KC1E_MOUSE - dbPTM
KC1E_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KC1E_MOUSE
UniProt AC Q9JMK2
Protein Name Casein kinase I isoform epsilon
Gene Name Csnk1e
Organism Mus musculus (Mouse).
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. 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 MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGAARNPEDVDRERREHEREERMGQLRGSATRALPPGPPTGATANRLRSAAEPVASTPASRIQQTGNTSPRAISRADRERKVSMRLHRGAPANVSSSDLTGRQEVSRLAASQTSVPFDHLGK
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
67PhosphorylationQGGVGIPSIKWCGAE
CCCCCCCCCCCCCCC
34.5723375375
101PhosphorylationNFCSRKFSLKTVLLL
HHHCCCCCHHHHHHH
31.8023140645
140UbiquitinationNFLMGLGKKGNLVYI
CEEECCCCCCCEEEE
63.65-
263UbiquitinationRSLRFDDKPDYSYLR
HHCCCCCCCCHHHHH
41.45-
323PhosphorylationRMGQLRGSATRALPP
HHHHHCCCCCCCCCC
21.7429514104
325PhosphorylationGQLRGSATRALPPGP
HHHCCCCCCCCCCCC
20.40-
343PhosphorylationATANRLRSAAEPVAS
HHHHHHHHCCCCCCC
36.1026824392
350PhosphorylationSAAEPVASTPASRIQ
HCCCCCCCCCHHHHH
34.8529514104
354PhosphorylationPVASTPASRIQQTGN
CCCCCCHHHHHCCCC
30.9929514104
359PhosphorylationPASRIQQTGNTSPRA
CHHHHHCCCCCCHHH
18.9429472430
362PhosphorylationRIQQTGNTSPRAISR
HHHCCCCCCHHHHHH
41.2627087446
363PhosphorylationIQQTGNTSPRAISRA
HHCCCCCCHHHHHHH
19.1825521595
382MethylationKVSMRLHRGAPANVS
HHHHHHCCCCCCCCC
47.7824129315
389PhosphorylationRGAPANVSSSDLTGR
CCCCCCCCHHHCCCH
24.7525521595
390PhosphorylationGAPANVSSSDLTGRQ
CCCCCCCHHHCCCHH
24.4825619855
391PhosphorylationAPANVSSSDLTGRQE
CCCCCCHHHCCCHHH
29.1825619855
394PhosphorylationNVSSSDLTGRQEVSR
CCCHHHCCCHHHHHH
35.0028066266
400PhosphorylationLTGRQEVSRLAASQT
CCCHHHHHHHHHHCC
22.3326643407
405PhosphorylationEVSRLAASQTSVPFD
HHHHHHHHCCCCCCC
28.5227087446
407PhosphorylationSRLAASQTSVPFDHL
HHHHHHCCCCCCCCC
29.2427087446
408PhosphorylationRLAASQTSVPFDHLG
HHHHHCCCCCCCCCC
21.8427087446

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 KC1E_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KC1E_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 KC1E_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DVL1_MOUSEDvl1genetic
14966280
DVL1_MOUSEDvl1physical
14966280
DVL2_MOUSEDvl2physical
17606995
TAGL2_HUMANTAGLN2physical
20360068
G6PI_HUMANGPIphysical
20360068
PGK1_HUMANPGK1physical
20360068
NACAM_HUMANNACAphysical
20360068
NACA_HUMANNACAphysical
20360068
C1QBP_HUMANC1QBPphysical
20360068
GAPD1_HUMANGAPVD1physical
20360068
F110B_HUMANFAM110Bphysical
20360068
AP2M1_HUMANAP2M1physical
20360068
CRY1_HUMANCRY1physical
20360068
CP131_HUMANCEP131physical
20360068
KC1E_HUMANCSNK1Ephysical
20360068
PER1_HUMANPER1physical
20360068
HNRPK_HUMANHNRNPKphysical
20360068
FA83H_HUMANFAM83Hphysical
20360068
CRCM_HUMANMCCphysical
20360068
PCBP1_HUMANPCBP1physical
20360068
F110A_HUMANFAM110Aphysical
20360068
TSR1_HUMANTSR1physical
20360068
KPYM_HUMANPKMphysical
20360068
TKT_HUMANTKTphysical
20360068
IF5A1_HUMANEIF5Aphysical
20360068
PER3_HUMANPER3physical
20360068
AP2A1_HUMANAP2A1physical
20360068
CRY2_HUMANCRY2physical
20360068
CPSM_HUMANCPS1physical
20360068
PPIA_HUMANPPIAphysical
20360068
PROF1_HUMANPFN1physical
20360068
SRSF2_HUMANSRSF2physical
20360068
PER2_HUMANPER2physical
20360068
IF4A1_HUMANEIF4A1physical
20360068
STOX2_HUMANSTOX2physical
20360068
VP13B_HUMANVPS13Bphysical
20360068
RAN_HUMANRANphysical
20360068
SNX24_HUMANSNX24physical
20360068
AHNK_HUMANAHNAKphysical
20360068
RRP12_HUMANRRP12physical
20360068
LTV1_HUMANLTV1physical
20360068
CTNB1_MOUSECtnnb1physical
17053159
CTNB1_MOUSECtnnb1physical
15327768
PER1_MOUSEPer1physical
21966515
CRY1_MOUSECry1physical
21966515
UBP2_MOUSEUsp2physical
21966515
CTNB1_MOUSECtnnb1physical
12417018

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KC1E_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP