KC1D_MOUSE - dbPTM
KC1D_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KC1D_MOUSE
UniProt AC Q9DC28
Protein Name Casein kinase I isoform delta
Gene Name Csnk1d
Organism Mus musculus (Mouse).
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 centrosome
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 MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNVSSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR
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
57UbiquitinationHIESKIYKMMQGGVG
HHHHHHHHHHCCCCC		31.22-
101PhosphorylationNFCSRKFSLKTVLLL
HHHCCCCCHHHHHHH		31.8023140645
140UbiquitinationNFLMGLGKKGNLVYI
CEEECCCCCCCEEEE		63.65-
255S-palmitoylationFATYLNFCRSLRFDD
HHHHHHHHHHCCCCC		2.5528680068
263UbiquitinationRSLRFDDKPDYSYLR
HHCCCCCCCCHHHHH		41.45-
323PhosphorylationRHSRNPATRGLPSTA
HHCCCCCCCCCCCCC		26.9129514104
328PhosphorylationPATRGLPSTASGRLR
CCCCCCCCCCCCCCC		41.4728973931
329PhosphorylationATRGLPSTASGRLRG
CCCCCCCCCCCCCCC		23.9327149854
331PhosphorylationRGLPSTASGRLRGTQ
CCCCCCCCCCCCCCC		25.2426824392
337PhosphorylationASGRLRGTQEVAPPT
CCCCCCCCCCCCCCC		18.3429233185
344PhosphorylationTQEVAPPTPLTPTSH
CCCCCCCCCCCCCCC		29.8522322096
347PhosphorylationVAPPTPLTPTSHTAN
CCCCCCCCCCCCCCC		26.2321082442
349PhosphorylationPPTPLTPTSHTANTS
CCCCCCCCCCCCCCC		28.0920469934
350PhosphorylationPTPLTPTSHTANTSP
CCCCCCCCCCCCCCC		21.7525521595
352PhosphorylationPLTPTSHTANTSPRP
CCCCCCCCCCCCCCC		22.7520469934
355PhosphorylationPTSHTANTSPRPVSG
CCCCCCCCCCCCCCC		37.3325521595
356PhosphorylationTSHTANTSPRPVSGM
CCCCCCCCCCCCCCC		20.7925521595
361PhosphorylationNTSPRPVSGMERERK
CCCCCCCCCCHHCHH		34.8021082442
370PhosphorylationMERERKVSMRLHRGA
CHHCHHHHHHHHCCC		10.96-
375MethylationKVSMRLHRGAPVNVS
HHHHHHHCCCCCCCC		47.7824129315
382 (in isoform 2)Phosphorylation-20.9424719451
382PhosphorylationRGAPVNVSSSDLTGR
CCCCCCCCHHHCCCC		20.9425521595
383PhosphorylationGAPVNVSSSDLTGRQ
CCCCCCCHHHCCCCC		24.4825521595
384PhosphorylationAPVNVSSSDLTGRQD
CCCCCCHHHCCCCCC		29.1825521595
387PhosphorylationNVSSSDLTGRQDTSR
CCCHHHCCCCCCCCC		35.0025619855
392PhosphorylationDLTGRQDTSRMSTSQ
HCCCCCCCCCCCCCC		15.1923984901
393PhosphorylationLTGRQDTSRMSTSQI
CCCCCCCCCCCCCCC		33.9923984901
396PhosphorylationRQDTSRMSTSQIPGR
CCCCCCCCCCCCCCC		24.6428066266
396 (in isoform 2)Phosphorylation-24.6423684622
397PhosphorylationQDTSRMSTSQIPGRV
CCCCCCCCCCCCCCH		18.4628066266
397 (in isoform 2)Phosphorylation-18.4627600695
398PhosphorylationDTSRMSTSQIPGRVA
CCCCCCCCCCCCCHH		20.8528066266
398 (in isoform 2)Phosphorylation-20.8529233185
401 (in isoform 2)Phosphorylation-19.5327600695
406PhosphorylationQIPGRVASSGLQSVV
CCCCCHHHCCCCCCC		23.2929514104
407PhosphorylationIPGRVASSGLQSVVH
CCCCHHHCCCCCCCC		33.5129514104
411PhosphorylationVASSGLQSVVHR---
HHHCCCCCCCCC---		31.0229514104
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

Oops, there are no upstream regulatory protein records of KC1D_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KC1D_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNAPN_MOUSESnapinphysical
17101137
KC1E_HUMANCSNK1Ephysical
26496610
ITA1_HUMANITGA1physical
26496610
PER1_HUMANPER1physical
26496610
PPM1A_HUMANPPM1Aphysical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
BCL7C_HUMANBCL7Cphysical
26496610
HMGN3_HUMANHMGN3physical
26496610
TRIM3_HUMANTRIM3physical
26496610
WWP2_HUMANWWP2physical
26496610
GAPD1_HUMANGAPVD1physical
26496610
SNX24_HUMANSNX24physical
26496610
RAIN_HUMANRASIP1physical
26496610
KNL1_HUMANCASC5physical
26496610
S35E1_HUMANSLC35E1physical
26496610
CD109_HUMANCD109physical
26496610
FA83H_HUMANFAM83Hphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KC1D_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND MASSSPECTROMETRY.

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