CSK21_ARATH
ID CSK21_ARATH Reviewed; 409 AA.
AC Q08467; B9DH00; B9DHA8; F4K3Q1; Q94F17; Q9FN14;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Casein kinase II subunit alpha-1;
DE Short=CK II;
DE EC=2.7.11.1 {ECO:0000269|PubMed:7696877};
DE AltName: Full=Casein kinase alpha 1;
DE Short=AtCKA1 {ECO:0000303|PubMed:7678767};
DE Flags: Precursor;
GN Name=CKA1 {ECO:0000303|PubMed:7678767}; OrderedLocusNames=At5g67380;
GN ORFNames=K8K14.10;
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] (ISOFORM 3), FUNCTION, ACTIVITY REGULATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7678767; DOI=10.1007/bf00019944;
RA Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N., Kamada H.,
RA Shinozaki K.;
RT "Cloning and characterization of two cDNAs encoding casein kinase II
RT catalytic subunits in Arabidopsis thaliana.";
RL Plant Mol. Biol. 21:279-289(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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] (ISOFORM 4).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, 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 [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).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21900482; DOI=10.1104/pp.111.179846;
RA Lu S.X., Liu H., Knowles S.M., Li J., Ma L., Tobin E.M., Lin C.;
RT "A role for protein kinase casein kinase2 alpha-subunits in the Arabidopsis
RT circadian clock.";
RL Plant Physiol. 157:1537-1545(2011).
RN [12]
RP FUNCTION.
RX PubMed=22487192; DOI=10.1111/j.1365-313x.2012.05019.x;
RA Moreno-Romero J., Armengot L., Mar Marques-Bueno M., Britt A.,
RA Carmen Martinez M.;
RT "CK2-defective Arabidopsis plants exhibit enhanced double-strand break
RT repair rates and reduced survival after exposure to ionizing radiation.";
RL Plant J. 71:627-638(2012).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. Phosphorylates casein in vitro (PubMed:7678767). The alpha
CC chain contains the catalytic site. The tetrameric holoenzyme CK2,
CC composed of two alpha and two beta subunits, phosphorylates the
CC transcription factor GBFl, resulting in stimulation of its DNA binding
CC activity (PubMed:7696877). CK2 phosphorylates the transcription factor
CC PIF1 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). Acts as circadian clock component
CC that maintains the correct period length through phosphorylation of
CC CCA1 (PubMed:21900482). Required for the maintenance and control of
CC genomic stability and chromatin structure (PubMed:22487192). May act as
CC an ectokinase that phosphorylates several extracellular proteins.
CC {ECO:0000269|PubMed:19509278, ECO:0000269|PubMed:19509420,
CC ECO:0000269|PubMed:21330376, ECO:0000269|PubMed:21900482,
CC ECO:0000269|PubMed:22487192, ECO:0000269|PubMed:7678767,
CC ECO:0000269|PubMed:7696877}.
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:7696877};
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:7696877};
CC -!- ACTIVITY REGULATION: Inhibited by heparin.
CC {ECO:0000269|PubMed:7678767}.
CC -!- SUBUNIT: Heterotetramer of two catalytic alpha subunits and two
CC regulatory beta subunits. {ECO:0000269|PubMed:19509278,
CC ECO:0000269|PubMed:7696877}.
CC -!- INTERACTION:
CC Q08467; P92973: CCA1; NbExp=4; IntAct=EBI-1644972, EBI-1644880;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16926165}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:16926165}. Note=Enriched in the
CC nucleolus. {ECO:0000269|PubMed:16926165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q08467-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08467-2; Sequence=VSP_043759;
CC Name=3;
CC IsoId=Q08467-3; Sequence=VSP_043758;
CC Name=4;
CC IsoId=Q08467-4; Sequence=VSP_043757;
CC -!- TISSUE SPECIFICITY: Seems to be present in all plant organs. But seems
CC to be less expressed than CKA2. {ECO:0000269|PubMed:7678767}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the triple mutant cka1, cka2 and cka3 show altered
CC circadian rhythms and delayed flowering under long day conditions.
CC {ECO:0000269|PubMed:21900482}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; D10246; BAA01090.1; -; mRNA.
DR EMBL; AB007645; BAB09023.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98334.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98335.1; -; Genomic_DNA.
DR EMBL; AF386966; AAK62411.1; -; mRNA.
DR EMBL; BT002141; AAN72152.1; -; mRNA.
DR EMBL; AK317345; BAH20017.1; -; mRNA.
DR EMBL; AK317458; BAH20125.1; -; mRNA.
DR PIR; S31098; S31098.
DR RefSeq; NP_001032165.1; NM_001037088.2. [Q08467-2]
DR RefSeq; NP_201539.2; NM_126138.4. [Q08467-1]
DR PDB; 6XX6; X-ray; 1.85 A; A=77-409.
DR PDB; 6XX7; X-ray; 2.40 A; A=77-409.
DR PDB; 6XX8; X-ray; 1.80 A; A/B=77-409.
DR PDB; 6XX9; X-ray; 1.84 A; A=77-409.
DR PDB; 6Z1C; X-ray; 1.75 A; A=78-409.
DR PDBsum; 6XX6; -.
DR PDBsum; 6XX7; -.
DR PDBsum; 6XX8; -.
DR PDBsum; 6XX9; -.
DR PDBsum; 6Z1C; -.
DR AlphaFoldDB; Q08467; -.
DR SMR; Q08467; -.
DR BioGRID; 22115; 28.
DR IntAct; Q08467; 11.
DR STRING; 3702.AT5G67380.1; -.
DR PaxDb; Q08467; -.
DR PRIDE; Q08467; -.
DR ProteomicsDB; 224419; -. [Q08467-1]
DR EnsemblPlants; AT5G67380.1; AT5G67380.1; AT5G67380. [Q08467-1]
DR EnsemblPlants; AT5G67380.2; AT5G67380.2; AT5G67380. [Q08467-2]
DR GeneID; 836873; -.
DR Gramene; AT5G67380.1; AT5G67380.1; AT5G67380. [Q08467-1]
DR Gramene; AT5G67380.2; AT5G67380.2; AT5G67380. [Q08467-2]
DR KEGG; ath:AT5G67380; -.
DR Araport; AT5G67380; -.
DR eggNOG; KOG0668; Eukaryota.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; Q08467; -.
DR OMA; NSKEKCI; -.
DR OrthoDB; 1098380at2759; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:Q08467; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q08467; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
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 3D-structure; Alternative splicing; ATP-binding; Glycoprotein; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..409
FT /note="Casein kinase II subunit alpha-1"
FT /id="PRO_0000417491"
FT DOMAIN 110..395
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 116..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..223
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_043757"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7678767"
FT /id="VSP_043758"
FT VAR_SEQ 115..147
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_043759"
FT CONFLICT 223
FT /note="I -> L (in Ref. 1; BAA01090)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> V (in Ref. 1; BAA01090)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..297
FT /note="MI -> LL (in Ref. 1; BAA01090)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..320
FT /note="VL -> GV (in Ref. 1; BAA01090)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="R -> G (in Ref. 5; BAH20017)"
FT /evidence="ECO:0000305"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6XX9"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:6XX8"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6XX9"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:6Z1C"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 201..220
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6Z1C"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 283..298
FT /evidence="ECO:0007829|PDB:6Z1C"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:6Z1C"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 386..390
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:6Z1C"
FT HELIX 396..409
FT /evidence="ECO:0007829|PDB:6Z1C"
SQ SEQUENCE 409 AA; 47640 MW; 35F553B9CDA53D33 CRC64;
MIDTLFFLFF LFFDSPLRRL LLLCAVLALR APTAHSPILR SSIVTPTARA VSEVSGCTTI
DPDFLVEISD SNQTRAMSKA RVYTEVNVIR PKDYWDYESL IVQWGEQDDY EVVRKVGRGK
YSEVFEGINV NSKEKCIIKI LKPVKKKKIR REIKILQNLC GGPNIVKLLD VVRDQHSKTP
SLIFEYVNST DFKVLYPTLT DYDIRYYIYE LLKALDFCHS QGIMHRDVKP HNVMIDHELR
KLRLIDWGLA EFYHPGKEYN VRVASRYFKG PELLVDLQDY DYSLDMWSLG CMFAGMIFRK
EPFFYGHDNQ DQLVKIAKVL GTDELNAYLN KYQLELDPQL EALVGRHSRK PWSKFINADN
QHLVSPEAID FLDKLLRYDH QDRLTAKEAM AHAYFAQVRA AETSRMRSQ
