|
|
|
|
|
|
Description:
Casein kinase I isoform alpha (EC 2.7.1.-) (CKI-alpha) (DmCK1).
Molecular weight: 39535
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-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-MAR-2006, entry version 53.
Phylogenetic order:
Eukaryota Metazoa Arthropoda Hexapoda Insecta Pterygota Neoptera Endopterygota Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila.
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 KC1A_DROME:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U55848 | AAB16904.1 | - |
| EMBL | X94695 | CAA64358.1 | - |
| EMBL | AE003490 | AAF48193.1 | - |
| EMBL | AY069346 | AAL39491.1 | - |
| HSSP | Q06486 | 1CKJ | |
| Ensembl | CG2028 | Drosophila melanogaster.1 | |
| FlyBase | FBgn0015024 | CkI-alpha. | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-001649-MONOMER | -.1 | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-001650-MONOMER | -.1 | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-001651-MONOMER | -.1 | |
| LinkHub | P54367 | -.1 | |
| GO | GO:0005737 | C:cytoplasm | IDA. |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0004672 | F:protein kinase activity | IDA. |
| GO | GO:0006281 | P:DNA repair | IDA. |
| GO | GO:0045879 | P:negative regulation of smoothened signaling... | IMP. |
| GO | GO:0030163 | P:protein catabolism | NAS. |
| GO | GO:0030162 | P:regulation of proteolysis and peptidolysis | 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; Complete proteome; Kinase; Nucleotide-binding; Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Glover C.V.C., Kandala G.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=96429306; PubMed=8832407;
RA Santos J.A., Logarinho E., Tapia C., Allende C.C., Allende J.E.,
RA Sunkel C.E.;
RT "The casein kinase 1 alpha gene of Drosophila melanogaster is
RT developmentally regulated and the kinase activity of the protein
RT induced by DNA damage.";
RL J. Cell Sci. 109:1847-1856(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RX MEDLINE=22426069; PubMed=12537572;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX MEDLINE=22426066; PubMed=12537569;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA Rubin G.M., Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
Feature:
CHAIN 1 337 Casein kinase I isoform alpha.
/FTId=PRO_0000192848.
DOMAIN 20 288 Protein kinase.
NP_BIND 26 34 ATP (By similarity).
ACT_SITE 139 139 Proton acceptor (By similarity).
BINDING 49 49 ATP (By similarity).
CONFLICT 1 3 Missing (in Ref. 2).
CONFLICT 331 337 GKPLIAD -> ASP (in Ref. 2).
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 (By similarity).
-!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
-!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. Casein
kinase I subfamily.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
Sequence length: 337
MDKMRILKES RPEIIVGGKY RVIRKIGSGS FGDIYLGMSI QSGEEVAIKM ESAHARHPQL
LYEAKLYRIL SGGVGFPRIR HHGKEKNFNT LVMDLLGPSL EDLFNFCTRH FTIKTVLMLV
DQMIGRLEYI HLKCFIHRDI KPDNFLMGIG RHCNKLFLID FGLAKKFRDP HTRHHIVYRE
DKNLTGTARY ASINAHLGIE QSRRDDMESL GYVMMYFNRG VLPWQGMKAN TKQQKYEKIS
EKKMSTPIEV LCKGSPAEFS MYLNYCRSLR FEEQPDYMYL RQLFRILFRT LNHQYDYIYD
WTMLKQKTHQ GQPNPAILLE QLDKDKEKQN GKPLIAD