dbPTM

KC1E_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KC1E_HUMAN
UniProt AC	P49674
Protein Name	Casein kinase I isoform epsilon
Gene Name	CSNK1E
Organism	Homo sapiens (Human).
Sequence Length	416
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	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..
Protein Sequence	MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGAARNPEDVDRERREHEREERMGQLRGSATRALPPGPPTGATANRLRSAAEPVASTPASRIQPAGNTSPRAISRVDRERKVSMRLHRGAPANVSSSDLTGRQEVSRIPASQTSVPFDHLGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	RLGRKIGSGSFGDIY ECCCEECCCCCCCEE	34.43	-
44	Phosphorylation	IKLECVKTKHPQLHI EEEEEHHCCCCCEEH	17.75	20507565
45	Ubiquitination	KLECVKTKHPQLHIE EEEEHHCCCCCEEHH	47.79	-
54	Ubiquitination	PQLHIESKFYKMMQG CCEEHHHHHHHHHCC	39.66	-
57	Ubiquitination	HIESKFYKMMQGGVG EHHHHHHHHHCCCCC	30.91	-
67	Phosphorylation	QGGVGIPSIKWCGAE CCCCCCCCCCCCCCC	34.57	24719451
122	Ubiquitination	RIEYIHSKNFIHRDV HHHHHHHCCCCCCCC	41.54	2189047
130	Ubiquitination	NFIHRDVKPDNFLMG CCCCCCCCCCCEEEC	51.44	21890473
140	Ubiquitination	NFLMGLGKKGNLVYI CEEECCCCCCCEEEE	63.65	21906983
141	Ubiquitination	FLMGLGKKGNLVYII EEECCCCCCCEEEEE	51.76	-
146	Phosphorylation	GKKGNLVYIIDFGLA CCCCCEEEEEECCCC	8.70	29496907
171	Ubiquitination	HIPYRENKNLTGTAR CCCCCCCCCCCCEEE	48.89	-
179	Phosphorylation	NLTGTARYASINTHL CCCCEEEEEEHHHHC	11.39	29496907
181	Phosphorylation	TGTARYASINTHLGI CCEEEEEEHHHHCCC	13.87	28857561
184	Phosphorylation	ARYASINTHLGIEQS EEEEEHHHHCCCCCH	19.46	30576142
232	Ubiquitination	YERISEKKMSTPIEV HHHHHHCCCCCCHHH	33.75	-
234	Phosphorylation	RISEKKMSTPIEVLC HHHHCCCCCCHHHHC	39.65	20068231
235	Phosphorylation	ISEKKMSTPIEVLCK HHHCCCCCCHHHHCC	25.45	29978859
242	Acetylation	TPIEVLCKGYPSEFS CCHHHHCCCCCHHHH	58.27	130647
244	Phosphorylation	IEVLCKGYPSEFSTY HHHHCCCCCHHHHHH	6.78	29978859
246	Phosphorylation	VLCKGYPSEFSTYLN HHCCCCCHHHHHHHH	42.67	29978859
249	Phosphorylation	KGYPSEFSTYLNFCR CCCCHHHHHHHHHHH	16.46	29978859
250	Phosphorylation	GYPSEFSTYLNFCRS CCCHHHHHHHHHHHH	37.03	29978859
251	Phosphorylation	YPSEFSTYLNFCRSL CCHHHHHHHHHHHHC	9.84	29496907
263	Ubiquitination	RSLRFDDKPDYSYLR HHCCCCCCCCHHHHH	41.45	21890473
266	Phosphorylation	RFDDKPDYSYLRQLF CCCCCCCHHHHHHHH	14.03	-
267	Phosphorylation	FDDKPDYSYLRQLFR CCCCCCHHHHHHHHH	25.68	29496907
284	Phosphorylation	FHRQGFSYDYVFDWN HHHCCCCCEEEEEHH	14.72	29496907
286	Phosphorylation	RQGFSYDYVFDWNML HCCCCCEEEEEHHHH	8.52	29496907
321	Methylation	EERMGQLRGSATRAL HHHHHHHCCCCCCCC	29.18	-
323	Phosphorylation	RMGQLRGSATRALPP HHHHHCCCCCCCCCC	21.74	23927012
325	Phosphorylation	GQLRGSATRALPPGP HHHCCCCCCCCCCCC	20.40	23927012
334	Phosphorylation	ALPPGPPTGATANRL CCCCCCCCCHHHHHH	42.45	22817900
337	Phosphorylation	PGPPTGATANRLRSA CCCCCCHHHHHHHHC	26.30	22817900
342	Methylation	GATANRLRSAAEPVA CHHHHHHHHCCCCCC	22.47	-
343	Phosphorylation	ATANRLRSAAEPVAS HHHHHHHHCCCCCCC	36.10	21082442
350	Phosphorylation	SAAEPVASTPASRIQ HCCCCCCCCCHHHCC	34.85	21712546
351	Phosphorylation	AAEPVASTPASRIQP CCCCCCCCCHHHCCC	17.09	21712546
354	Phosphorylation	PVASTPASRIQPAGN CCCCCCHHHCCCCCC	30.99	26055452
362	Phosphorylation	RIQPAGNTSPRAISR HCCCCCCCCHHHHHH	38.91	29255136
363	Phosphorylation	IQPAGNTSPRAISRV CCCCCCCCHHHHHHH	19.18	29255136
368	Phosphorylation	NTSPRAISRVDRERK CCCHHHHHHHHHHHH	25.85	26074081
377	Phosphorylation	VDRERKVSMRLHRGA HHHHHHHHHHEECCC	10.96	20068231
382	Methylation	KVSMRLHRGAPANVS HHHHHEECCCCCCCC	47.78	-
389	Phosphorylation	RGAPANVSSSDLTGR CCCCCCCCHHHCCCC	24.75	29255136
390	Phosphorylation	GAPANVSSSDLTGRQ CCCCCCCHHHCCCCH	24.48	29255136
391	Phosphorylation	APANVSSSDLTGRQE CCCCCCHHHCCCCHH	29.18	29255136
394	Phosphorylation	NVSSSDLTGRQEVSR CCCHHHCCCCHHCCC	35.00	29255136
400	Phosphorylation	LTGRQEVSRIPASQT CCCCHHCCCCCCCCC	24.60	-
405	Phosphorylation	EVSRIPASQTSVPFD HCCCCCCCCCCCCCC	28.74	26055452
407	Phosphorylation	SRIPASQTSVPFDHL CCCCCCCCCCCCCCC	29.24	10542239
408	Phosphorylation	RIPASQTSVPFDHLG CCCCCCCCCCCCCCC	21.84	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
44	T	Phosphorylation	Kinase	CSNK1E	P49674	GPS
323	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
323	S	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
323	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
325	T	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
325	T	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
325	T	Phosphorylation	Kinase	CSNK1E	P49674	GPS
334	T	Phosphorylation	Kinase	CSNK1E	P49674	GPS
334	T	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
334	T	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
337	T	Phosphorylation	Kinase	CSNK1E	P49674	GPS
337	T	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
337	T	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
368	S	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
368	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
368	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
389	S	Phosphorylation	Kinase	PRKAA1	Q5EG47	GPS
389	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
405	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
405	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
405	S	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
407	T	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
407	T	Phosphorylation	Kinase	CSNK1E	P49674	GPS
407	T	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
408	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
408	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
408	S	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KC1E_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of KC1E_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DVL2_HUMAN	DVL2	physical	16189514
FSBP_HUMAN	RAD54B	physical	16189514
RA54B_HUMAN	RAD54B	physical	16189514
PER3_HUMAN	PER3	physical	14701732
PER1_HUMAN	PER1	physical	10848614
BMAL1_HUMAN	ARNTL	physical	11875063
P53_MOUSE	Trp53	physical	9349507
AXIN1_HUMAN	AXIN1	physical	11884395
DVL1_HUMAN	DVL1	physical	11818547
NCOA3_HUMAN	NCOA3	physical	21577200
CADM4_HUMAN	CADM4	physical	21900206
HES1_HUMAN	HES1	physical	21900206
TF3C1_HUMAN	GTF3C1	physical	21900206
RBX1_HUMAN	RBX1	physical	21900206
KAT7_HUMAN	KAT7	physical	21900206
TAOK1_HUMAN	TAOK1	physical	21900206
BBS10_HUMAN	BBS10	physical	21900206
ZN227_HUMAN	ZNF227	physical	21900206
PNO1_HUMAN	PNO1	physical	21900206
WDCP_HUMAN	C2orf44	physical	21900206
F110A_HUMAN	FAM110A	physical	21900206
F16P1_HUMAN	FBP1	physical	21900206
ARHG1_HUMAN	ARHGEF1	physical	21900206
FA83D_HUMAN	FAM83D	physical	21900206
CRCM_HUMAN	MCC	physical	21900206
PKCB1_HUMAN	ZMYND8	physical	21900206
MYCN_HUMAN	MYCN	genetic	22623531
DBND2_HUMAN	DBNDD2	physical	16618118
A4_HUMAN	APP	physical	21832049
SDCG3_HUMAN	SDCCAG3	physical	21988832
TNS2_HUMAN	TENC1	physical	21988832
F110A_HUMAN	FAM110A	physical	21988832
F110C_HUMAN	FAM110C	physical	21988832
TAZ_HUMAN	TAZ	physical	20858893
REST_HUMAN	REST	physical	24760862
ZSWM8_HUMAN	ZSWIM8	physical	23455922
USP9Y_HUMAN	USP9Y	physical	23455922
DVL2_HUMAN	DVL2	physical	23455922
ANM5_HUMAN	PRMT5	physical	23455922
SC16A_HUMAN	SEC16A	physical	23455922
PER1_HUMAN	PER1	physical	23455922
SAHH2_HUMAN	AHCYL1	physical	23455922
HMMR_HUMAN	HMMR	physical	23455922
MTA2_HUMAN	MTA2	physical	23455922
FARP2_HUMAN	FARP2	physical	23455922
CRCM_HUMAN	MCC	physical	23455922
KC1D_HUMAN	CSNK1D	physical	23455922
SEC13_HUMAN	SEC13	physical	23455922
WDR5_HUMAN	WDR5	physical	23455922
ACACA_HUMAN	ACACA	physical	23455922
PRDX4_HUMAN	PRDX4	physical	23455922
STK3_HUMAN	STK3	physical	23455922
CUL2_HUMAN	CUL2	physical	23455922
ELOB_HUMAN	TCEB2	physical	23455922
CRY1_HUMAN	CRY1	physical	23455922
F110C_HUMAN	FAM110C	physical	23455922
PP6R3_HUMAN	PPP6R3	physical	23455922
FA83B_HUMAN	FAM83B	physical	23455922
F199X_HUMAN	FAM199X	physical	23455922
FA83H_HUMAN	FAM83H	physical	23455922
VP13B_HUMAN	VPS13B	physical	23455922
F110B_HUMAN	FAM110B	physical	23455922
USP9X_HUMAN	USP9X	physical	23455922
SAHH3_HUMAN	AHCYL2	physical	23455922
SNX22_HUMAN	SNX22	physical	23455922
KLDC3_HUMAN	KLHDC3	physical	23455922
UN45A_HUMAN	UNC45A	physical	23455922
SAV1_HUMAN	SAV1	physical	23455922
FA83D_HUMAN	FAM83D	physical	23455922
ADA22_HUMAN	ADAM22	physical	23455922
STOX2_HUMAN	STOX2	physical	23455922
NGAP_HUMAN	RASAL2	physical	23455922
SNX24_HUMAN	SNX24	physical	23455922
DVL3_HUMAN	DVL3	physical	25416956
OCLN_HUMAN	OCLN	physical	16616143
KC1E_HUMAN	CSNK1E	physical	16616143
DEC1_HUMAN	DEC1	physical	23555304
BHE41_HUMAN	BHLHE41	physical	23555304
PER1_HUMAN	PER1	physical	23555304
PER2_HUMAN	PER2	physical	23555304
PP1G_HUMAN	PPP1CC	physical	23555304
2A5E_HUMAN	PPP2R5E	physical	23555304
RORG_HUMAN	RORC	physical	23555304
CSK2B_HUMAN	CSNK2B	physical	23555304
FBW1B_HUMAN	FBXW11	physical	23555304
NR1D2_HUMAN	NR1D2	physical	23555304
KC1E_HUMAN	CSNK1E	physical	23555304
2A5D_HUMAN	PPP2R5D	physical	23555304
RORA_HUMAN	RORA	physical	23555304
CLOCK_HUMAN	CLOCK	physical	23555304
NOB1_HUMAN	NOB1	physical	26344197
PPM1B_HUMAN	PPM1B	physical	26344197
CRY1_HUMAN	CRY1	physical	26496610
CRY2_HUMAN	CRY2	physical	26496610
CRCM_HUMAN	MCC	physical	26496610
PCM1_HUMAN	PCM1	physical	26496610
PER1_HUMAN	PER1	physical	26496610
KAP2_HUMAN	PRKAR2A	physical	26496610
OFD1_HUMAN	OFD1	physical	26496610
NGAP_HUMAN	RASAL2	physical	26496610
MOONR_HUMAN	KIAA0753	physical	26496610
TRIM3_HUMAN	TRIM3	physical	26496610
CP131_HUMAN	CEP131	physical	26496610
GAPD1_HUMAN	GAPVD1	physical	26496610
SNX24_HUMAN	SNX24	physical	26496610
CEP72_HUMAN	CEP72	physical	26496610
STOX2_HUMAN	STOX2	physical	26496610
MIER1_HUMAN	MIER1	physical	26496610
FOPNL_HUMAN	FOPNL	physical	26496610
SPICE_HUMAN	SPICE1	physical	26496610
WDR90_HUMAN	WDR90	physical	26496610
CCD61_HUMAN	CCDC61	physical	26496610
TRAF3_HUMAN	TRAF3	physical	26928339
SNX24_HUMAN	SNX24	physical	28514442
KC1D_HUMAN	CSNK1D	physical	28514442
CRY1_HUMAN	CRY1	physical	28514442
ZN618_HUMAN	ZNF618	physical	28514442
GAPD1_HUMAN	GAPVD1	physical	28514442
PER2_HUMAN	PER2	physical	28514442
CRY2_HUMAN	CRY2	physical	28514442
F110B_HUMAN	FAM110B	physical	28514442
MYOME_HUMAN	PDE4DIP	physical	28514442
PER1_HUMAN	PER1	physical	28514442
F199X_HUMAN	FAM199X	physical	28514442
PIMT_HUMAN	PCMT1	physical	28514442
RS4Y2_HUMAN	RPS4Y2	physical	28514442
UQCC1_HUMAN	UQCC1	physical	28514442
POTEF_HUMAN	POTEF	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442
KLH42_HUMAN	KLHL42	physical	28514442
BTBD1_HUMAN	BTBD1	physical	28514442
KAP3_HUMAN	PRKAR2B	physical	28514442
MTMR4_HUMAN	MTMR4	physical	28514442
FA83H_HUMAN	FAM83H	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KC1E_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-343; SER-354;THR-362; SER-363; SER-389; SER-391; SER-405; THR-407 AND SER-408, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-343; SER-350;THR-351; SER-354; THR-362; SER-363; SER-389; SER-405 AND SER-408, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-389, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351; SER-354 ANDSER-389, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND MASSSPECTROMETRY.	17192257 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-362, AND MASSSPECTROMETRY.	17081983 [Abstract]