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Description:
Casein kinase I isoform epsilon (EC 2.7.1.-) (CKI-epsilon) (CKIe).
Molecular weight: 47315
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
07-MAR-2006, entry version 55.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein KC1E_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | L37043 | AAC41761.1 | - |
| EMBL | AB024597 | BAA92345.1 | - |
| EMBL | AB091043 | BAC10902.1 | - |
| EMBL | CR456429 | CAG30315.1 | - |
| EMBL | AL020993 | CAA15888.1 | - |
| EMBL | BC006490 | AAH06490.1 | - |
| PIR | I61744 | I61744. | |
| HSSP | Q06486 | 1CKJ | |
| SMR | P49674 | 1-296.1 | |
| Ensembl | ENSG00000100181 | Homo sapiens.1 | |
| H-InvDB | HIX0016469 | -.1 | |
| HGNC | HGNC:2453 | CSNK1E.1 | |
| MIM | 600863 | gene. | |
| GO | GO:0004681 | F:casein kinase I activity | TAS. |
| GO | GO:0006281 | P:DNA repair | TAS. |
| GO | GO:0006468 | P:protein amino acid phosphorylation | TAS. |
| GO | GO:0007165 | P:signal transduction | TAS. |
| InterPro | IPR000719 | Prot_kinase. | |
| InterPro | IPR008271 | Ser_thr_pkin_AS. | |
| InterPro | IPR002290 | Ser_thr_pkinase. | |
| InterPro | IPR001245 | Tyr_pkinase. | |
| Pfam | PF00069 | Pkinase | 1. |
| ProDom | PD000001 | Prot_kinase | 1. |
| PROSITE | PS00107 | PROTEIN_KINASE_ATP | 1. |
| PROSITE | PS50011 | PROTEIN_KINASE_DOM | 1. |
| PROSITE | PS00108 | PROTEIN_KINASE_ST | 1. |
Keywords:
ATP-binding; Kinase; Nucleotide-binding; Phosphorylation; Serine/threonine-protein kinase; Transferase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=95318039; PubMed=7797465; DOI=10.1074/jbc.270.25.14875;
RA Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.;
RT "Isolation and characterization of human casein kinase I epsilon
RT (CKI), a novel member of the CKI gene family.";
RL J. Biol. Chem. 270:14875-14883(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Ono K., Murata-Hori M., Hosoya H.;
RT "Casein kinase I epsilon from HeLa cell.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Okamura A., Iwata N., Tamekane A., Nagata A., Shimoyama M., Gomyo H.,
RA Hamaguchi M., Chihara K., Ito M., Matsui T.;
RT "Involvement of casein kinase I epsilon in cytokine-induced
RT granulocytic differentiation.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [7]
RP ROLE IN WNT SIGNALING.
RX MEDLINE=22578304; PubMed=12556519; DOI=10.1074/jbc.M213265200;
RA Hino S., Michiue T., Asashima M., Kikuchi A.;
RT "Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and
RT is essential for Wnt-3a-induced accumulation of beta-catenin.";
RL J. Biol. Chem. 278:14066-14073(2003).
RN [8]
RP PHOSPHORYLATION SITE SER-363.
RX PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Feature:
CHAIN 1 416 Casein kinase I isoform epsilon.
/FTId=PRO_0000192837.
DOMAIN 9 277 Protein kinase.
NP_BIND 15 23 ATP (By similarity).
ACT_SITE 128 128 Proton acceptor (By similarity).
BINDING 38 38 ATP (By similarity).
MOD_RES 363 363 Phosphoserine.
Comments:
-!- FUNCTION: Casein kinases are operationally defined by their
preferential utilization of acidic proteins such as caseins as
substrates. It can phosphorylate a large number of proteins.
Participates in Wnt signaling. Phosphorylates DVL1.
-!- SUBUNIT: Monomer (By similarity).
-!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
-!- PTM: Autophosphorylated (By similarity).
-!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. Casein
kinase I subfamily.
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Sequence length: 416
MELRVGNKYR LGRKIGSGSF GDIYLGANIA SGEEVAIKLE CVKTKHPQLH IESKFYKMMQ
GGVGIPSIKW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH
SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA
SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL
CKGYPSEFST YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGAARN
PEDVDRERRE HEREERMGQL RGSATRALPP GPPTGATANR LRSAAEPVAS TPASRIQPAG
NTSPRAISRV DRERKVSMRL HRGAPANVSS SDLTGRQEVS RIPASQTSVP FDHLGK