KC1D_HUMAN - dbPTM
KC1D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KC1D_HUMAN
UniProt AC P48730
Protein Name Casein kinase I isoform delta
Gene Name CSNK1D
Organism Homo sapiens (Human).
Sequence Length 415
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton, spindle. Golgi apparatus. Localized at mitotic spindle microtubules, and at the centrosomes
Protein Description Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. 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. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate..
Protein Sequence MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
17PhosphorylationRLGRKIGSGSFGDIY
ECCCEECCCCCCCEE		34.43-
43UbiquitinationAIKLECVKTKHPQLH
EEEEEHHCCCCCCCH		64.6133845483
44PhosphorylationIKLECVKTKHPQLHI
EEEEHHCCCCCCCHH		17.7520507565
45UbiquitinationKLECVKTKHPQLHIE
EEEHHCCCCCCCHHH		47.7927667366
54UbiquitinationPQLHIESKIYKMMQG
CCCHHHHHHHHHHCC		36.9523000965
57AcetylationHIESKIYKMMQGGVG
HHHHHHHHHHCCCCC		31.2225953088
57UbiquitinationHIESKIYKMMQGGVG
HHHHHHHHHHCCCCC		31.2223000965
65UbiquitinationMMQGGVGIPTIRWCG
HHCCCCCCCEEECCC		2.2421890473
73UbiquitinationPTIRWCGAEGDYNVM
CEEECCCCCCCHHEE		17.9222817900
83UbiquitinationDYNVMVMELLGPSLE
CHHEEEEHHHCCCHH		29.4522817900
84UbiquitinationYNVMVMELLGPSLED
HHEEEEHHHCCCHHH		3.4622817900
114UbiquitinationLLADQMISRIEYIHS
HHHHHHHHHHHHHHH		23.1227667366
122UbiquitinationRIEYIHSKNFIHRDV
HHHHHHHCCCCCCCC		41.5421890473
122 (in isoform 2)Ubiquitination-41.5421890473
122 (in isoform 1)Ubiquitination-41.5421890473
122UbiquitinationRIEYIHSKNFIHRDV
HHHHHHHCCCCCCCC		41.5421890473
130 (in isoform 2)Ubiquitination-51.4421890473
130UbiquitinationNFIHRDVKPDNFLMG
CCCCCCCCCCCEEEC		51.4422817900
130 (in isoform 1)Ubiquitination-51.4421890473
140AcetylationNFLMGLGKKGNLVYI
CEEECCCCCCCEEEE		63.6525953088
140UbiquitinationNFLMGLGKKGNLVYI
CEEECCCCCCCEEEE		63.6527667366
140 (in isoform 2)Ubiquitination-63.6521890473
140 (in isoform 1)Ubiquitination-63.6521890473
141UbiquitinationFLMGLGKKGNLVYII
EEECCCCCCCEEEEE		51.7622817900
146PhosphorylationGKKGNLVYIIDFGLA
CCCCCEEEEEECCCC		8.7029496907
155UbiquitinationIDFGLAKKYRDARTH
EECCCCHHHHHCCCC		39.65-
171UbiquitinationHIPYRENKNLTGTAR
CCCCCCCCCCCCEEE		48.8927667366
179PhosphorylationNLTGTARYASINTHL
CCCCEEEEEEHHHHC		11.3929496907
181PhosphorylationTGTARYASINTHLGI
CCEEEEEEHHHHCCC		13.8728857561
184PhosphorylationARYASINTHLGIEQS
EEEEEHHHHCCCCCH		19.4630576142
206UbiquitinationLGYVLMYFNLGSLPW
HHHHHHHCCCCCCCH		3.6621890473
232UbiquitinationYERISEKKMSTPIEV
HHHHHHCCCCCCHHH		33.7529967540
234PhosphorylationRISEKKMSTPIEVLC
HHHHCCCCCCHHHHC		39.6520068231
235PhosphorylationISEKKMSTPIEVLCK
HHHCCCCCCHHHHCC		25.4520068231
242AcetylationTPIEVLCKGYPSEFA
CCHHHHCCCCCHHHH		58.27130587
263 (in isoform 2)Ubiquitination-41.4521890473
263 (in isoform 1)Ubiquitination-41.4521890473
263UbiquitinationRSLRFDDKPDYSYLR
HHCCCCCCCCHHHHH		41.4521890473
263UbiquitinationRSLRFDDKPDYSYLR
HHCCCCCCCCHHHHH		41.4521890473
266PhosphorylationRFDDKPDYSYLRQLF
CCCCCCCHHHHHHHH		14.03-
267PhosphorylationFDDKPDYSYLRQLFR
CCCCCCHHHHHHHHH		25.6829496907
284PhosphorylationFHRQGFSYDYVFDWN
HHHCCCCCEEEECHH		14.7229496907
286PhosphorylationRQGFSYDYVFDWNML
HCCCCCEEEECHHHH		8.5229496907
328PhosphorylationPATRGLPSTASGRLR
CCCCCCCCCCCCCCC		41.4729255136
329PhosphorylationATRGLPSTASGRLRG
CCCCCCCCCCCCCCC		23.9329255136
331PhosphorylationRGLPSTASGRLRGTQ
CCCCCCCCCCCCCCC		25.2429255136
335MethylationSTASGRLRGTQEVAP
CCCCCCCCCCCCCCC		44.76-
337PhosphorylationASGRLRGTQEVAPPT
CCCCCCCCCCCCCCC		18.3422199227
344PhosphorylationTQEVAPPTPLTPTSH
CCCCCCCCCCCCCCC		29.8522167270
347PhosphorylationVAPPTPLTPTSHTAN
CCCCCCCCCCCCCCC		26.2327273156
349PhosphorylationPPTPLTPTSHTANTS
CCCCCCCCCCCCCCC		28.0923401153
350PhosphorylationPTPLTPTSHTANTSP
CCCCCCCCCCCCCCC		21.7522167270
352PhosphorylationPLTPTSHTANTSPRP
CCCCCCCCCCCCCCC		22.7522167270
355PhosphorylationPTSHTANTSPRPVSG
CCCCCCCCCCCCCCC		37.3322167270
356PhosphorylationTSHTANTSPRPVSGM
CCCCCCCCCCCCCCC		20.7922167270
361PhosphorylationNTSPRPVSGMERERK
CCCCCCCCCCHHCHH		34.8022167270
370PhosphorylationMERERKVSMRLHRGA
CHHCHHHHHHHHCCC		10.96-
375MethylationKVSMRLHRGAPVNIS
HHHHHHHCCCCCCCC		47.78-
382PhosphorylationRGAPVNISSSDLTGR
CCCCCCCCHHHCCCC		20.7029255136
383 (in isoform 2)Phosphorylation-24.8718220336
383PhosphorylationGAPVNISSSDLTGRQ
CCCCCCCHHHCCCCC		24.8729255136
384PhosphorylationAPVNISSSDLTGRQD
CCCCCCHHHCCCCCC		29.8329255136
387PhosphorylationNISSSDLTGRQDTSR
CCCHHHCCCCCCCCC		35.0029255136
392 (in isoform 2)Phosphorylation-15.1919369195
392PhosphorylationDLTGRQDTSRMSTSQ
HCCCCCCCCCCCCCC		15.1923090842
393PhosphorylationLTGRQDTSRMSTSQI
CCCCCCCCCCCCCCC		33.9923090842
393 (in isoform 2)Phosphorylation-33.9919369195
396PhosphorylationRQDTSRMSTSQIPGR
CCCCCCCCCCCCCCC		24.6418691976
396 (in isoform 2)Phosphorylation-24.6430266825
397PhosphorylationQDTSRMSTSQIPGRV
CCCCCCCCCCCCCCH		18.4618691976
397 (in isoform 2)Phosphorylation-18.4630266825
398 (in isoform 2)Phosphorylation-20.8530266825
398PhosphorylationDTSRMSTSQIPGRVA
CCCCCCCCCCCCCHH		20.8518691976
401 (in isoform 2)Phosphorylation-19.5330266825
406PhosphorylationQIPGRVASSGLQSVV
CCCCCHHHCCCCCCC		23.2921082442
407PhosphorylationIPGRVASSGLQSVVH
CCCCHHHCCCCCCCC		33.5121082442
411PhosphorylationVASSGLQSVVHR---
HHHCCCCCCCCC---		31.0211161704
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
53SPhosphorylationKinasePKCAP17252
PSP
161TPhosphorylationKinasePKCAP17252
PSP
174TPhosphorylationKinasePKCAP17252
PSP
176TPhosphorylationKinasePKCAP17252
PSP
181SPhosphorylationKinasePKCAP17252
PSP
191SPhosphorylationKinasePKCAP17252
PSP
298SPhosphorylationKinasePKCAP17252
PSP
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KC1D_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 KC1D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DVL3_HUMANDVL3physical
16189514
CXA1_HUMANGJA1physical
12270943
DVL1_HUMANDVL1physical
11818547
MDM2_HUMANMDM2physical
20708156
JUPI2_HUMANHN1Lphysical
21900206
VGFR2_HUMANKDRphysical
22711876
P53_HUMANTP53physical
16870621
MDM2_HUMANMDM2physical
16870621
MDM2_HUMANMDM2physical
22976441
P53_HUMANTP53physical
18246126
PML_HUMANPMLphysical
18246126
DBND2_HUMANDBNDD2physical
16618118
SYUA_HUMANSNCAphysical
16618118
TAU_HUMANMAPTphysical
16618118
A4_HUMANAPPphysical
21832049
UBP16_HUMANUSP16physical
22939629
SMAD2_HUMANSMAD2physical
19139564
SMAD3_HUMANSMAD3physical
19139564
SMAD4_HUMANSMAD4physical
19139564
FHL1_HUMANFHL1physical
19139564
DVL3_HUMANDVL3physical
25416956
TRIM9_HUMANTRIM9physical
25416956
LURA1_HUMANLURAP1physical
25416956
BRCA1_HUMANBRCA1physical
25184681
TAU_HUMANMAPTphysical
17101137
P53_HUMANTP53physical
17101137
PER2_HUMANPER2physical
23555304
NOB1_HUMANNOB1physical
26344197
PPM1B_HUMANPPM1Bphysical
26344197
RAB1A_HUMANRAB1Aphysical
26195667
SNX24_HUMANSNX24physical
28514442
F110B_HUMANFAM110Bphysical
28514442
ZN618_HUMANZNF618physical
28514442
GAPD1_HUMANGAPVD1physical
28514442
CRY2_HUMANCRY2physical
28514442
CRY1_HUMANCRY1physical
28514442
PER1_HUMANPER1physical
28514442
MYOME_HUMANPDE4DIPphysical
28514442
ANR49_HUMANANKRD49physical
28514442
TYDP1_HUMANTDP1physical
28514442
F199X_HUMANFAM199Xphysical
28514442
AKAP9_HUMANAKAP9physical
28514442
VP13B_HUMANVPS13Bphysical
28514442
FA83H_HUMANFAM83Hphysical
28514442
FKBPL_HUMANFKBPLphysical
28514442
FA83D_HUMANFAM83Dphysical
28514442
HMMR_HUMANHMMRphysical
28514442
KAP3_HUMANPRKAR2Bphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615224Advanced sleep phase syndrome, familial, 2 (FASPS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KC1D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-383, AND MASSSPECTROMETRY.
"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-328; THR-329; SER-331;THR-337; THR-344; THR-347; THR-349; SER-350; THR-352; THR-355;SER-356; SER-361; SER-382; SER-383; THR-392; SER-393; SER-396;THR-397; SER-398; PRO-401; SER-406 AND SER-411, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-401 (ISOFORM 2), AND MASS SPECTROMETRY.
"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-382, AND MASSSPECTROMETRY.
"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-331; THR-347; THR-349;SER-382 AND SER-384, AND MASS SPECTROMETRY.
"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-328; SER-331; THR-347;SER-382; SER-383; SER-384; THR-387; SER-396; THR-397; SER-398; SER-406AND SER-407, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401(ISOFORM 2), AND MASS SPECTROMETRY.
"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-383, AND MASSSPECTROMETRY.
"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-331 AND SER-382, ANDMASS SPECTROMETRY.
"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 SER-350, AND MASSSPECTROMETRY.

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