CSK2D_ARATH
ID CSK2D_ARATH Reviewed; 276 AA.
AC O81275; Q24JI1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Casein kinase II subunit beta-3;
DE Short=CK II beta-3;
GN Name=CKB3; OrderedLocusNames=At3g60250; ORFNames=F27H5_40;
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], AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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=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 PIF1 after an exposure to light, resulting in a proteasome-
CC dependent 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). Stimulates the binding of CCA1 to promoters
CC (Probable). {ECO:0000269|PubMed:19509278, ECO:0000269|PubMed:21330376,
CC ECO:0000305|PubMed:9724822}.
CC -!- SUBUNIT: Heterotetramer of two catalytic alpha subunits and two
CC regulatory beta subunits (PubMed:19509278). Interacts with CCA1
CC (PubMed:9724822). Interacts with LHY (PubMed:10535927).
CC {ECO:0000269|PubMed:10535927, ECO:0000269|PubMed:19509278,
CC ECO:0000269|PubMed:9724822}.
CC -!- INTERACTION:
CC O81275; P92973: CCA1; NbExp=6; IntAct=EBI-1644873, 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=O81275-1; 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; AF068318; AAC33896.1; -; mRNA.
DR EMBL; AL163852; CAB87862.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80030.1; -; Genomic_DNA.
DR EMBL; BT024908; ABD91499.1; -; mRNA.
DR EMBL; AK229231; BAF01098.1; -; mRNA.
DR PIR; T49220; T49220.
DR RefSeq; NP_191584.1; NM_115889.5. [O81275-1]
DR AlphaFoldDB; O81275; -.
DR SMR; O81275; -.
DR BioGRID; 10510; 7.
DR IntAct; O81275; 3.
DR STRING; 3702.AT3G60250.1; -.
DR PaxDb; O81275; -.
DR PRIDE; O81275; -.
DR ProteomicsDB; 220358; -. [O81275-1]
DR EnsemblPlants; AT3G60250.1; AT3G60250.1; AT3G60250. [O81275-1]
DR GeneID; 825196; -.
DR Gramene; AT3G60250.1; AT3G60250.1; AT3G60250. [O81275-1]
DR KEGG; ath:AT3G60250; -.
DR Araport; AT3G60250; -.
DR TAIR; locus:2081937; AT3G60250.
DR eggNOG; KOG3092; Eukaryota.
DR HOGENOM; CLU_034027_3_1_1; -.
DR InParanoid; O81275; -.
DR OMA; DETGWIQ; -.
DR OrthoDB; 1335521at2759; -.
DR PhylomeDB; O81275; -.
DR PRO; PR:O81275; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O81275; baseline and differential.
DR Genevisible; O81275; 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:0042752; P:regulation of circadian rhythm; IMP: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..276
FT /note="Casein kinase II subunit beta-3"
FT /id="PRO_0000068250"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 30798 MW; 611FFC1222B2CC55 CRC64;
MYKERSGGGG GGSSRSEILG GAIDRKRIND ALNKKLEKSS TSTTTSRVFS SKDKDPFSFT
STKTQLPDVE SETDSEGSDV SGSEGDDTSW ISWFCNLRGN DFFCEVDEDY IQDDFNLCGL
SGQVPYYDYA LDLILDVDAS NSEMFTDEQH EMVESAAEML YGLIHVRYIL TTKGMAAMTE
KYKNCDFGRC PRVFCCGQSC LPVGQSDIPR SSTVKIYCPK CEDISYPRSK FQGNIDGAYF
GTTFPHLFLM TYGNLKPQKP TQSYVPKIFG FKVHKP
