CSK2A_DROME
ID CSK2A_DROME Reviewed; 336 AA.
AC P08181; Q0E8B4; Q9W5T2;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II subunit alpha;
DE EC=2.7.11.1 {ECO:0000269|PubMed:24615015};
GN Name=CkIIalpha; Synonyms=Cask-II-a; ORFNames=CG17520;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3119988; DOI=10.1128/mcb.7.10.3409-3417.1987;
RA Saxena A., Padmanabha R., Glover C.V.C.;
RT "Isolation and sequencing of cDNA clones encoding alpha and beta subunits
RT of Drosophila melanogaster casein kinase II.";
RL Mol. Cell. Biol. 7:3409-3417(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX 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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PROTEIN SEQUENCE OF 2-42.
RX PubMed=3468112; DOI=10.1016/s0021-9258(19)75714-7;
RA Padmanabha R., Glover C.V.C.;
RT "Casein kinase II of yeast contains two distinct alpha polypeptides and an
RT unusually large beta subunit.";
RL J. Biol. Chem. 262:1829-1835(1987).
RN [6]
RP CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24615015; DOI=10.1128/mcb.00658-13;
RA Hovhanyan A., Herter E.K., Pfannstiel J., Gallant P., Raabe T.;
RT "Drosophila mbm is a nucleolar myc and casein kinase 2 target required for
RT ribosome biogenesis and cell growth of central brain neuroblasts.";
RL Mol. Cell. Biol. 34:1878-1891(2014).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. The alpha chain contains the catalytic site. May
CC participate in Wnt signaling.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:24615015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:24615015};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24615015};
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC -!- INTERACTION:
CC P08181; O96863: CkIIbeta2; NbExp=3; IntAct=EBI-93115, EBI-181456;
CC P08181; O61735: Clk; NbExp=2; IntAct=EBI-93115, EBI-143834;
CC P08181; P13098: E(spl)m8-HLH; NbExp=3; IntAct=EBI-93115, EBI-185388;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:24615015}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in
CC mislocalization of mbm in interphase cells with partial localization to
CC the cytoplasm as well as nucleolar expression.
CC {ECO:0000269|PubMed:24615015}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M16534; AAA28429.1; -; mRNA.
DR EMBL; AE014296; AAN11415.1; -; Genomic_DNA.
DR EMBL; AY069553; AAL39698.1; -; mRNA.
DR PIR; A26688; A26688.
DR RefSeq; NP_001036624.1; NM_001043159.3.
DR RefSeq; NP_001287151.1; NM_001300222.1.
DR RefSeq; NP_001287152.1; NM_001300223.1.
DR RefSeq; NP_001287153.1; NM_001300224.1.
DR RefSeq; NP_524918.1; NM_080179.5.
DR RefSeq; NP_730774.1; NM_168985.2.
DR RefSeq; NP_730775.1; NM_168986.2.
DR AlphaFoldDB; P08181; -.
DR SMR; P08181; -.
DR BioGRID; 71396; 50.
DR DIP; DIP-18339N; -.
DR IntAct; P08181; 22.
DR MINT; P08181; -.
DR STRING; 7227.FBpp0110433; -.
DR PaxDb; P08181; -.
DR PRIDE; P08181; -.
DR DNASU; 48448; -.
DR EnsemblMetazoa; FBtr0070042; FBpp0070041; FBgn0264492.
DR EnsemblMetazoa; FBtr0070043; FBpp0070042; FBgn0264492.
DR EnsemblMetazoa; FBtr0070044; FBpp0070043; FBgn0264492.
DR EnsemblMetazoa; FBtr0111141; FBpp0110433; FBgn0264492.
DR EnsemblMetazoa; FBtr0344974; FBpp0311229; FBgn0264492.
DR EnsemblMetazoa; FBtr0345138; FBpp0311359; FBgn0264492.
DR EnsemblMetazoa; FBtr0345139; FBpp0311360; FBgn0264492.
DR GeneID; 48448; -.
DR KEGG; dme:Dmel_CG17520; -.
DR CTD; 48448; -.
DR FlyBase; FBgn0264492; CkIIalpha.
DR VEuPathDB; VectorBase:FBgn0264492; -.
DR eggNOG; KOG0668; Eukaryota.
DR GeneTree; ENSGT00390000004215; -.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; P08181; -.
DR OMA; RAYWDYD; -.
DR OrthoDB; 1098380at2759; -.
DR PhylomeDB; P08181; -.
DR BRENDA; 2.7.11.1; 1994.
DR Reactome; R-DME-201688; WNT mediated activation of DVL.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-DME-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
DR SignaLink; P08181; -.
DR BioGRID-ORCS; 48448; 1 hit in 3 CRISPR screens.
DR ChiTaRS; CkIIalpha; fly.
DR GenomeRNAi; 48448; -.
DR PRO; PR:P08181; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0264492; Expressed in cleaving embryo and 22 other tissues.
DR ExpressionAtlas; P08181; baseline and differential.
DR Genevisible; P08181; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0002118; P:aggressive behavior; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0060810; P:intracellular mRNA localization involved in pattern specification process; IGI:FlyBase.
DR GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IMP:FlyBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14132; STKc_CK2_alpha; 1.
DR InterPro; IPR045216; CK2_alpha.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24054; PTHR24054; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3468112"
FT CHAIN 2..336
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085900"
FT DOMAIN 37..322
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 336 AA; 39960 MW; 69D15F124427B21E CRC64;
MTLPSAARVY TDVNAHKPDE YWDYENYVVD WGNQDDYQLV RKLGRGKYSE VFEAINITTT
EKCVVKILKP VKKKKIKREI KILENLRGGT NIITLLAVVK DPVSRTPALI FEHVNNTDFK
QLYQTLTDYE IRYYLFELLK ALDYCHSMGI MHRDVKPHNV MIDHENRKLR LIDWGLAEFY
HPGQEYNVRV ASRYFKGPEL LVDYQMYDYS LDMWSLGCML ASMIFRKEPF FHGHDNYDQL
VRIAKVLGTE ELYAYLDKYN IDLDPRFHDI LQRHSRKRWE RFVHSDNQHL VSPEALDFLD
KLLRYDHVDR LTAREAMAHP YFLPIVNGQM NPNNQQ
