherin in vitro and in a cell culture system. We show that the major CK1 phosphorylation site of E-cadherin is serine 846

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-73799	Ser87	KTVEGAGsIAAATGF	Homo sapiens	Neuron
pmid	sentence
10617630	In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2. These data demonstrate that alpha-synuclein is constitutively phosphorylated within its c terminus and may indicate that the function of alpha-synuclein is regulated by phosphorylation/dephosphorylation.From these data we conclude that _-synuclein is predominantly phosphorylated at serine residue 129. However, a second serine at position 87 is also used for phosphorylation to some extent. together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of _-synuclein could affect its binding to membranes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-64254	Ser97	TIAESEDsQESVDSV	Homo sapiens
pmid	sentence
9931297	Ser108, ser111 and ser114, located in a region matching the consensus sequence for the casein kinase ii target, were required.These results strongly suggest that the casein kinase ii target region is involved in cell cycle-regulated phosphorylation of the creb protein and also in transcriptional enhancement.

Publications:

1

Organism:

Homo Sapiens

Pathways:

WNT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-143034	Thr1493	NPPPSPAtERSHYTM	Homo sapiens
pmid	sentence
16341017	We show that wnt induces sequential phosphorylation of lrp6 by gsk3 and casein kinase 1, and this dual phosphorylation promotes the engagement of lrp6 with the scaffolding protein axin.Site ii, like site i, was phosphorylated, as detected by means of a phospho-specific antibody (ab1493, for phosphorylated t1493 in lrp6)

Identifier	Residue	Organism
SIGNOR-143037		Homo sapiens
pmid	sentence
16341017	We show that wnt induces sequential phosphorylation of lrp6 by gsk3 and casein kinase 1, and this dual phosphorylation promotes the engagement of lrp6 with the scaffolding protein axin.

Publications:

2

Organism:

Homo Sapiens

Pathways:

WNT Signaling, WNT/FLT3

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250796	Thr232	LTLWTSDtQGDEAEA	Homo sapiens	HEK-293 Cell
pmid	sentence
9360956	This protein kinase has been identified as casein kinase Ialpha (CKIalpha) by peptide mapping analysis and sequencing. Among mammalian 14-3-3, only 14-3-3 tau possesses a phosphorylatable residue at the same position (Ser-233), and we show that this residue is also phosphorylated by CKI. In addition, we show that 14-3-3 zeta is exclusively phosphorylated on Thr-233 in human embryonic kidney 293 cells. The residue 233 is located within a region shown to be important for the association of 14-3-3 to target proteins. \| We have now shown that in vivo phosphorylation of 14-3-3 zeta at the CKIalpha site (Thr-233) negatively regulates its binding to c-Raf, and may be important in Raf-mediated signal transduction.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-116512		Homo sapiens
pmid	sentence
11955435	In principle, pka, ck-1 and gsk3 can phosphorylate as many as 19 serine residues in gli3: fourpkasites, three primarygsk3sites, four primary ck-1 sites and eight secondary gsk3 and ck-1 sites

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273746		Homo sapiens	HEK-293 Cell
pmid	sentence
29789297	We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273745		Homo sapiens	HEK-293 Cell
pmid	sentence
29789297	We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-227967		Homo sapiens
pmid	sentence
22083140	In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)]

Identifier	Residue	Organism
SIGNOR-227964		Homo sapiens
pmid	sentence
19293931	In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)]

Publications:

2

Organism:

Homo Sapiens

Pathways:

Wnt in cancer, WNT Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264877
pmid	sentence
30925160	CK1a1, JNK1 and CDK1 had the highest site-specific activity for ORP4L, while CDK1, GSK3a, CK1a1 and GSK3b showed the highest specificity for the site when corrected for background activity with ORP4L-S4A. Because of the complexity of the serine/proline-rich site, we did not determine which serine(s) in ORP4L were phosphorylated by candidate kinases.\|We conclude that phosphorylation of a unique serine/proline motif in the ORD induces a conformation change in ORP4L that enhances interaction with vimentin and cholesterol extraction from membranes.

Publications:

1

Identifier	Residue	Organism	Cell Line
SIGNOR-183658		Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity

Publications:

1

Organism:

Homo Sapiens

Pathways:

WNT/FLT3

Identifier	Residue	Organism	Cell Line
SIGNOR-236895		Homo sapiens	KG-1 Cell
pmid	sentence
26131937	We demonstrate that lenalidomide induces the ubiquitination of casein kinase 1A1 (CK1a) by the E3 ubiquitin ligase CUL4RBX1DDB1CRBN (known as CRL4CRBN)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-174542		Homo sapiens
pmid	sentence
21695114	We demonstrate that mammalian Smo (mSmo) is activated through multi-site phosphorylation of its carboxyl-terminal tail by CK1α and GRK2. Phosphorylation of mSmo induces its active conformation and simultaneously promotes its ciliary accumulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-183667		Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-184696		Homo sapiens
pmid	sentence
19293931	In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)]

Identifier	Residue	Organism
SIGNOR-177233		Homo sapiens
pmid	sentence
22083140	In the absence of secreted wnt ligands, cytosolic beta-catenin is phosphorylated at ser45 by the priming kinase casein kinase 1 (ck1). Consequently, glycogen synthase kinase 3 (gsk3), in complex with axin and adenomatous polyposis coli (apc), phosphorylates beta-catenin at thr41, ser37, and ser33 apc cooperates with axin to promote the phosphorylation of b-catenin by gsk3 [which requires priming phosphorylation by casein kinase 1, alpha-isoform (ck1alpha)]

Publications:

2

Organism:

Homo Sapiens

Pathways:

WNT/FLT3

Identifier	Residue	Organism
SIGNOR-146112		Homo sapiens
pmid	sentence
16611981	Gli2 can also be phosphorylated directly by ck-1 at the non-optimal sites

Identifier	Residue	Organism
SIGNOR-154222		Homo sapiens
pmid	sentence
17419683	In the absence of hedgehog signaling, gli1 is transcriptionally repressed, gli2 is phosphorylated by gsk3 and ck1 for the fbxw11 (betatrcp2)-mediated degradation, and gli3 is processed to a cleaved repressor.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273748		Homo sapiens	HEK-293 Cell
pmid	sentence
29789297	We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273749		Homo sapiens	HEK-293 Cell
pmid	sentence
29789297	We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273750		Homo sapiens	HEK-293 Cell
pmid	sentence
29789297	We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-183664		Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-236907		Homo sapiens	KG-1 Cell
pmid	sentence
26131937	We demonstrate that lenalidomide induces the ubiquitination of casein kinase 1A1 (CK1a) by the E3 ubiquitin ligase CUL4RBX1DDB1CRBN (known as CRL4CRBN)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273752		Homo sapiens	HEK-293 Cell
pmid	sentence
29789297	We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273751		Homo sapiens	HEK-293 Cell
pmid	sentence
29789297	We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-273747		Homo sapiens	HEK-293 Cell
pmid	sentence
29789297	We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates.

Publications:

1

Organism:

Homo Sapiens

Name	CSNK1A1 View Modifications
Full Name	Casein kinase I isoform alpha
Synonyms	CKI-alpha, CK1
Primary ID	P48729
Links	- -
Type	protein
Relations	83
Pathways	Wnt in cancer, WNT Signaling, WNT/FLT3
Function	Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis (PubMed:11955436, PubMed:1409656, PubMed:18305108). May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration (PubMed:23902688).

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