CSK2E_ARATH
ID CSK2E_ARATH Reviewed; 283 AA.
AC O80507; Q941C4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative casein kinase II subunit beta-4;
DE Short=CK II beta-4;
GN Name=CKB4 {ECO:0000305}; OrderedLocusNames=At2g44680; ORFNames=F16B22.17;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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). {ECO:0000269|PubMed:19509278,
CC ECO:0000269|PubMed:21330376}.
CC -!- SUBUNIT: Heterotetramer of two catalytic alpha subunits and two
CC regulatory beta subunits. {ECO:0000269|PubMed:19509278}.
CC -!- INTERACTION:
CC O80507; Q8H1R0: PYL10; NbExp=5; IntAct=EBI-25528847, EBI-2363213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16926165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O80507-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80507-2; Sequence=VSP_009188;
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; AC003672; AAC27470.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10454.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10455.1; -; Genomic_DNA.
DR EMBL; AY052265; AAK97735.1; -; mRNA.
DR EMBL; AY062585; AAL32663.1; -; mRNA.
DR EMBL; AY060523; AAL31136.1; -; mRNA.
DR EMBL; AY093344; AAM13343.1; -; mRNA.
DR EMBL; AY088075; AAM65621.1; -; mRNA.
DR PIR; T01595; T01595.
DR RefSeq; NP_181996.1; NM_130032.3. [O80507-1]
DR RefSeq; NP_850421.1; NM_180090.2. [O80507-2]
DR AlphaFoldDB; O80507; -.
DR SMR; O80507; -.
DR BioGRID; 4412; 6.
DR IntAct; O80507; 1.
DR STRING; 3702.AT2G44680.1; -.
DR PaxDb; O80507; -.
DR PRIDE; O80507; -.
DR ProteomicsDB; 220359; -. [O80507-1]
DR EnsemblPlants; AT2G44680.1; AT2G44680.1; AT2G44680. [O80507-1]
DR EnsemblPlants; AT2G44680.2; AT2G44680.2; AT2G44680. [O80507-2]
DR GeneID; 819076; -.
DR Gramene; AT2G44680.1; AT2G44680.1; AT2G44680. [O80507-1]
DR Gramene; AT2G44680.2; AT2G44680.2; AT2G44680. [O80507-2]
DR KEGG; ath:AT2G44680; -.
DR Araport; AT2G44680; -.
DR TAIR; locus:2042431; AT2G44680.
DR eggNOG; KOG3092; Eukaryota.
DR HOGENOM; CLU_034027_3_1_1; -.
DR InParanoid; O80507; -.
DR OMA; FPEMFLM; -.
DR OrthoDB; 1335521at2759; -.
DR PhylomeDB; O80507; -.
DR PRO; PR:O80507; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80507; baseline and differential.
DR Genevisible; O80507; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005956; C:protein kinase CK2 complex; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IMP:TAIR.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0042753; P:positive 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; Phosphoprotein; Reference proteome.
FT CHAIN 1..283
FT /note="Putative casein kinase II subunit beta-4"
FT /id="PRO_0000068251"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 239..240
FT /note="GN -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_009188"
SQ SEQUENCE 283 AA; 31631 MW; DF5811A78F060797 CRC64;
MYKDRSGGGI MGGGGSSRSE ILGGAIDRKR INDALDKHLK KSSPSTSRVF TSKDKDSVPS
TSTAKSQLHS RSPDVESDTD SEGSDVSGSE GDDTSWISWF CNLRGNEFFC EVDEDYIQDD
FNLCGLSGQV PYYDYALDLI LDVESSNGDM FTEEQHEMVE SAAEMLYGLI HVRYILTTKG
MAAMMEKYKN YDFGRCPRVF CCGQSCLPVG QSDIPRSSTV KIYCPKCEDI YYPRSKYQGN
IDGAYFGTTF PHLFLMAYGN MKPQKPAQNY VPKIFGFKVH NKQ
