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Reviewed, UniProtKB/Swiss-Prot P54367 (KC1A_DROME)

Last modified February 9, 2010. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Casein kinase I isoform alpha
      Short name=CKI-alpha
      Short name=DmCK1
    EC=2.7.11.1
Gene names
Name: CkIalpha
Synonyms: CKI
ORF Names: CG2028
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (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. May be required for mechanisms associated with DNA repair during early embryogenesis. Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium. Ref.2

Subcellular location

Cytoplasm. Nucleus. Note: Levels in the nucleus are significantly increased after DNA damage. Ref.2

Developmental stage

Expressed both maternally and zygotically. Ref.2

Induction

By DNA damage. Ref.2

Post-translational modification

Phosphorylated. Dephosphorylated kinase is active in the cytoplasm, the active kinase in the nucleus is phosphorylated.

Sequence similarities

Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.

Contains 1 protein kinase domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Casein kinase I isoform alpha
PRO_0000192848

Regions

Domain20 – 288269Protein kinase
Nucleotide binding26 – 349ATP By similarity

Sites

Active site1391Proton acceptor By similarity
Binding site491ATP By similarity

Experimental info

Sequence conflict331 – 3377GKPLIAD → ASP in CAA64358. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P54367-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 495144945093E69D

FASTA33739,535
        10         20         30         40         50         60 
MDKMRILKES RPEIIVGGKY RVIRKIGSGS FGDIYLGMSI QSGEEVAIKM ESAHARHPQL 

        70         80         90        100        110        120 
LYEAKLYRIL SGGVGFPRIR HHGKEKNFNT LVMDLLGPSL EDLFNFCTRH FTIKTVLMLV 

       130        140        150        160        170        180 
DQMIGRLEYI HLKCFIHRDI KPDNFLMGIG RHCNKLFLID FGLAKKFRDP HTRHHIVYRE 

       190        200        210        220        230        240 
DKNLTGTARY ASINAHLGIE QSRRDDMESL GYVMMYFNRG VLPWQGMKAN TKQQKYEKIS 

       250        260        270        280        290        300 
EKKMSTPIEV LCKGSPAEFS MYLNYCRSLR FEEQPDYMYL RQLFRILFRT LNHQYDYIYD 

       310        320        330 
WTMLKQKTHQ GQPNPAILLE QLDKDKEKQN GKPLIAD

« Hide

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References

« Hide 'large scale' references
[1]Glover C.V.C., Kandala G.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Canton-S.
Tissue: Embryo.
[2]"The casein kinase 1 alpha gene of Drosophila melanogaster is developmentally regulated and the kinase activity of the protein induced by DNA damage."
Santos J.A., Logarinho E., Tapia C., Allende C.C., Allende J.E., Sunkel C.E.
J. Cell Sci. 109:1847-1856(1996) [PubMed: 8832407] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, COFACTOR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION.
Strain: Canton-S.
Tissue: Embryo.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U55848 mRNA. Translation: AAB16904.1.
X94695 mRNA. Translation: CAA64358.1. Different initiation.
AE014298 Genomic DNA. Translation: AAF48192.1.
AE014298 Genomic DNA. Translation: AAN09313.1.
AY069346 mRNA. Translation: AAL39491.1.
RefSeqNP_001162737.1.
NP_511140.1.
NP_727631.1.
NP_727632.1.

3D structure databases

SMRP54367. Positions 13-305.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-22041N.
IntActP54367. 5 interactions.
STRINGP54367.

Proteomic databases

PRIDEP54367.

Genome annotation databases

EnsemblFBtr0073680; FBpp0073513; FBgn0015024; Drosophila melanogaster. [Genome view]
FBtr0073681; FBpp0073514; FBgn0015024; Drosophila melanogaster. [Genome view]
FBtr0073682; FBpp0073515; FBgn0015024; Drosophila melanogaster. [Genome view]
FBtr0300380; FBpp0289609; FBgn0015024; Drosophila melanogaster. [Genome view]
GeneID32221.
KEGGdme:Dmel_CG2028.

Organism-specific databases

CTD32221.
FlyBaseFBgn0015024. CkIalpha.

Phylogenomic databases

eggNOGinNOG05782.
InParanoidP54367.
OMAMIGRIEY.
OrthoDBEOG9NCMK8.
PhylomeDBP54367.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-001649-MONOMER.
DMEL-XXX-02:DMEL-XXX-02-001650-MONOMER.
DMEL-XXX-02:DMEL-XXX-02-001651-MONOMER.
BRENDA2.7.11.1. 48.

Gene expression databases

GermOnlineCG2028. Drosophila melanogaster.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio777455.

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Entry information

Entry nameKC1A_DROME
AccessionPrimary (citable) accession number: P54367
Secondary accession number(s): A4V4D3, Q0KHT2, Q9VYK2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 9, 2010
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents