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Casein kinase II subunit alpha-1 (CK II) (EC 2.7.11.1) (Casein kinase alpha 1) (AtCKA1)

 CSK21_ARATH             Reviewed;         409 AA.
Q08467; B9DH00; B9DHA8; F4K3Q1; Q94F17; Q9FN14;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
16-MAY-2012, sequence version 3.
12-SEP-2018, entry version 149.
RecName: Full=Casein kinase II subunit alpha-1;
Short=CK II;
EC=2.7.11.1 {ECO:0000269|PubMed:7696877};
AltName: Full=Casein kinase alpha 1;
Short=AtCKA1 {ECO:0000303|PubMed:7678767};
Flags: Precursor;
Name=CKA1 {ECO:0000303|PubMed:7678767}; OrderedLocusNames=At5g67380;
ORFNames=K8K14.10;
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 3), FUNCTION, ACTIVITY REGULATION,
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=9501997; DOI=10.1093/dnares/4.6.401;
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III.
Sequence features of the regions of 1,191,918 bp covered by seventeen
physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
[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 4).
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=7696877; DOI=10.1105/tpc.7.1.105;
Klimczak L.J., Collinge M.A., Farini D., Giuliano G., Walker J.C.,
Cashmore A.R.;
"Reconstitution of Arabidopsis casein kinase II from recombinant
subunits and phosphorylation of transcription factor GBF1.";
Plant Cell 7:105-115(1995).
[7]
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).
[8]
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).
[9]
FUNCTION.
PubMed=19509420; DOI=10.1074/jbc.M109.007658;
Dennis M.D., Person M.D., Browning K.S.;
"Phosphorylation of plant translation initiation factors by CK2
enhances the in vitro interaction of multifactor complex components.";
J. Biol. Chem. 284:20615-20628(2009).
[10]
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).
[11]
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).
[12]
FUNCTION.
PubMed=22487192; DOI=10.1111/j.1365-313X.2012.05019.x;
Moreno-Romero J., Armengot L., Mar Marques-Bueno M., Britt A.,
Carmen Martinez M.;
"CK2-defective Arabidopsis plants exhibit enhanced double-strand break
repair rates and reduced survival after exposure to ionizing
radiation.";
Plant J. 71:627-638(2012).
-!- FUNCTION: Casein kinases are operationally defined by their
preferential utilization of acidic proteins such as caseins as
substrates. Phosphorylates casein in vitro (PubMed:7678767). The
alpha chain contains the catalytic site. The tetrameric holoenzyme
CK2, composed of two alpha and two beta subunits, phosphorylates
the transcription factor GBFl, resulting in stimulation of its DNA
binding activity (PubMed:7696877). CK2 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,
PubMed:19509420). Acts as circadian clock component that maintains
the correct period length through phosphorylation of CCA1
(PubMed:21900482). Required for the maintenance and control of
genomic stability and chromatin structure (PubMed:22487192). May
act as an ectokinase that phosphorylates several extracellular
proteins. {ECO:0000269|PubMed:19509278,
ECO:0000269|PubMed:19509420, ECO:0000269|PubMed:21330376,
ECO:0000269|PubMed:21900482, ECO:0000269|PubMed:22487192,
ECO:0000269|PubMed:7678767, ECO:0000269|PubMed:7696877}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:7696877}.
-!- ACTIVITY REGULATION: Inhibited by heparin.
{ECO:0000269|PubMed:7678767}.
-!- SUBUNIT: Heterotetramer of two catalytic alpha subunits and two
regulatory beta subunits. {ECO:0000269|PubMed:19509278,
ECO:0000269|PubMed:7696877}.
-!- INTERACTION:
P92973:CCA1; NbExp=4; IntAct=EBI-1644972, EBI-1644880;
-!- 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=4;
Name=1;
IsoId=Q08467-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q08467-2; Sequence=VSP_043759;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q08467-3; Sequence=VSP_043758;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q08467-4; Sequence=VSP_043757;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Seems to be present in all plant organs. But
seems to be less expressed than CKA2.
{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; D10246; BAA01090.1; -; mRNA.
EMBL; AB007645; BAB09023.1; -; Genomic_DNA.
EMBL; CP002688; AED98334.1; -; Genomic_DNA.
EMBL; CP002688; AED98335.1; -; Genomic_DNA.
EMBL; AF386966; AAK62411.1; -; mRNA.
EMBL; BT002141; AAN72152.1; -; mRNA.
EMBL; AK317345; BAH20017.1; -; mRNA.
EMBL; AK317458; BAH20125.1; -; mRNA.
PIR; S31098; S31098.
RefSeq; NP_001032165.1; NM_001037088.2. [Q08467-2]
RefSeq; NP_201539.2; NM_126138.4. [Q08467-1]
UniGene; At.24323; -.
ProteinModelPortal; Q08467; -.
SMR; Q08467; -.
BioGrid; 22115; 7.
IntAct; Q08467; 5.
STRING; 3702.AT5G67380.1; -.
PaxDb; Q08467; -.
PRIDE; Q08467; -.
EnsemblPlants; AT5G67380.1; AT5G67380.1; AT5G67380. [Q08467-1]
EnsemblPlants; AT5G67380.2; AT5G67380.2; AT5G67380. [Q08467-2]
GeneID; 836873; -.
Gramene; AT5G67380.1; AT5G67380.1; AT5G67380. [Q08467-1]
Gramene; AT5G67380.2; AT5G67380.2; AT5G67380. [Q08467-2]
KEGG; ath:AT5G67380; -.
Araport; AT5G67380; -.
eggNOG; KOG0668; Eukaryota.
eggNOG; ENOG410XNPP; LUCA.
HOGENOM; HOG000233021; -.
InParanoid; Q08467; -.
KO; K03097; -.
OMA; NREYWDY; -.
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:Q08467; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q08467; baseline and differential.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005956; C:protein kinase CK2 complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
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 35 {ECO:0000255}.
CHAIN 36 409 Casein kinase II subunit alpha-1.
/FTId=PRO_0000417491.
DOMAIN 110 395 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 116 124 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 227 227 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 139 139 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 223 Missing (in isoform 4).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_043757.
VAR_SEQ 1 76 Missing (in isoform 3).
{ECO:0000303|PubMed:7678767}.
/FTId=VSP_043758.
VAR_SEQ 115 147 Missing (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_043759.
CONFLICT 223 223 I -> L (in Ref. 1; BAA01090).
{ECO:0000305}.
CONFLICT 264 264 A -> V (in Ref. 1; BAA01090).
{ECO:0000305}.
CONFLICT 296 297 MI -> LL (in Ref. 1; BAA01090).
{ECO:0000305}.
CONFLICT 319 320 VL -> GV (in Ref. 1; BAA01090).
{ECO:0000305}.
CONFLICT 349 349 R -> G (in Ref. 5; BAH20017).
{ECO:0000305}.
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


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