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UniProtKB/Swiss-Prot entry P49674


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KC1E_HUMAN
Primary accession number P49674
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 87)
Name and origin of the protein
Protein name Casein kinase I isoform epsilon
Synonyms EC 2.7.11.1
CKI-epsilon
CKIe
Gene name
Name: CSNK1E
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1074/jbc.270.25.14875; PubMed=7797465 [NCBI, ExPASy, EBI, Israel, Japan]
Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.;
"Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family.";
J. Biol. Chem. 270:14875-14883(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Ono K., Murata-Hori M., Hosoya H.;
"Casein kinase I epsilon from HeLa cell.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SOCS3, INDUCTION, AND FUNCTION.
TISSUE=Hematopoietic stem cell;
DOI=10.1182/blood-2003-08-2768; PubMed=15070676 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Involvement of casein kinase Iepsilon in cytokine-induced granulocytic differentiation.";
Blood 103:2997-3004(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH PER1.
PubMed=10790862 [NCBI, ExPASy, EBI, Israel, Japan]
Keesler G.A., Camacho F., Guo Y., Virshup D., Mondadori C., Yao Z.;
"Phosphorylation and destabilization of human period I clock protein by human casein kinase I epsilon.";
NeuroReport 11:951-955(2000).
[8]
ROLE IN WNT SIGNALING.
DOI=10.1074/jbc.M213265200; PubMed=12556519 [NCBI, ExPASy, EBI, Israel, Japan]
Hino S., Michiue T., Asashima M., Kikuchi A.;
"Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and is essential for Wnt-3a-induced accumulation of beta-catenin.";
J. Biol. Chem. 278:14066-14073(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-362, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-389, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[13]
VARIANTS [LARGE SCALE ANALYSIS] LEU-256 AND ARG-413.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L37043; AAC41761.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB024597; BAA92345.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB091043; BAC10902.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456429; CAG30315.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL020993; CAA15888.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006490; AAH06490.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I61744; I61744.
RefSeq NP_001885.1; -.
NP_689407.1; -.
UniGene Hs.474833
3D structure databases
HSSP Q06486; 1CKJ. [HSSP ENTRY / PDB]
SMR P49674; 1-296.
ModBase P49674.
Protein-protein interaction databases
IntAct P49674; -.
PTM databases
PhosphoSite P49674; -.
Organism-specific databases
H-InvDB HIX0016469; -.
HGNC HGNC:2453; CSNK1E.
GeneLynx CSNK1E; Homo sapiens.
GenAtlas CSNK1E.
HPA CAB009626; -.
MIM 600863; gene. [NCBI / EBI]
PharmGKB PA26953; -.
GeneCards P49674.
Gene expression databases
ArrayExpress P49674; -.
CleanEx HS_CSNK1E; -.
GermOnline ENSG00000100181; Homo sapiens.
Ontologies
GO
GO:0004681; Molecular function: casein kinase I activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006281; Biological process: DNA repair (traceable author statement from ProtInc).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P49674.
Genome annotation databases
Ensembl ENSG00000213923; Homo sapiens. [Contig view]
GeneID 1454; -.
KEGG hsa:1454; -.
Phylogenomic databases
HOGENOM P49674; -.
HOVERGEN P49674; -.
Other
LinkHub P49674; -.
SOURCE CSNK1E; Homo sapiens.
ProtoNet P49674.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   416  416     Casein kinase I isoform epsilon. PRO_0000192837
DOMAIN   9   277  269     Protein kinase. 
NP_BIND   15    23  9     ATP (By similarity). 
ACT_SITE   128   128        Proton acceptor (By similarity). 
BINDING   38    38        ATP (By similarity). 
MOD_RES   343   343        Phosphoserine. 
MOD_RES   362   362        Phosphothreonine. 
MOD_RES   363   363        Phosphoserine. 
MOD_RES   389   389        Phosphoserine. 
VARIANT   256   256  1     R -> L (in a lung adenocarcinoma sample; somatic mutation). VAR_042082 [3D]
VARIANT   413   413  1     H -> R. VAR_042083 
Sequence information
Length: 416 AA [This is the length of the unprocessed precursor] Molecular weight: 47315 Da [This is the MW of the unprocessed precursor] CRC64: EE1B1698AE914324 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELRVGNKYR LGRKIGSGSF GDIYLGANIA SGEEVAIKLE CVKTKHPQLH IESKFYKMMQ 

        70         80         90        100        110        120 
GGVGIPSIKW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH 

       130        140        150        160        170        180 
SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA 

       190        200        210        220        230        240 
SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL 

       250        260        270        280        290        300 
CKGYPSEFST YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGAARN 

       310        320        330        340        350        360 
PEDVDRERRE HEREERMGQL RGSATRALPP GPPTGATANR LRSAAEPVAS TPASRIQPAG 

       370        380        390        400        410 
NTSPRAISRV DRERKVSMRL HRGAPANVSS SDLTGRQEVS RIPASQTSVP FDHLGK 

P49674 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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