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P49674

- KC1E_HUMAN

UniProt

P49674 - KC1E_HUMAN

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Protein

Casein kinase I isoform epsilon

Gene

CSNK1E

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 phospohorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Phosphorylation leads to a decrease of the catalytic activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381ATPPROSITE-ProRule annotation
Active sitei128 – 1281Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 239ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. protein kinase activity Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cellular protein localization Source: Ensembl
  2. circadian regulation of gene expression Source: UniProtKB
  3. DNA repair Source: ProtInc
  4. G2/M transition of mitotic cell cycle Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. negative regulation of Wnt signaling pathway Source: Ensembl
  7. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  8. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  9. protein phosphorylation Source: UniProtKB
  10. regulation of circadian rhythm Source: UniProtKB
  11. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_200668. WNT mediated activation of DVL.
REACT_24941. Circadian Clock.
SignaLinkiP49674.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase I isoform epsilon (EC:2.7.11.1)
Short name:
CKI-epsilon
Short name:
CKIe
Gene namesi
Name:CSNK1E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:2453. CSNK1E.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB
  3. ribonucleoprotein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26953.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Casein kinase I isoform epsilonPRO_0000192837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei343 – 3431Phosphoserine2 Publications
Modified residuei354 – 3541Phosphoserine2 Publications
Modified residuei362 – 3621Phosphothreonine1 Publication
Modified residuei363 – 3631Phosphoserine3 Publications
Modified residuei389 – 3891Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated. Partially dephosphorylated by PPP5C. May be dephosphorylated by PP1.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49674.
PaxDbiP49674.
PRIDEiP49674.

PTM databases

PhosphoSiteiP49674.

Expressioni

Tissue specificityi

Expressed in all tissues examined, including brain, heart, lung, liver, pancreas, kidney, placenta and skeletal muscle. Expressed in monocytes and lymphocytes but not in granulocytes.

Inductioni

Down-regulated during granulocytic differentiation.1 Publication

Gene expression databases

BgeeiP49674.
CleanExiHS_CSNK1E.
ExpressionAtlasiP49674. baseline and differential.
GenevestigatoriP49674.

Organism-specific databases

HPAiCAB009626.
HPA026288.

Interactioni

Subunit structurei

Monomer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK, or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts with ANKRD6, DBNDD2, LRP5, LRP6 and SOCS3. Interacts with SNAI1 (via zinc fingers).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APCP250548EBI-749343,EBI-727707
AXIN1O151694EBI-749343,EBI-710484
Axin1O702397EBI-749343,EBI-6857773From a different organism.
DVL1O146406EBI-749343,EBI-723489
Dvl2Q608383EBI-749343,EBI-641940From a different organism.
HSP90AB1P082382EBI-749343,EBI-352572
MDM2Q009873EBI-749343,EBI-389668
OCLNQ166257EBI-749343,EBI-2903088

Protein-protein interaction databases

BioGridi107838. 98 interactions.
IntActiP49674. 75 interactions.
MINTiMINT-1444044.
STRINGi9606.ENSP00000352929.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83Combined sources
Beta strandi14 – 163Combined sources
Beta strandi22 – 287Combined sources
Turni29 – 313Combined sources
Beta strandi35 – 417Combined sources
Helixi51 – 566Combined sources
Turni57 – 615Combined sources
Beta strandi68 – 747Combined sources
Beta strandi77 – 837Combined sources
Helixi89 – 957Combined sources
Turni96 – 983Combined sources
Helixi102 – 12019Combined sources
Turni121 – 1233Combined sources
Helixi131 – 1333Combined sources
Beta strandi134 – 1363Combined sources
Helixi139 – 1413Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi154 – 1574Combined sources
Turni159 – 1613Combined sources
Helixi177 – 1793Combined sources
Helixi182 – 1854Combined sources
Helixi192 – 20817Combined sources
Turni212 – 2154Combined sources
Helixi221 – 23414Combined sources
Helixi237 – 2404Combined sources
Turni241 – 2433Combined sources
Helixi246 – 25510Combined sources
Helixi266 – 28015Combined sources
Helixi289 – 2913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HNIX-ray2.74A/B1-294[»]
4HOKX-ray2.77A/C/E/G/I/K/M/O/Q/S/U/W1-294[»]
ProteinModelPortaliP49674.
SMRiP49674. Positions 4-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 277269Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000182055.
HOVERGENiHBG000176.
InParanoidiP49674.
KOiK08960.
OrthoDBiEOG7CZK5W.
PhylomeDBiP49674.
TreeFamiTF300544.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49674-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELRVGNKYR LGRKIGSGSF GDIYLGANIA SGEEVAIKLE CVKTKHPQLH
60 70 80 90 100
IESKFYKMMQ GGVGIPSIKW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF
110 120 130 140 150
SLKTVLLLAD QMISRIEYIH SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF
160 170 180 190 200
GLAKKYRDAR THQHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG
210 220 230 240 250
YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL CKGYPSEFST
260 270 280 290 300
YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGAARN
310 320 330 340 350
PEDVDRERRE HEREERMGQL RGSATRALPP GPPTGATANR LRSAAEPVAS
360 370 380 390 400
TPASRIQPAG NTSPRAISRV DRERKVSMRL HRGAPANVSS SDLTGRQEVS
410
RIPASQTSVP FDHLGK
Length:416
Mass (Da):47,315
Last modified:February 1, 1996 - v1
Checksum:iEE1B1698AE914324
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti256 – 2561R → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042082
Natural varianti413 – 4131H → R.1 Publication
Corresponds to variant rs35665927 [ dbSNP | Ensembl ].
VAR_042083

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37043 mRNA. Translation: AAC41761.1.
AB024597 mRNA. Translation: BAA92345.1.
AB091043 mRNA. Translation: BAC10902.1.
CR456429 mRNA. Translation: CAG30315.1.
AL020993 Genomic DNA. Translation: CAA15888.1.
BC006490 mRNA. Translation: AAH06490.1.
CCDSiCCDS13970.1.
PIRiI61744.
RefSeqiNP_001276841.1. NM_001289912.1.
NP_001885.1. NM_001894.4.
NP_689407.1. NM_152221.2.
UniGeneiHs.474833.
Hs.720223.

Genome annotation databases

EnsembliENST00000359867; ENSP00000352929; ENSG00000213923.
ENST00000396832; ENSP00000380044; ENSG00000213923.
ENST00000400206; ENSP00000383067; ENSG00000213923.
ENST00000403904; ENSP00000384074; ENSG00000213923.
GeneIDi102800317.
1454.
KEGGihsa:102800317.
hsa:1454.
UCSCiuc003avj.3. human.

Polymorphism databases

DMDMi1346369.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37043 mRNA. Translation: AAC41761.1 .
AB024597 mRNA. Translation: BAA92345.1 .
AB091043 mRNA. Translation: BAC10902.1 .
CR456429 mRNA. Translation: CAG30315.1 .
AL020993 Genomic DNA. Translation: CAA15888.1 .
BC006490 mRNA. Translation: AAH06490.1 .
CCDSi CCDS13970.1.
PIRi I61744.
RefSeqi NP_001276841.1. NM_001289912.1.
NP_001885.1. NM_001894.4.
NP_689407.1. NM_152221.2.
UniGenei Hs.474833.
Hs.720223.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4HNI X-ray 2.74 A/B 1-294 [» ]
4HOK X-ray 2.77 A/C/E/G/I/K/M/O/Q/S/U/W 1-294 [» ]
ProteinModelPortali P49674.
SMRi P49674. Positions 4-294.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107838. 98 interactions.
IntActi P49674. 75 interactions.
MINTi MINT-1444044.
STRINGi 9606.ENSP00000352929.

Chemistry

BindingDBi P49674.
ChEMBLi CHEMBL4937.
GuidetoPHARMACOLOGYi 1998.

PTM databases

PhosphoSitei P49674.

Polymorphism databases

DMDMi 1346369.

Proteomic databases

MaxQBi P49674.
PaxDbi P49674.
PRIDEi P49674.

Protocols and materials databases

DNASUi 1454.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359867 ; ENSP00000352929 ; ENSG00000213923 .
ENST00000396832 ; ENSP00000380044 ; ENSG00000213923 .
ENST00000400206 ; ENSP00000383067 ; ENSG00000213923 .
ENST00000403904 ; ENSP00000384074 ; ENSG00000213923 .
GeneIDi 102800317.
1454.
KEGGi hsa:102800317.
hsa:1454.
UCSCi uc003avj.3. human.

Organism-specific databases

CTDi 1454.
GeneCardsi GC22M038686.
H-InvDB HIX0080286.
HGNCi HGNC:2453. CSNK1E.
HPAi CAB009626.
HPA026288.
MIMi 600863. gene.
neXtProti NX_P49674.
PharmGKBi PA26953.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000182055.
HOVERGENi HBG000176.
InParanoidi P49674.
KOi K08960.
OrthoDBi EOG7CZK5W.
PhylomeDBi P49674.
TreeFami TF300544.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_200668. WNT mediated activation of DVL.
REACT_24941. Circadian Clock.
SignaLinki P49674.

Miscellaneous databases

ChiTaRSi CSNK1E. human.
GeneWikii CSNK1E.
NextBioi 5969.
PROi P49674.
SOURCEi Search...

Gene expression databases

Bgeei P49674.
CleanExi HS_CSNK1E.
ExpressionAtlasi P49674. baseline and differential.
Genevestigatori P49674.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family."
    Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.
    J. Biol. Chem. 270:14875-14883(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Casein kinase I epsilon from HeLa cell."
    Ono K., Murata-Hori M., Hosoya H.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Involvement of casein kinase Iepsilon in cytokine-induced granulocytic differentiation."
    Okamura A., Iwata N., Nagata A., Tamekane A., Shimoyama M., Gomyo H., Yakushijin K., Urahama N., Hamaguchi M., Fukui C., Chihara K., Ito M., Matsui T.
    Blood 103:2997-3004(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SOCS3, INDUCTION, FUNCTION.
    Tissue: Hematopoietic stem cell.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  7. "Phosphorylation and destabilization of human period I clock protein by human casein kinase I epsilon."
    Keesler G.A., Camacho F., Guo Y., Virshup D., Mondadori C., Yao Z.
    NeuroReport 11:951-955(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PER1.
  8. "Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and is essential for Wnt-3a-induced accumulation of beta-catenin."
    Hino S., Michiue T., Asashima M., Kikuchi A.
    J. Biol. Chem. 278:14066-14073(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN WNT SIGNALING.
  9. "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein."
    Shirogane T., Jin J., Ang X.L., Harper J.W.
    J. Biol. Chem. 280:26863-26872(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PER1 KINASE.
  10. "Dysbindin structural homologue CK1BP is an isoform-selective binding partner of human casein kinase-1."
    Yin H., Laguna K.A., Li G., Kuret J.
    Biochemistry 45:5297-5308(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DBNDD2.
  11. "Negative regulation of LRP6 function by casein kinase I epsilon phosphorylation."
    Swiatek W., Kang H., Garcia B.A., Shabanowitz J., Coombs G.S., Hunt D.F., Virshup D.M.
    J. Biol. Chem. 281:12233-12241(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRP5 AND LRP6.
  12. "Posttranslational regulation of the mammalian circadian clock by cryptochrome and protein phosphatase 5."
    Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.
    Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION, DEPHOSPHORYLATION BY PPP5C, ENZYME REGULATION.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-354; THR-362 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Role of CK1 in GSK3beta-mediated phosphorylation and degradation of snail."
    Xu Y., Lee S.H., Kim H.S., Kim N.H., Piao S., Park S.H., Jung Y.S., Yook J.I., Park B.J., Ha N.C.
    Oncogene 29:3124-3133(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAI1.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Structural basis for the potent and selective inhibition of casein kinase 1 epsilon."
    Long A.M., Zhao H., Huang X.
    J. Med. Chem. 55:10307-10311(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 1-294 ALONE AND IN COMPLEX WITH INHIBITOR.
  22. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-256 AND ARG-413.

Entry informationi

Entry nameiKC1E_HUMAN
AccessioniPrimary (citable) accession number: P49674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3