CSK2B_ARATH
ID CSK2B_ARATH Reviewed; 287 AA.
AC P40228;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Casein kinase II subunit beta-1 {ECO:0000305};
DE Short=CK II beta-1 {ECO:0000305};
GN Name=CKB1; OrderedLocusNames=At5g47080; ORFNames=K14A3.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8061317; DOI=10.1007/bf00029603;
RA Collinge M.A., Walker J.C.;
RT "Isolation of an Arabidopsis thaliana casein kinase II beta subunit by
RT complementation in Saccharomyces cerevisiae.";
RL Plant Mol. Biol. 25:649-658(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=7696877; DOI=10.2307/3869841;
RA Klimczak L.J., Collinge M.A., Farini D., Giuliano G., Walker J.C.,
RA Cashmore A.R.;
RT "Reconstitution of Arabidopsis casein kinase II from recombinant subunits
RT and phosphorylation of transcription factor GBF1.";
RL Plant Cell 7:105-115(1995).
RN [5]
RP INTERACTION WITH CCA1.
RX PubMed=9724822; DOI=10.1073/pnas.95.18.11020;
RA Sugano S., Andronis C., Green R.M., Wang Z.-Y., Tobin E.M.;
RT "Protein kinase CK2 interacts with and phosphorylates the Arabidopsis
RT circadian clock-associated 1 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11020-11025(1998).
RN [6]
RP INTERACTION WITH LHY.
RX PubMed=10535927; DOI=10.1073/pnas.96.22.12362;
RA Sugano S., Andronis C., Ong M.S., Green R.M., Tobin E.M.;
RT "The protein kinase CK2 is involved in regulation of circadian rhythms in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12362-12366(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=16926165; DOI=10.1093/pcp/pcj100;
RA Salinas P., Fuentes D., Vidal E., Jordana X., Echeverria M., Holuigue L.;
RT "An extensive survey of CK2 alpha and beta subunits in Arabidopsis:
RT multiple isoforms exhibit differential subcellular localization.";
RL Plant Cell Physiol. 47:1295-1308(2006).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19509278; DOI=10.1074/jbc.m109.006692;
RA Dennis M.D., Browning K.S.;
RT "Differential phosphorylation of plant translation initiation factors by
RT Arabidopsis thaliana CK2 holoenzymes.";
RL J. Biol. Chem. 284:20602-20614(2009).
RN [9]
RP FUNCTION.
RX PubMed=19509420; DOI=10.1074/jbc.m109.007658;
RA Dennis M.D., Person M.D., Browning K.S.;
RT "Phosphorylation of plant translation initiation factors by CK2 enhances
RT the in vitro interaction of multifactor complex components.";
RL J. Biol. Chem. 284:20615-20628(2009).
RN [10]
RP FUNCTION.
RX PubMed=21330376; DOI=10.1074/jbc.m110.186882;
RA Bu Q., Zhu L., Dennis M.D., Yu L., Lu S.X., Person M.D., Tobin E.M.,
RA Browning K.S., Huq E.;
RT "Phosphorylation by CK2 enhances the rapid light-induced degradation of
RT phytochrome interacting factor 1 in Arabidopsis.";
RL J. Biol. Chem. 286:12066-12074(2011).
CC -!- FUNCTION: Plays a complex role in regulating the basal catalytic
CC activity of the alpha subunit. The tetrameric holoenzyme CK2, composed
CC of two alpha and two beta subunits, phosphorylates the transcription
CC factor GBFl, resulting in stimulation of its DNA binding activity
CC (PubMed:7696877). CK2 phosphorylates the transcription factor PIF1
CC after an exposure to light, resulting in a proteasome-dependent
CC degradation of PIF1 and promotion of photomorphogenesis
CC (PubMed:21330376). CK2 phosphorylates translation initiation factors.
CC May participate in the regulation of the initiation of translation
CC (PubMed:19509278, PubMed:19509420). Stimulates the binding of CCA1 to
CC promoters (Probable). {ECO:0000269|PubMed:19509278,
CC ECO:0000269|PubMed:19509420, ECO:0000269|PubMed:21330376,
CC ECO:0000269|PubMed:7696877, ECO:0000305|PubMed:9724822}.
CC -!- SUBUNIT: Heterotetramer of two catalytic alpha subunits and two
CC regulatory beta subunits (PubMed:7696877, PubMed:19509278). Interacts
CC with CCA1 (PubMed:9724822). Interacts with LHY (PubMed:10535927).
CC {ECO:0000269|PubMed:10535927, ECO:0000269|PubMed:19509278,
CC ECO:0000269|PubMed:7696877, ECO:0000269|PubMed:9724822}.
CC -!- INTERACTION:
CC P40228; P92973: CCA1; NbExp=3; IntAct=EBI-1644917, EBI-1644880;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16926165}.
CC Nucleus {ECO:0000269|PubMed:16926165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P40228-1; Sequence=Displayed;
CC -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000305}.
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DR EMBL; L22563; AAA53233.1; -; mRNA.
DR EMBL; AB025609; BAA98103.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95466.1; -; Genomic_DNA.
DR PIR; S47967; S47967.
DR RefSeq; NP_199519.1; NM_124079.4. [P40228-1]
DR AlphaFoldDB; P40228; -.
DR SMR; P40228; -.
DR BioGRID; 20002; 2.
DR IntAct; P40228; 2.
DR STRING; 3702.AT5G47080.1; -.
DR PaxDb; P40228; -.
DR ProteomicsDB; 222655; -. [P40228-1]
DR EnsemblPlants; AT5G47080.1; AT5G47080.1; AT5G47080. [P40228-1]
DR GeneID; 834754; -.
DR Gramene; AT5G47080.1; AT5G47080.1; AT5G47080. [P40228-1]
DR KEGG; ath:AT5G47080; -.
DR Araport; AT5G47080; -.
DR TAIR; locus:2152002; AT5G47080.
DR eggNOG; KOG3092; Eukaryota.
DR InParanoid; P40228; -.
DR OMA; QIPEAYL; -.
DR OrthoDB; 1335521at2759; -.
DR PhylomeDB; P40228; -.
DR PRO; PR:P40228; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P40228; baseline and differential.
DR Genevisible; P40228; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:TAIR.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0071900; P:regulation of protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..287
FT /note="Casein kinase II subunit beta-1"
FT /id="PRO_0000068248"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 32355 MW; 43C811727B0985EE CRC64;
MYRDRGTVNS RPEVVDRKRI NDALERPSPS TSRQVNGKGK GTVTAATTTA NLIGKQQSNN
INHRDSRSAS LSKNNTVSDD ESDTDSEESD VSGSDGEDTS WISWFCNLRG NEFFCEVDDD
YIQDDFNLCG LSSLVPYYEY ALDLILDVES SQGEMFTEEQ NELIESAAEM LYGLIHARYI
LTSKGLAAML DKYKNYDFGR CPRVYCCGQP CLPVGQSDLP RSSTVKIYCP KCEDIYYPRS
KYQGNIDGAY FGTTFPHLFL MTYGHLKPAK ATQNYVQRVF GFKLHKP
