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Casein kinase II subunit alpha-2 (CK II) (EC 2.7.11.1) (Casein kinase alpha 2) (AtCKA2)

 CSK22_ARATH             Reviewed;         403 AA.
Q08466; Q8H120; Q8H765; Q9SN18;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
16-MAY-2012, sequence version 3.
23-MAY-2018, entry version 134.
RecName: Full=Casein kinase II subunit alpha-2;
Short=CK II;
EC=2.7.11.1;
AltName: Full=Casein kinase alpha 2 {ECO:0000305};
Short=AtCKA2 {ECO:0000303|PubMed:7678767};
Flags: Precursor;
Name=CKA2 {ECO:0000303|PubMed:7678767}; OrderedLocusNames=At3g50000;
ORFNames=F3A4.80;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=7678767; DOI=10.1007/BF00019944;
Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N., Kamada H.,
Shinozaki K.;
"Cloning and characterization of two cDNAs encoding casein kinase II
catalytic subunits in Arabidopsis thaliana.";
Plant Mol. Biol. 21:279-289(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
SUBCELLULAR LOCATION.
PubMed=16926165; DOI=10.1093/pcp/pcj100;
Salinas P., Fuentes D., Vidal E., Jordana X., Echeverria M.,
Holuigue L.;
"An extensive survey of CK2 alpha and beta subunits in Arabidopsis:
multiple isoforms exhibit differential subcellular localization.";
Plant Cell Physiol. 47:1295-1308(2006).
[6]
FUNCTION, AND SUBUNIT.
PubMed=19509278; DOI=10.1074/jbc.M109.006692;
Dennis M.D., Browning K.S.;
"Differential phosphorylation of plant translation initiation factors
by Arabidopsis thaliana CK2 holoenzymes.";
J. Biol. Chem. 284:20602-20614(2009).
[7]
FUNCTION.
PubMed=21330376; DOI=10.1074/jbc.M110.186882;
Bu Q., Zhu L., Dennis M.D., Yu L., Lu S.X., Person M.D., Tobin E.M.,
Browning K.S., Huq E.;
"Phosphorylation by CK2 enhances the rapid light-induced degradation
of phytochrome interacting factor 1 in Arabidopsis.";
J. Biol. Chem. 286:12066-12074(2011).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21900482; DOI=10.1104/pp.111.179846;
Lu S.X., Liu H., Knowles S.M., Li J., Ma L., Tobin E.M., Lin C.;
"A role for protein kinase casein kinase2 alpha-subunits in the
Arabidopsis circadian clock.";
Plant Physiol. 157:1537-1545(2011).
-!- FUNCTION: Casein kinases are operationally defined by their
preferential utilization of acidic proteins such as caseins as
substrates (By similarity). The alpha chain contains the catalytic
site. The tetrameric holoenzyme CK2, composed of two alpha and two
beta subunits, phosphorylates the transcription factor PIF1 after
an exposure to light, resulting in a proteasome-dependent
degradation of PIF1 and promotion of photomorphogenesis
(PubMed:21330376). CK2 phosphorylates translation initiation
factors. May participate in the regulation of the initiation of
translation (PubMed:19509278). Acts as circadian clock component
that maintains the correct period length through phosphorylation
of CCA1 (PubMed:21900482). May act as an ectokinase that
phosphorylates several extracellular proteins.
{ECO:0000250|UniProtKB:Q08467, ECO:0000269|PubMed:19509278,
ECO:0000269|PubMed:21330376, ECO:0000269|PubMed:21900482}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Heterotetramer of two catalytic alpha subunits and two
regulatory beta subunits. {ECO:0000269|PubMed:19509278}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16926165}.
Nucleus, nucleolus {ECO:0000269|PubMed:16926165}. Note=Enriched in
the nucleolus. {ECO:0000269|PubMed:16926165}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q08466-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q08466-2; Sequence=VSP_043760;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Seems to be present in all plant organs. But
seems to be more expressed than CKA1.
{ECO:0000269|PubMed:7678767}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but the triple mutant cka1, cka2 and cka3 show altered
circadian rhythms and delayed flowering under long day conditions.
{ECO:0000269|PubMed:21900482}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CK2 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; D10247; BAA01091.1; -; mRNA.
EMBL; AL132978; CAB62108.1; -; Genomic_DNA.
EMBL; CP002686; AEE78615.1; -; Genomic_DNA.
EMBL; AF370308; AAK44123.2; -; mRNA.
EMBL; BT000888; AAN41288.1; -; mRNA.
PIR; S31099; S31099.
PIR; T45853; T45853.
RefSeq; NP_190569.2; NM_114860.4. [Q08466-1]
UniGene; At.268; -.
ProteinModelPortal; Q08466; -.
SMR; Q08466; -.
BioGrid; 9480; 4.
IntAct; Q08466; 1.
STRING; 3702.AT3G50000.1; -.
PaxDb; Q08466; -.
PRIDE; Q08466; -.
EnsemblPlants; AT3G50000.1; AT3G50000.1; AT3G50000. [Q08466-1]
GeneID; 824162; -.
Gramene; AT3G50000.1; AT3G50000.1; AT3G50000. [Q08466-1]
KEGG; ath:AT3G50000; -.
Araport; AT3G50000; -.
eggNOG; KOG0668; Eukaryota.
eggNOG; ENOG410XNPP; LUCA.
HOGENOM; HOG000233021; -.
InParanoid; Q08466; -.
KO; K03097; -.
OMA; NNTDFRS; -.
OrthoDB; EOG09360EPL; -.
BRENDA; 2.7.11.1; 399.
Reactome; R-ATH-2514853; Condensation of Prometaphase Chromosomes.
Reactome; R-ATH-6804756; Regulation of TP53 Activity through Phosphorylation.
PRO; PR:Q08466; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q08466; baseline and differential.
Genevisible; Q08466; AT.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Glycoprotein;
Kinase; Nucleotide-binding; Nucleus; Reference proteome;
Serine/threonine-protein kinase; Signal; Transferase.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 403 Casein kinase II subunit alpha-2.
/FTId=PRO_0000417492.
DOMAIN 104 389 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 110 118 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 221 221 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 133 133 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 70 Missing (in isoform 2).
{ECO:0000303|PubMed:7678767}.
/FTId=VSP_043760.
CONFLICT 142 142 K -> E (in Ref. 1; BAA01091).
{ECO:0000305}.
CONFLICT 232 232 E -> G (in Ref. 1; BAA01091).
{ECO:0000305}.
SEQUENCE 403 AA; 47233 MW; 495EA87AF560FE83 CRC64;
MHLIFFFSYF LRRYLLLLCA ILILRAPLAH SLIPPLTCVN TGTVESDVTG IRFDRCLDTD
SLAKISLSTV MSKARVYTDV NVIRPKDYWD YESLNVQWGE QDDYEVVRKV GRGKYSEVFE
GINMNNNEKC IIKILKPVKK KKIRREIKIL QNLCGGPNIV KLLDVVRDQH SKTPSLIFEY
VNSTDFKVLY PTLTDYDIRY YIYELLKALD FCHSQGIMHR DVKPHNVMID HELRKLRLID
WGLAEFYHPG KEYNVRVASR YFKGPELLVD LQDYDYSLDM WSLGCMFAGM IFRKEPFFYG
HDNQDQLVKI AKVLGTDELN AYLNKYQLEL DTQLEALVGR HSRKPWSKFI NADNRHLVSP
EAIDYLDKLL RYDHQDRLTA KEAMAHPYFA QVRAAESSRM RTQ


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