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CK1-E (human)

Overview CK1-E an ubiquitous protein kinase of the CK1 family. Together with Dvl-1 and Frat-1 activate the Wnt signaling pathway. Central component of the circadian clock. May act as a negative regulator of circadian rhythmicity by phosphorylating PER1 and PER2. May play a role in cell cycle progression. Two splice variant isoforms have been described. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK, or NPAS2, BMAL1 or BMAL2, CK1-D and/or CK1-E, TIMELESS and the PER proteins. Interacts directly with PER1 and PER2 which may lead to their degradation. Interacts with SOCS3. Mutations in hamster and Drosophila orthologs have circadian rhythm phenotypes, and the circadian gene period (per) is a substrate in both human and fly. A coding SNP variant in human, which increases CK1 activity, is negatively associated with circadian disorder. LOF mutations and LOH seen in mammary ductal carcinoma. Note: This description may include information from UniProtKB. Protein type: Protein kinase, Ser/Thr (non-receptor); Protein kinase, CK1; Kinase, protein; EC 2.7.11.1; CK1 group; CK1 family Cellular Component: cytosol; nucleus; ribonucleoprotein complex Molecular Function: protein serine/threonine kinase activity; protein binding; ATP binding; protein kinase activity Biological Process: negative regulation of Wnt receptor signaling pathway; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; mitotic cell cycle; signal transduction; DNA repair; G2/M transition of mitotic cell cycle; protein amino acid phosphorylation Reference #:  P49674 (UniProtKB) Alt. Names/Synonyms: casein kinase 1, epsilon; Casein kinase I isoform epsilon; CKI-epsilon; CKIe; CSNK1E; HCKIE; KC1E; MGC10398 Gene Symbols: CSNK1E Molecular weight: 47,315 Da Basal Isoelectric point: 9.68  Predict pI for various phosphorylation states CST Pathways:  Hedgehog Signaling  |  Hippo Signaling  |  Wnt/ß-Catenin Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below CK1-E 4HNI - A/B=1-294 (human) 4HOK - S/A/O/W/K/E/Q/M/C/I/G/U=1-294 (human) Substrate Sequence Logo

STRING  |  Scansite  |  KinBase  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 4HNI 4HOK  |  ENZYME  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
transcription, altered: S389‑p enzymatic activity, induced: T44‑p enzymatic activity, inhibited: S323‑p, T325‑p, T334‑p, T337‑p, S368‑p, S405‑p, T407‑p, S408‑p protein degradation: S389‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		S17-p	RLGRKIGsGSFGDIY
1	0		T44-p	IKLECVKtKHPQLHI
0	2		K140-u	NFLMGLGkKGNLVYI
0	1		K242-a	TPIEVLCkGYPSEFS
0	2		K263-u	RSLRFDDkPDYSYLR
2	2		S323-p	RMGQLRGsAtRALPP
2	1		T325-p	GQLRGsAtRALPPGP
2	0		T334-p	ALPPGPPtGAtANRL
2	0		T337-p	PGPPtGAtANRLRsA
0	3		S343-p	AtANRLRsAAEPVAs
0	2		S350-p	sAAEPVAstPAsRIQ
0	11		T351-p	AAEPVAstPAsRIQP
0	4		S354-p	PVAstPAsRIQPAGN
0	1		T362-p	RIQPAGNtsPRAIsR
0	15		S363-p	IQPAGNtsPRAIsRV
2	0		S368-p	NtsPRAIsRVDRERK
0	6		S377-p	VDRERKVsMRLHRGA
0	2		R382	KVsMRLHRGAPANVs
1	19		S389-p	RGAPANVsssDLtGR
0	1		S390-p	GAPANVsssDLtGRQ
0	5		S391-p	APANVsssDLtGRQE
0	6		T394-p	NVsssDLtGRQEVsR
0	1		S400-p	LtGRQEVsRIPAsQt
2	7		S405-p	EVsRIPAsQtsVPFD
2	2		T407-p	sRIPAsQtsVPFDHL
2	15		S408-p	RIPAsQtsVPFDHLG

	mouse
S17	RLGRKIGSGSFGDIY
T44	IKLECVKTKHPQLHI
K140-u	NFLMGLGkKGNLVYI
K242	TPIEVLCKGYPSEFS
K263-u	RSLRFDDkPDYSYLR
S323	RMGQLRGSATRALPP
T325	GQLRGSATRALPPGP
T334	ALPPGPPTGATANRL
T337	PGPPTGATANRLRSA
S343	ATANRLRSAAEPVAS
S350	SAAEPVASTPASRIQ
T351	AAEPVASTPASRIQQ
S354	PVASTPASRIQQTGN
T362	RIQQTGNTsPRAISR
S363-p	IQQTGNTsPRAISRA
S368	NTsPRAISRADRERK
S377	ADRERKVSMRLHrGA
R382-m1	KVSMRLHrGAPANVS
S389	rGAPANVSSSDLTGR
S390	GAPANVSSSDLTGRQ
S391	APANVSSSDLTGRQE
T394	NVSSSDLTGRQEVSR
S400	LTGRQEVSRLAAsQt
S405-p	EVSRLAAsQtsVPFD
T407-p	SRLAAsQtsVPFDHL
S408-p	RLAAsQtsVPFDHLG

	rat
S17	RLGRKIGSGSFGDIY
T44	IKLECVKTKHPQLHI
K140	NFLMGLGKKGNLVYI
K242	TPIEVLCKGYPSEFS
K263	RSLRFDDKPDYSYLR
S323	RMGQLRGSATRALPP
T325	GQLRGSATRALPPGP
T334	ALPPGPPTGATANRL
T337	PGPPTGATANRLRSA
S343	ATANRLRSAAEPVAS
S350	SAAEPVASTPASRIQ
T351	AAEPVASTPASRIQQ
S354	PVASTPASRIQQAGN
T362	RIQQAGNTSPRAISR
S363	IQQAGNTSPRAISRA
S368	NTSPRAISRADRERK
S377	ADRERKVSMRLHRGA
R382	KVSMRLHRGAPANVS
S389	RGAPANVSSSDLTGR
S390	GAPANVSSSDLTGRQ
S391	APANVSSSDLTGRQE
T394	NVSSSDLTGRQEVSR
S400	LTGRQEVSRIAASQT
S405	EVSRIAASQTSVPFD
T407	SRIAASQTSVPFDHL
S408	RIAASQTSVPFDHLG

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