CSK2B_DROME
ID CSK2B_DROME Reviewed; 235 AA.
AC P08182; Q76NS4; Q9VYU4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Casein kinase II subunit beta;
DE Short=CK II beta;
GN Name=CkIIbeta; Synonyms=Cask-II-b; ORFNames=CG15224;
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] (ISOFORM B), AND FUNCTION.
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 [GENOMIC DNA].
RC STRAIN=Oregon-R;
RA Glover C.V.C., Beckman J.S., Bidwai A.P., Carlson L.K., Cerjan C.M.,
RA Crawford M.J., McCann R.O., Saxena A., Zhao W.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
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).
CC -!- FUNCTION: Participates in Wnt signaling (By similarity). Plays a
CC complex role in regulating the basal catalytic activity of the alpha
CC subunit. {ECO:0000250, ECO:0000269|PubMed:3119988}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=E;
CC IsoId=P08182-1; Sequence=Displayed;
CC Name=B; Synonyms=G;
CC IsoId=P08182-3; Sequence=VSP_011641;
CC -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M16535; AAA28430.1; -; mRNA.
DR EMBL; U52952; AAC13880.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48092.3; -; Genomic_DNA.
DR EMBL; AE014298; AAF48093.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65321.1; -; Genomic_DNA.
DR EMBL; AY113447; AAM29452.1; -; mRNA.
DR RefSeq; NP_001014731.1; NM_001014731.2. [P08182-3]
DR RefSeq; NP_001245628.1; NM_001258699.1. [P08182-3]
DR RefSeq; NP_511131.3; NM_078576.5. [P08182-3]
DR RefSeq; NP_542940.1; NM_080762.4. [P08182-3]
DR RefSeq; NP_727561.1; NM_167304.3. [P08182-3]
DR RefSeq; NP_727562.1; NM_167305.3. [P08182-3]
DR RefSeq; NP_996415.1; NM_206692.3. [P08182-1]
DR AlphaFoldDB; P08182; -.
DR SMR; P08182; -.
DR BioGRID; 58538; 65.
DR DIP; DIP-17048N; -.
DR IntAct; P08182; 14.
DR MINT; P08182; -.
DR STRING; 7227.FBpp0089135; -.
DR iPTMnet; P08182; -.
DR PaxDb; P08182; -.
DR DNASU; 32132; -.
DR EnsemblMetazoa; FBtr0073558; FBpp0073403; FBgn0000259. [P08182-3]
DR EnsemblMetazoa; FBtr0073560; FBpp0073405; FBgn0000259. [P08182-3]
DR EnsemblMetazoa; FBtr0073561; FBpp0073406; FBgn0000259. [P08182-3]
DR EnsemblMetazoa; FBtr0073562; FBpp0089135; FBgn0000259. [P08182-1]
DR EnsemblMetazoa; FBtr0100540; FBpp0099985; FBgn0000259. [P08182-3]
DR EnsemblMetazoa; FBtr0299569; FBpp0288844; FBgn0000259. [P08182-3]
DR EnsemblMetazoa; FBtr0307896; FBpp0300330; FBgn0000259. [P08182-3]
DR GeneID; 32132; -.
DR KEGG; dme:Dmel_CG15224; -.
DR CTD; 32132; -.
DR FlyBase; FBgn0000259; CkIIbeta.
DR VEuPathDB; VectorBase:FBgn0000259; -.
DR eggNOG; KOG3092; Eukaryota.
DR GeneTree; ENSGT00390000003781; -.
DR InParanoid; P08182; -.
DR OMA; DADFGRC; -.
DR PhylomeDB; P08182; -.
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-6798695; Neutrophil degranulation.
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; P08182; -.
DR BioGRID-ORCS; 32132; 2 hits in 3 CRISPR screens.
DR ChiTaRS; CkIIbeta; fly.
DR GenomeRNAi; 32132; -.
DR PRO; PR:P08182; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000259; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P08182; baseline and differential.
DR Genevisible; P08182; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:FlyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0008062; P:eclosion rhythm; TAS:FlyBase.
DR GO; GO:0060810; P:intracellular mRNA localization involved in pattern specification process; IGI:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0007622; P:rhythmic behavior; TAS:FlyBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1820.10; -; 1.
DR InterPro; IPR016149; Casein_kin_II_reg-sub_N.
DR InterPro; IPR035991; Casein_kinase_II_beta-like.
DR InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR PANTHER; PTHR11740; PTHR11740; 1.
DR Pfam; PF01214; CK_II_beta; 1.
DR PRINTS; PR00472; CASNKINASEII.
DR SMART; SM01085; CK_II_beta; 1.
DR SUPFAM; SSF57798; SSF57798; 1.
DR PROSITE; PS01101; CK2_BETA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..235
FT /note="Casein kinase II subunit beta"
FT /id="PRO_0000068245"
FT REGION 213..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000305"
FT VAR_SEQ 214..235
FT /note="QRGQPPKDEEPENNADTVPKRL -> KN (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:3119988"
FT /id="VSP_011641"
SQ SEQUENCE 235 AA; 27088 MW; 8109CBF2A2B543B1 CRC64;
MSSSEEVSWV TWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPNYRQAL DMILDLEPED
ELEDNPLQSD MTEQAAEMLY GLIHARYILT NRGIAQMIEK YQTGDFGHCP RVYCESQPML
PLGLSDIPGE AMVKTYCPKC IDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPT
NQFVPRLYGF KIHSLAYQIQ LQAAANFKMP LRAQRGQPPK DEEPENNADT VPKRL
