Casein kinase I isoform epsilon Recombinant Protein | CSNK1E recombinant protein

Recombinant Human Casein kinase I isoform epsilon protein

Cat. Num. AAA717130

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Casein kinase I isoform epsilon; Recombinant Human Casein kinase I isoform epsilon protein; CSNK1E recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 17-231aa; Partial
• Sequence: SGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEK

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for CSNK1E recombinant protein

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.

Product Categories/Family for CSNK1E recombinant protein

Signal Transduction

References

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) Casein kinase I epsilon from HeLa cell.Ono K., Murata-Hori M., Hosoya H.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) A genome annotation-driven approach to cloning the human ORFeome.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.Genome Biol. 5:R84.1-R84.11(2004) 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) 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) 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) 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) 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) 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) 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) 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) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) 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) Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.Mol. Cell. Proteomics 8:1751-1764(2009) 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) 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) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) 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. 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NCBI and Uniprot Product Information

• NCBI GI #: 583966087
• NCBI GeneID: 102800317
• NCBI Accession #: NP_001276841.1
• NCBI GenBank Nucleotide #: NM_001289912.1
• UniProt Accession #: P49674
• Molecular Weight: 51.5 kDa
• NCBI Official Full Name: casein kinase I isoform epsilon
• UniProt Protein Name: Casein kinase I isoform epsilon
• Protein Family: Casein kinase
• UniProt Gene Name: CSNK1E
• UniProt Synonym Gene Names: CKI-epsilon; CKIe
• UniProt Entry Name: KC1E_HUMAN

NCBI Description

This locus represents naturally occurring readthrough transcription between the neighboring LOC400927 (transmembrane phosphoinositide 3-phosphatase and tensin homolog 2 pseudogene) and CSNK1E (casein kinase I isoform epsilon) genes on chromosome 22. The readthrough transcript encodes the same protein as the downstream gene product (casein kinase I isoform epsilon). [provided by RefSeq, Feb 2014]

Uniprot Description

CK1E: an ubiquitous protein kinase of the CK1 family. Together with Dvl-1 and Frat-1 activate the Wnt signaling pathway. Central component of the circadian clock. May act as a negative regulator of circadian rhythmicity by phosphorylating PER1 and PER2. May play a role in cell cycle progression. Two splice variant isoforms have been described. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK, or NPAS2, BMAL1 or BMAL2, CK1-D and/or CK1-E, TIMELESS and the PER proteins. Interacts directly with PER1 and PER2 which may lead to their degradation. Interacts with SOCS3. Mutations in hamster and Drosophila orthologs have circadian rhythm phenotypes, and the circadian gene period (per) is a substrate in both human and fly. A coding SNP variant in human, which increases CK1 activity, is negatively associated with circadian disorder. LOF mutations and LOH seen in mammary ductal carcinoma.

Protein type: Kinase, protein; EC 2.7.11.1; Protein kinase, CK1; Protein kinase, Ser/Thr (non-receptor); CK1 group; CK1 family

Chromosomal Location of Human Ortholog: 22q13.1

Cellular Component: cytoplasm; cytosol; nucleus; ribonucleoprotein complex

Molecular Function: ATP binding; protein binding; protein kinase activity; protein serine/threonine kinase activity

Biological Process: circadian regulation of gene expression; circadian rhythm; DNA repair; G2/M transition of mitotic cell cycle; mitotic cell cycle; negative regulation of protein binding; negative regulation of Wnt receptor signaling pathway; organelle organization and biogenesis; peptidyl-serine phosphorylation; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein amino acid phosphorylation; regulation of circadian rhythm; signal transduction; Wnt receptor signaling pathway