KC1D_RAT - dbPTM
KC1D_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KC1D_RAT
UniProt AC Q06486
Protein Name Casein kinase I isoform delta
Gene Name Csnk1d
Organism Rattus norvegicus (Rat).
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 (By similarity)..
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
114PhosphorylationLLADQMISRIEYIHS
HHHHHHHHHHHHHHH		23.1230181290
263AcetylationRSLRFDDKPDYSYLR
HHCCCCCCCCHHHHH		41.4522902405
318PhosphorylationREERLRHSRNPATRG
HHHHHHHCCCCCCCC		27.5826022182
323PhosphorylationRHSRNPATRGLPSTA
HHCCCCCCCCCCCCC		26.9126022182
328PhosphorylationPATRGLPSTASGRLR
CCCCCCCCCCCCCCC		41.4726437020
329PhosphorylationATRGLPSTASGRLRG
CCCCCCCCCCCCCCC		23.9326437020
331PhosphorylationRGLPSTASGRLRGTQ
CCCCCCCCCCCCCCC		25.2427097102
337PhosphorylationASGRLRGTQEVAPPT
CCCCCCCCCCCCCCC		18.3428432305
344PhosphorylationTQEVAPPTPLTPTSH
CCCCCCCCCCCCCCC		29.8527097102
347PhosphorylationVAPPTPLTPTSHTAN
CCCCCCCCCCCCCCC		26.2327097102
349PhosphorylationPPTPLTPTSHTANTS
CCCCCCCCCCCCCCC		28.0927097102
350PhosphorylationPTPLTPTSHTANTSP
CCCCCCCCCCCCCCC		21.7527097102
352PhosphorylationPLTPTSHTANTSPRP
CCCCCCCCCCCCCCC		22.7527097102
355PhosphorylationPTSHTANTSPRPVSG
CCCCCCCCCCCCCCC		37.3327097102
356PhosphorylationTSHTANTSPRPVSGM
CCCCCCCCCCCCCCC		20.7927097102
361PhosphorylationNTSPRPVSGMERERK
CCCCCCCCCCHHCHH		34.8027097102
370PhosphorylationMERERKVSMRLHRGA
CHHCHHHHHHHHCCC		10.9617594292
375MethylationKVSMRLHRGAPVNVS
HHHHHHHCCCCCCCC		47.78-
382PhosphorylationRGAPVNVSSSDLTGR
CCCCCCCCHHHCCCC		20.9428689409
383PhosphorylationGAPVNVSSSDLTGRQ
CCCCCCCHHHCCCCC		24.4827097102
384PhosphorylationAPVNVSSSDLTGRQD
CCCCCCHHHCCCCCC		29.1827097102
387PhosphorylationNVSSSDLTGRQDTSR
CCCHHHCCCCCCCCC		35.0027097102
392PhosphorylationDLTGRQDTSRMSTSQ
HCCCCCCCCCCCCCC		15.1925575281
393PhosphorylationLTGRQDTSRMSTSQI
CCCCCCCCCCCCCCC		33.9925575281
396PhosphorylationRQDTSRMSTSQIPGR
CCCCCCCCCCCCCCC		24.64-
397PhosphorylationQDTSRMSTSQIPGRV
CCCCCCCCCCCCCCH		18.46-
398PhosphorylationDTSRMSTSQIPGRVA
CCCCCCCCCCCCCHH		20.85-
406PhosphorylationQIPGRVASSGLQSVV
CCCCCHHHCCCCCCC		23.2927097102
407PhosphorylationIPGRVASSGLQSVVH
CCCCHHHCCCCCCCC		33.5127097102
411PhosphorylationVASSGLQSVVHR---
HHHCCCCCCCCC---		31.0227097102
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
328SPhosphorylationKinaseCHEK1O14757
GPS
328SPhosphorylationKinasePRKCAP17252
GPS
329TPhosphorylationKinasePRKCAP17252
GPS
331SPhosphorylationKinaseCHEK1O14757
GPS
370SPhosphorylationKinaseAKT1P31749
PSP
370SPhosphorylationKinaseCHEK1O14757
GPS
370SPhosphorylationKinaseCLK2P49760
PSP
370SPhosphorylationKinasePRKACAP17612
GPS
370SPhosphorylationKinasePRKCAP17252
GPS
370SPhosphorylationKinasePKA-FAMILY-GPS
370SPhosphorylationKinasePKA-Uniprot
370SPhosphorylationKinasePKA_GROUP-PhosphoELM
392TPhosphorylationKinasePRKCAP17252
GPS
393SPhosphorylationKinasePRKCAP17252
GPS
397TPhosphorylationKinaseCHEK1O14757
GPS
397TPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KC1D_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKAP9_HUMANAKAP9physical
12270714
SID4_SCHPOsid4physical
24055157
SNAPN_RATSnapinphysical
17101137
MAP4_RATMap4physical
17101137
PRKN_HUMANPARK2physical
15557340
P53_HUMANTP53physical
17594292
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KC1D_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation of CK1delta: identification of Ser370 as the majorphosphorylation site targeted by PKA in vitro and in vivo.";
Giamas G., Hirner H., Shoshiashvili L., Grothey A., Gessert S.,Kuehl M., Henne-Bruns D., Vorgias C.E., Knippschild U.;
Biochem. J. 406:389-398(2007).
Cited for: PHOSPHORYLATION AT SER-370 BY PKA.

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